Any feedback?
Information on EC 3.5.2.6 - beta-lactamase
for references in articles please use BRENDA:EC3.5.2.6Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.5.2.6 beta-lactamaseIUBMB Comments
A group of enzymes of varying specificity hydrolysing beta-lactams; some act more rapidly on penicillins, some more rapidly on cephalosporins. The latter were formerly listed as EC 3.5.2.8, cephalosporinase.
Specify your search results
Word Map
- 3.5.2.6
- pneumonia
- klebsiella
- enterobacteriaceae
-
esbls
- carbapenems
- aeruginosa
-
carbapenem-resistant
- ampicillin
-
esbl-producing
-
multidrug-resistant
- enterobacter
- cefotaxime
- ceftazidime
- aureus
- acinetobacter
-
surveillance
- meropenem
-
nosocomial
-
clavulanic
-
microbiological
- haemophilus
- aminoglycosides
- ciprofloxacin
- baumannii
- cloacae
- tetracycline
-
pulsed-field
-
outbreak
-
disk
- gentamicin
- integrons
-
plasmid-mediated
- colistin
- amikacin
- ceftriaxone
- fluoroquinolones
-
microdilution
-
quinolone
- citrobacter
- proteus
-
multilocus
-
carriage
- mirabilis
- gonorrhoeae
-
staphylococci
-
community-acquired
-
third-generation
- methicillin
-
penicillin-binding
-
enterococci
- drug development
- synthesis
- diagnostics
- medicine
- pharmacology
The enzyme appears in viruses and cellular organisms
Synonyms
beta-lactamase, carbapenemase, extended-spectrum beta-lactamase, ndm-1, penicillinase, tem-1, blandm-1, ges-1, blactx-m-15, kpc-2, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AmpC
AmpC beta-lactamase
AmpC beta-lactamases M19
AmpC beta-lactamases M29
AmpC beta-lactamases M37
AmpC M19
AmpC M29
AmpC M37
apo Bacillus cereus 569/H/9 enzyme
BcII
BCL-1
Beta lactamase OXA-10
-
-
-
-
beta-lactamase
beta-lactamase A-C
-
different in substrate specificity, amino acid sequence, mechanistic properties, metal ion requirement
beta-lactamase AME I
-
-
-
-
beta-lactamase I-III
beta-lactamase II
-
-
-
-
beta-lactamase OXA-10
beta-lactamase P99
beta-lactamase, class C
beta-lactamse A-D
BLA
Bla-A
Bla-B
BlaA
BlaB
BlaC
blaCMY-2
blaCTX-M-14
blaCTX-M-15
BLAIMP
-
-
-
-
blaKPC-2
BlaMab
blaNDM-7
blaSHV-14
blaTEM-1
carbapenem-hydrolyzing class A beta-lactamase
carbapenemase
Carbenicillinase
cefotaximase
-
-
-
-
ceftazidimase
-
-
-
-
cefurooximase
-
-
-
-
Cefuroximase
-
-
-
-
Cephalosporinase
CIA-1
CKO
class A beta-lactamase
class C beta-lactamase
class C P99 beta-lactamase
class D beta-lactamase
CMY-37
CTX-M-14
CTX-M-64
CTX-M-64 beta-lactamase
EC 3.5.2.8
-
-
formerly
-
ESBL
extended spectrum beta-lactamase
extended-spectrum beta-lactamase
GC1 beta-lactamase
GES-5
GIM-1
Imipenem-cefoxitin hydrolyzing enzyme
-
-
-
-
imipenemase
-
-
-
-
ImiS
IMP-1
IMP-13
IMP-18
KLUA-9
KPC-2
L1 beta-lactamase
L2 beta-lactamase
M19
M29
M37
MbetaL
MBL
metallo-beta-lactamase
metallo-beta-lactamase IMP-1
metallo-beta-lactamase L1
MIR-4 beta-lactamase
Mox-1
Mox-1 beta-lactamase
MSMEG_4455
NDM
NDM-1
neutrapen
-
-
-
-
New Delhi MBL
New Delhi metallo-beta-lactamase
New Delhi metallo-beta-lactamase-1
OXA-1
oxa-1 beta-lactamase
OXA-10
OXA-40
OXA-63
Oxacillinase
P99 beta-lactamase
penicillinase
penicillinase I, II
PSE-1
serine beta-lactamase
SFC-1
Sfh-I
SHV-1
SHV-14 beta-lactamase
SHV-2A
TEM
TEM-1
TEM-1 beta-lactamase
TEM-149
VIM-1
VIM-11
VIM-12
VIM-13
VIM-2
VIM-7
VIM-type MBL
zinc beta-lactamase
additional information
beta-lactamase
-
-
-
-
beta-lactamase I-III
-
different in molecular weight, localization, metal ion requirement
beta-lactamase I-III
-
different in molecular weight, localization, metal ion requirement
-
beta-lactamase I-III
-
different in molecular weight, localization, metal ion requirement
beta-lactamse A-D
-
A,C and D enzymes utilize a nucleophilic serine at the active center which becomes acylated by substrate, B enzymes are metalloenzymes requiring Zn2+ for activity
beta-lactamse A-D
-
A,C and D enzymes utilize a nucleophilic serine at the active center which becomes acylated by substrate, B enzymes are metalloenzymes requiring Zn2+ for activity
-
beta-lactamse A-D
-
A,C and D enzymes utilize a nucleophilic serine at the active center which becomes acylated by substrate, B enzymes are metalloenzymes requiring Zn2+ for activity
beta-lactamse A-D
-
A,C and D enzymes utilize a nucleophilic serine at the active center which becomes acylated by substrate, B enzymes are metalloenzymes requiring Zn2+ for activity
-
carbapenemase
-
-
-
-
Carbenicillinase
-
-
-
-
Cephalosporinase
-
-
-
-
metallo-beta-lactamase
-
-
-
-
metallo-beta-lactamase
-
-
New Delhi MBL
-
New Delhi metallo-beta-lactamase
-
Oxacillinase
-
-
-
-
penicillinase
-
-
-
-
penicillinase I, II
-
different in substrate specificity, pH and temperature stability, molecular weight
penicillinase I, II
Bacillus sp. (in: Bacteria) No. 170
-
different in substrate specificity, pH and temperature stability, molecular weight
-
SHV-2A
-
-
-
-
additional information
-
no metallo-beta-lactamase, MBL, in Pseudomonas aeruginosa
additional information
VIM-2 belongs to the B1 subfamily ofMBLs
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a beta-lactam + H2O = a substituted beta-amino acid
-
-
-
-
a beta-lactam + H2O = a substituted beta-amino acid
2-step mechanism: in the first step, the catalytic Ser64 attacks the carbonyl carbon of the beta-lactam ring, forming an acyl intermediate, in the second step, a deacylating water hydrolyzes the ester bond to regenerate the enzyme and the reaction product, hydrolyzed antibiotic
a beta-lactam + H2O = a substituted beta-amino acid
active site, Asp120 is important for catalysis, as well as substrate and Zn2+ binding
a beta-lactam + H2O = a substituted beta-amino acid
Arg234 is involved in catalysis
a beta-lactam + H2O = a substituted beta-amino acid
catalytic mechanism of enzyme class D, unique in comparison with classes A and C, active site structure with elements S-X-X-K, S-X-N, and K-T/S-G
a beta-lactam + H2O = a substituted beta-amino acid
enzyme-ligand interaction-structure, computational analysis, residues K67, N152, Y150, and K315 are involved in substrate binding, tetrahedral intermediate
-
a beta-lactam + H2O = a substituted beta-amino acid
Glu166 is important for catalysis, mechanism
a beta-lactam + H2O = a substituted beta-amino acid
reaction and kinetic mechanism
-
a beta-lactam + H2O = a substituted beta-amino acid
reaction mechanism, Lys70 is involved in catalysis, active site structure
-
a beta-lactam + H2O = a substituted beta-amino acid
VIM-2 catalytic Cys221, located in the Cys site, shows a high tendency to be strongly oxidized becoming a cysteinesulfonic residue, active site structure, overview
a beta-lactam + H2O = a substituted beta-amino acid
overall mechanism for beta-lactamase-inhibitor reaction, Quantum mechanical/molecular mechanical calculations and Raman spectral analysis, overview
a beta-lactam + H2O = a substituted beta-amino acid
overall mechanism for beta-lactamase-inhibitor reaction, Quantum mechanical/molecular mechanical calculations and Raman spectral analysis, overview. The protonation of the zeta-nitrogen leads to a barrierless decarboxylation of the lysine carbamate
a beta-lactam + H2O = a substituted beta-amino acid
reaction and kinetic mechanism
-
-
a beta-lactam + H2O = a substituted beta-amino acid
enzyme-ligand interaction-structure, computational analysis, residues K67, N152, Y150, and K315 are involved in substrate binding, tetrahedral intermediate
-
-
a beta-lactam + H2O = a substituted beta-amino acid
reaction and kinetic mechanism
-
-
a beta-lactam + H2O = a substituted beta-amino acid
2-step mechanism: in the first step, the catalytic Ser64 attacks the carbonyl carbon of the beta-lactam ring, forming an acyl intermediate, in the second step, a deacylating water hydrolyzes the ester bond to regenerate the enzyme and the reaction product, hydrolyzed antibiotic
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylic acid amide hydrolysis
-
-
-
-
hydrolysis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
beta-lactam hydrolase
A group of enzymes of varying specificity hydrolysing beta-lactams; some act more rapidly on penicillins, some more rapidly on cephalosporins. The latter were formerly listed as EC 3.5.2.8, cephalosporinase.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9073-60-3
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(5R,6E)-6-[(4H,6H-pyrazolo[1,5-c][1,3]thiazol-2-yl)methylidene]-4-thia-1-azabicyclo[3.2.0]hept-2-en-7-one + H2O
(2E)-2-[(2R)-2,3-dihydro-1,3-thiazol-2-yl]-3-(4H,6H-pyrazolo[1,5-c][1,3]thiazol-2-yl)prop-2-enoic acid
-
-
-
?
(5R,6Z)-6-[(1,6,7,8a-tetrahydro-5H-imidazo[2,1-b][1,3]oxazin-2-yl)methylidene]-4-thia-1-azabicyclo[3.2.0]hept-2-en-7-one + H2O
(2Z)-2-[(2R)-2,3-dihydro-1,3-thiazol-2-yl]-3-(1,6,7,8a-tetrahydro-5H-imidazo[2,1-b][1,3]oxazin-2-yl)prop-2-enoic acid
-
-
-
?
(6R,7R)-3-[(acetyloxy)methyl]-7-(formylamino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy(formylamino)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
(6R,7R)-3-[(acetyloxy)methyl]-7-(hydroxyamino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy(hydroxyamino)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
(6R,7R)-3-[(acetyloxy)methyl]-7-amino-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-amino(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
(6R,7R)-3-[(acetyloxy)methyl]-7-[formyl(hydroxy)amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[formyl(hydroxy)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
(6R,7R)-3-[(acetyloxy)methyl]-7-[hydroxy(phenylacetyl)amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[hydroxy(phenylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
(6R,7R)-3-[(acetyloxy)methyl]-8-oxo-7-[(thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
(6R,7S)-3-[(3-carboxy-4-nitro-phenyl)sulfanylmethyl]-8-oxo-7-[(2-thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo-[4.2.0]-oct-2-ene-2-carboxylic acid + H2O
?
-
-
-
?
(6R,7Z)-3-[(acetyloxy)methyl]-7-(hydroxyimino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(Z)-carboxy(hydroxyimino)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
(6R,7Z)-7-(hydroxyimino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate 5,5-dioxide + H2O
(2R)-2-[(Z)-carboxy(hydroxyimino)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylate 1,1-dioxide
-
-
-
-
?
(7R)-7-(benzyloxycarbonylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
2-[(R)-{[(benzyloxy)carbonyl]amino}(carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
(7S)-7-(benzyloxycarbonylamino)-3-methyl-8-thioxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
2-[(S)-{[(benzyloxy)carbonyl]amino}(carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
2-(2-(2-phenylacetamido)ethanethioyloxy)acetate + H2O
?
-
2-(2-(2-phenylacetamido)ethanethioyloxy)acetate is much poorer a substrate than 2-(2-(2-phenylacetamido)acetoxy)acetate
-
-
?
2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(+)-2-azabicyclo[2.2.1]hept-5-en-3-one + (-)-4-amino-cyclopent-2-enecarboxylic acid
-
-
-
-
?
2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(-)-2-azabicyclo[2.2.1]hept-5-en-3-one + (+)-4-amino-cyclopent-2-enecarboxylic acid
-
-
-
-
?
3-([3-dibenzylamino-3-oxopropanoyl]oxy)benzoic acid + H2O
?
-
-
-
?
3-([3-[benzyl(methyl)amino]-3-oxopropanoyl]oxy)benzoic acid + H2O
?
-
-
-
?
3-([N-[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]glycyl]oxy)benzoic acid + H2O
?
3-([[(2R)-3-(benzylamino)-2-methoxy-3-oxopropanoyl]oxy]methyl)benzoic acid + H2O
?
-
-
-
?
3-([[(2R)-3-(benzylamino)-2-methyl-3-oxopropanoyl]oxy]methyl)benzoic acid + H2O
?
-
-
-
?
3-([[(2S)-3-(benzylamino)-2-methoxy-3-oxopropanoyl]oxy]methyl)benzoic acid + H2O
?
-
-
-
?
3-([[(2S)-3-(benzylamino)-2-methyl-3-oxopropanoyl]oxy]methyl)benzoic acid + H2O
?
-
-
-
?
3-([[2-benzyl-3-oxo-3-(benzylamino)propanoyl]oxy]methyl)benzoic acid + H2O
?
-
-
-
?
3-[2-(2-aminothiazol-4-yl)2-(Z)-methoxyiminoacetylglycyl]oxybenzoic acid + H2O
?
-
-
-
-
?
3-[[(2S)-2-hydroxy-3-phenylpropanoyl]oxy]benzoic acid + H2O
?
-
-
-
?
4beta-methoxy-trinem + H2O
(1R,4R,7aS)-1-[(2R)-1-carboxy-2-hydroxypropyl]-4-methoxy-2,4,5,6,7,7a-hexahydro-1H-isoindole-3-carboxylic acid
6-aminopenicillanic acid + H2O
(2R,4S)-2-[amino(carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
6-beta-iodopenicillanate + H2O
(2R,4S)-2-[(R)-carboxy(iodo)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylate
-
-
-
-
?
7-(thienyl-2-acetamido)-3-[2-(4-N,N-dimethylaminophenylazo)pyridinium-methyl]-3-cephem-4-carboxylic acid + H2O
(2R)-2-[(R)-carboxy{(E)-[1-hydroxy-2-(thiophen-2-yl)ethylidene]amino}methyl]-5-{[(2E)-2-{[4-(dimethyliminio)cyclohexa-2,5-dien-1-ylidene]hydrazinylidene}pyridin-1(2H)-yl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
7-beta-formamidoyl-7-alpha-methoxycephalosporanic acid + H2O
(2R)-5-[(acetyloxy)methyl]-2-{(S)-carboxy[(E)-(hydroxymethylidene)amino]methoxymethyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
7alpha-aminocephalosporanic acid + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(S)-amino(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
7beta-aminocephalosporanic acid + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-amino(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
7beta-[(thien-2-yl)acetamido]-3-[(4-nitro-3-carboxyphenylthio)methyl]-3-cephem-4-carboxylic acid + H2O
(2R)-2-[(R)-carboxy{(E)-[1-hydroxy-2-(thiophen-2-yl)ethylidene]amino}methyl]-5-{[(3-carboxy-4-nitrophenyl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
amoxicillin + H2O
(2R,4S)-2-[(R)-{[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino}(carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
amoxicillin + H2O
(2R,4S)-2-[[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
ampicilin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
azlocillin + H2O
(2R,4S)-2-[(R)-carboxy({(2R)-2-[(2-oxoimidazolidine-1-carbonyl)amino]-2-phenylacetyl}amino)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-azaniumyl-1,3-thiazol-4-yl)-2- [[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-azaniumyl-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
benzyl cephalosporin C + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-{[(5R)-5-amino-6-(benzyloxy)-6-oxohexanoyl]amino}(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
benzyl [[(2R)-2-hydroxy-3-phenylpropanoyl]oxy]carbamate + H2O
? + hydroxamate
-
-
-
?
benzyl [[(2S)-2-hydroxy-2-phenylacetyl]oxy]carbamate + H2O
? + hydroxamate
-
-
-
?
benzyl [[(2S)-2-hydroxy-3-phenylpropanoyl]oxy]carbamate + H2O
? + hydroxamate
-
-
-
?
benzyl [[(2S)-2-hydroxy-4-phenylbutanoyl]oxy]carbamate + H2O
? + hydroxamate
-
-
-
?
benzyl [[(2S)-2-hydroxypropanoyl]oxy]carbamate + H2O
? + hydroxamate
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
biapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[(6,7-dihydro-5H-pyrazolo[1,2-a][1,2,4]triazol-4-ium-6-yl)sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylate
Bocillin-FL + H2O
?
activity analysis with Bocillin-FL, a fluorescent penicillin
-
-
?
carbenicillin + H2O
(2R,4S)-2-((R)-carboxy[2-carboxy(phenyl)acetamido]methyl)-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
cefaclor + H2O
(2R)-2-[(R)-{[(2R)-2-amino-2-phenylacetyl]amino}(carboxy)methyl]-5-chloro-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cefadroxil + H2O
(2R)-2-[((R)-([(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino)carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
AB702957
-
-
-
?
cefadroxil + H2O
(2R)-2-[(R)-{[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino}(carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefaloridine + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
cefalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cefalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cefamandole + H2O
(2R)-2-[(R)-carboxy[[(2R)-2-hydroxy-2-phenylacetyl]amino]methyl]-5-[[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cefamandole + H2O
(2R)-2-[(R)-carboxy{[(2R)-2-hydroxy-2-phenylacetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cefazolin + H2O
(2R)-2-[(R)-carboxy[2-(1H-tetrazol-1-yl)acetamido]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cefcapene + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)pent-2-enoyl]amino}(carboxy)methyl]-5-[(carbamoyloxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefdinir + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(hydroxyimino)acetyl]amino}(carboxy)methyl]-5-ethenyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
cefmetazole + H2O
(2R)-2-[(S)-carboxy{2-[(cyanomethyl)sulfanyl]acetamido}methoxymethyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoperazone + H2O
(2R)-2-[(R)-carboxy([(2S)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-(4-hydroxyphenyl)acetyl]amino)methyl]-5-([(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoperazone + H2O
(2R)-2-[(R)-carboxy{[(2S)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-(4-hydroxyphenyl)acetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cefotetan + H2O
(2R)-2-[(S)-{[4-(2-amino-1-carboxy-2-oxoethylidene)-1,3-dithietane-2-carbonyl]amino}(carboxy)methoxymethyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotiam + H2O
(2R)-2-[(R)-[2-(2-amino-1,3-thiazol-4-yl)acetamido](carboxy)methyl]-5-[({1-[2-(dimethylamino)ethyl]-1H-tetrazol-5-yl}sulfanyl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cefpirome + H2O
(2S)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino}(carboxy)methyl]-5-[(6,7-dihydro-5H-cyclopenta[b]pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
cefpodoxime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino}(carboxy)methyl]-5-(methoxymethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefprozil + H2O
(2R)-2-[(R)-{[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino}(carboxy)methyl]-5-[(1E)-prop-1-en-1-yl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefsulodin + H2O
(2R)-5-[(4-carbamoylpyridin-1-ium-1-yl)methyl]-2-[(R)-carboxy{[(2R)-2-phenyl-2-sulfoacetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
cefsulodine + H2O
(2R)-5-[(4-carbamoylpyridin-1-ium-1-yl)methyl]-2-[(R)-carboxy{[(2R)-2-phenyl-2-sulfoacetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftaxidime + H2O
(2R)-2-[(R)-([(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-([(2-carboxypropan-2-yl)oxy]imino)acetyl]amino)(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
ceftaxidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino](carboxy)methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
ceftazidime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino](carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
ceftizoxime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino}(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
ceftriaxone + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[[(2-methyl-5,6-dioxo-1,2,5,6-tetrahydro-1,2,4-triazin-3-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
ceftriaxone + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[[(6-hydroxy-2-methyl-5-oxo-2,5-dihydro-1,2,4-triazin-3-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy[[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
CENTA + H2O
(2R)-5-{[(3-carboxy-4-nitrophenyl)sulfanyl]methyl}-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cephaloglycin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-{[(2R)-2-amino-2-phenylacetyl]amino}(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
cephalosporin C + H2O
N6-[(R)-{(2R)-5-[(acetyloxy)methyl]-4-carboxy-3,6-dihydro-2H-1,3-thiazin-2-yl}(carboxy)methyl]-6-oxo-D-lysine
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cephalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cephamandol + H2O
2R)-2-[(R)-carboxy{[(2R)-2-hydroxy-2-phenylacetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephapirin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy{2-[(pyridin-4-yl)sulfanyl]acetamido}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cephradine + H2O
(2R)-2-[(R)-{[(2R)-2-amino-2-(cyclohexa-1,4-dien-1-yl)acetyl]amino}(carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
chromacef + H2O
(2S)-2-[(S)-carboxy(2-phenylacetamido)methyl]-5-[(E)-2-(4-nitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
ciclacillin + H2O
(2R,4S)-2-[(R)-[(1-aminocyclohexane-1-carbonyl)amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
clavulanic acid + H2O
(2R,4R,5Z)-2-(carboxymethyl)-5-(2-hydroxyethylidene)-1,3-oxazolidine-4-carboxylic acid
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy([[3-(2-chlorophenyl)-5-methyl-1,2-oxazol-4-yl]carbonyl]amino)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
plasmid pGEM-T-easy
-
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
CP 45899 + H2O
(2R,4S)-2-(carboxymethyl)-5,5-dimethyl-1,1-dioxo-1lambda~6~,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
doripenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4-methyl-3-(((3S,5S)-5-[(sulfamoylamino)methyl]pyrrolidin-3-yl)sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
doripenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4-methyl-3-([(3S,5S)-5-[(sulfamoylamino)methyl]pyrrolidin-3-yl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
doripenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4-methyl-3-({(3S,5S)-5-[(sulfamoylamino)methyl]pyrrolidin-3-yl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
ertapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl]sulfanyl)-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
ertapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl}sulfanyl)-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
faropenem + H2O
(2R)-2-[(1S,2R)-1-carboxy-2-hydroxypropyl]-5-[(2R)-tetrahydrofuran-2-yl]-2,3-dihydro-1,3-thiazole-4-carboxylic acid
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([2-[(iminomethyl)amino]ethyl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala + H2O
?
peptidoglycan-mimetic pentapeptide substrate
-
-
?
loracarbef + H2O
(6R)-6-[(S)-{[(2R)-2-amino-2-phenylacetyl]amino}(carboxy)methyl]-3-chloro-1,4,5,6-tetrahydropyridine-2-carboxylic acid
-
-
-
-
?
mecillinam + H2O
(2R,4S)-2-[(R)-{(E)-[(azepan-1-yl)methylidene]amino}(carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
methicillin + H2O
(2R,4S)-2-[(R)-carboxy(2,6-dimethoxybenzamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
mezlocillin + H2O
(2R,4S)-2-[(R)-carboxy{[(2R)-2-{[3-(methanesulfonyl)-2-oxoimidazolidine-1-carbonyl]amino}-2-phenylacetyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
moxalactam + H2O
(2R)-2-{(R)-carboxy[2-carboxy(4-hydroxyphenyl)acetamido]methoxymethyl}-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-oxazine-4-carboxylic acid
Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
?
artificial substrate
-
-
?
nitrocefin + H2O
(2R)-2-((R)-carboxy[2-(thiophen-2-yl)acetamido]methyl)-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
nitrocefin + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
nitrocefin + H2O
(2R)-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
nitrocefin + H2O
?
nitrocefin shows autohydrolysis at pH 7.5-9.0 in Tris buffer, while not in HEPES buffer with the same pH
-
-
?
oxacillin + H2O
(2R,4S)-2-((R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl)-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
oxacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(5-methyl-3-phenyl-1,2-oxazol-4-yl)carbonyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
panipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S)-1-ethanimidoylpyrrolidin-3-yl]sulfanyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
penicillin N + H2O
N6-{(R)-carboxy[(2R,4S)-4-carboxy-5,5-dimethyl-1,3-thiazolidin-2-yl]methyl}-6-oxo-D-lysine
-
-
-
-
?
penicillin V + H2O
(2R,4S)-2-[(R)-carboxy(2-phenoxyacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
phenoxyethylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(3-phenoxypropanamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
phenoxymethylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenoxyacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
phenoxypenicillin + H2O
(2R,4S)-2-{(R)-carboxy[(phenoxycarbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
beta-lactamase A
-
-
?
phenoxypropylpenicillin + H2O
(2R,4S)-2-[carboxy(4-phenoxybutanamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy([(2R)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-phenylacetyl]amino)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
sanfetrinem + H2O
(1R,4S,7aS)-1-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4-methoxy-2,4,5,6,7,7a-hexahydro-1H-isoindole-3-carboxylic acid
sulbactam + H2O
(2R,4S)-2-(carboxymethyl)-5,5-dimethyl-1,1-dioxo-1lambda~6~,3-thiazolidine-4-carboxylic acid
tazobactam + H2O
(2R,4S,5S)-2-(carboxymethyl)-5-methyl-1,1-dioxo-5-[(1H-1,2,3-triazol-1-yl)methyl]-1lambda6,3-thiazolidine-4-carboxylic acid
tazobactam + H2O
(2R,4S,5S)-2-(carboxymethyl)-5-methyl-1,1-dioxo-5-[(1H-1,2,3-triazol-1-yl)methyl]-1lambda~6~,3-thiazolidine-4-carboxylic acid
-
-
-
?
tebipenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[1-(4,5-dihydro-1,3-thiazol-2-yl)azetidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
very low activity, active site of BlaC-tebipenem Michaelis-Menten complex showing interactions and interatomic distances between tebipenem and active site residues, overview
-
-
?
temocillin + H2O
(2R,4S)-2-[(S)-carboxy[[carboxy(thiophen-3-yl)acetyl]amino]methoxymethyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
(6R,7R)-3-[(acetyloxy)methyl]-7-(formylamino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy(formylamino)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
(6R,7R)-3-[(acetyloxy)methyl]-7-(formylamino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy(formylamino)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
(6R,7R)-3-[(acetyloxy)methyl]-7-[hydroxy(phenylacetyl)amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[hydroxy(phenylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
(6R,7R)-3-[(acetyloxy)methyl]-7-[hydroxy(phenylacetyl)amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[hydroxy(phenylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
(6R,7R)-3-[(acetyloxy)methyl]-8-oxo-7-[(thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
(6R,7R)-3-[(acetyloxy)methyl]-8-oxo-7-[(thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
(7R)-7-(benzyloxycarbonylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
2-[(R)-{[(benzyloxy)carbonyl]amino}(carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
(7R)-7-(benzyloxycarbonylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
2-[(R)-{[(benzyloxy)carbonyl]amino}(carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
(7S)-7-(benzyloxycarbonylamino)-3-methyl-8-thioxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
2-[(S)-{[(benzyloxy)carbonyl]amino}(carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
is 1000000times poorer (kcat and kcat/Km) as a substrate than (7R)-7-(benzyloxycarbonylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
-
?
(7S)-7-(benzyloxycarbonylamino)-3-methyl-8-thioxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
2-[(S)-{[(benzyloxy)carbonyl]amino}(carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
is 1000000times poorer (kcat and kcat/Km) as a substrate than (7R)-7-(benzyloxycarbonylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
-
?
3-([N-[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]glycyl]oxy)benzoic acid + H2O
?
-
GC1 beta-lactamase
-
-
?
3-([N-[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]glycyl]oxy)benzoic acid + H2O
?
-
P99 beta-lactamase
-
-
?
4beta-methoxy-trinem + H2O
(1R,4R,7aS)-1-[(2R)-1-carboxy-2-hydroxypropyl]-4-methoxy-2,4,5,6,7,7a-hexahydro-1H-isoindole-3-carboxylic acid
-
-
-
-
?
4beta-methoxy-trinem + H2O
(1R,4R,7aS)-1-[(2R)-1-carboxy-2-hydroxypropyl]-4-methoxy-2,4,5,6,7,7a-hexahydro-1H-isoindole-3-carboxylic acid
-
-
-
-
?
6-aminopenicillanic acid + H2O
(2R,4S)-2-[amino(carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
6-aminopenicillanic acid + H2O
(2R,4S)-2-[amino(carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
6-aminopenicillanic acid + H2O
(2R,4S)-2-[amino(carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
6-aminopenicillanic acid + H2O
(2R,4S)-2-[amino(carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
6-aminopenicillanic acid + H2O
(2R,4S)-2-[amino(carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
6-aminopenicillanic acid + H2O
(2R,4S)-2-[amino(carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
7-(thienyl-2-acetamido)-3-[2-(4-N,N-dimethylaminophenylazo)pyridinium-methyl]-3-cephem-4-carboxylic acid + H2O
(2R)-2-[(R)-carboxy{(E)-[1-hydroxy-2-(thiophen-2-yl)ethylidene]amino}methyl]-5-{[(2E)-2-{[4-(dimethyliminio)cyclohexa-2,5-dien-1-ylidene]hydrazinylidene}pyridin-1(2H)-yl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
i.e. PADAC
-
-
?
7-(thienyl-2-acetamido)-3-[2-(4-N,N-dimethylaminophenylazo)pyridinium-methyl]-3-cephem-4-carboxylic acid + H2O
(2R)-2-[(R)-carboxy{(E)-[1-hydroxy-2-(thiophen-2-yl)ethylidene]amino}methyl]-5-{[(2E)-2-{[4-(dimethyliminio)cyclohexa-2,5-dien-1-ylidene]hydrazinylidene}pyridin-1(2H)-yl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
chromophoric substrate
-
-
?
7-(thienyl-2-acetamido)-3-[2-(4-N,N-dimethylaminophenylazo)pyridinium-methyl]-3-cephem-4-carboxylic acid + H2O
(2R)-2-[(R)-carboxy{(E)-[1-hydroxy-2-(thiophen-2-yl)ethylidene]amino}methyl]-5-{[(2E)-2-{[4-(dimethyliminio)cyclohexa-2,5-dien-1-ylidene]hydrazinylidene}pyridin-1(2H)-yl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
chromophoric substrate
-
-
?
7-(thienyl-2-acetamido)-3-[2-(4-N,N-dimethylaminophenylazo)pyridinium-methyl]-3-cephem-4-carboxylic acid + H2O
(2R)-2-[(R)-carboxy{(E)-[1-hydroxy-2-(thiophen-2-yl)ethylidene]amino}methyl]-5-{[(2E)-2-{[4-(dimethyliminio)cyclohexa-2,5-dien-1-ylidene]hydrazinylidene}pyridin-1(2H)-yl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
7alpha-aminocephalosporanic acid + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(S)-amino(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
7alpha-aminocephalosporanic acid + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(S)-amino(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
7beta-aminocephalosporanic acid + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-amino(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
7beta-aminocephalosporanic acid + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-amino(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
7beta-aminocephalosporanic acid + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-amino(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
7beta-aminocephalosporanic acid + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-amino(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
beta-lactamase A
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
Klebsiella pneumoniae MTCC 3384
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
Klebsiella pneumoniae NDM-7
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-{[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino}(carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-{[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino}(carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-{[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino}(carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-{[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino}(carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-{[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino}(carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-{[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino}(carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-{[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino}(carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
AB702957
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicilin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicilin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
AB702957
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
beta-lactamase III
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
beta-lactamase III
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
Bacillus sp. (in: Bacteria) No. 170
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
beta-lactamase A
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
beta-lactamases CTX-M-25
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
plasmid-encoded, pBC1e, beta-lactamase ACT-1
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
plasmid-encoded, pBC2e, beta-lactamase MIR-1
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
plasmid-encoded, pBC3e, beta-lactamase CMY-1
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
plasmid-encoded, pBC4e, beta-lactamase CMY-2
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
beta-lactamases CTX-M-26
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
Klebsiella pneumoniae MTCC 3384
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
low activity
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
plasmid pBG66
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
plasmid pGEM-T-easy
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
9% relative activity to cephaloridine
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
38% relative activity to benzylpenicillin
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
azlocillin + H2O
(2R,4S)-2-[(R)-carboxy({(2R)-2-[(2-oxoimidazolidine-1-carbonyl)amino]-2-phenylacetyl}amino)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
beta-lactamase A
-
-
?
azlocillin + H2O
(2R,4S)-2-[(R)-carboxy({(2R)-2-[(2-oxoimidazolidine-1-carbonyl)amino]-2-phenylacetyl}amino)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
azlocillin + H2O
(2R,4S)-2-[(R)-carboxy({(2R)-2-[(2-oxoimidazolidine-1-carbonyl)amino]-2-phenylacetyl}amino)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
azlocillin + H2O
(2R,4S)-2-[(R)-carboxy({(2R)-2-[(2-oxoimidazolidine-1-carbonyl)amino]-2-phenylacetyl}amino)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
beta-lactamases CTX-M-25
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
poorly active against ceftazidime and aztreonam
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
poorly active against ceftazidime and aztreonam
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
beta-lactamases CTX-M-26
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-azaniumyl-1,3-thiazol-4-yl)-2- [[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-azaniumyl-1,3-thiazol-4-yl)-2- [[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-azaniumyl-1,3-thiazol-4-yl)-2- [[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-azaniumyl-1,3-thiazol-4-yl)-2- [[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-azaniumyl-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-azaniumyl-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
benzyl cephalosporin C + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-{[(5R)-5-amino-6-(benzyloxy)-6-oxohexanoyl]amino}(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
benzyl cephalosporin C + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-{[(5R)-5-amino-6-(benzyloxy)-6-oxohexanoyl]amino}(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
benzyl cephalosporin C + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-{[(5R)-5-amino-6-(benzyloxy)-6-oxohexanoyl]amino}(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
the enzyme catalyzes the hydrolysis of the C-N bond of the beta-lactam ring
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
beta-lactamase III
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
beta-lactamase III
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
beta-lactamase A
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
beta-lactamases CTX-M-25
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
plasmid-encoded, pBC1e, beta-lactamase ACT-1
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
plasmid-encoded, pBC2e, beta-lactamase MIR-1
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
plasmid-encoded, pBC3e, beta-lactamase CMY-1
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
plasmid-encoded, pBC4e, beta-lactamase CMY-2
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
beta-lactamases CTX-M-26
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
2.8% of the activity with cephaloridine
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
3% relative activity to cephaloridine
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
670% of the activity with amoxicillin
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
100% relative activity to other substrates tested
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
best substrate
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
plasmid pGEM-T-easy
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
plasmid pQE32Chl17
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
biapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[(6,7-dihydro-5H-pyrazolo[1,2-a][1,2,4]triazol-4-ium-6-yl)sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylate
-
-
-
?
biapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[(6,7-dihydro-5H-pyrazolo[1,2-a][1,2,4]triazol-4-ium-6-yl)sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylate
-
-
-
-
?
biapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[(6,7-dihydro-5H-pyrazolo[1,2-a][1,2,4]triazol-4-ium-6-yl)sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylate
-
-
-
-
?
biapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[(6,7-dihydro-5H-pyrazolo[1,2-a][1,2,4]triazol-4-ium-6-yl)sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylate
-
-
-
-
?
biapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[(6,7-dihydro-5H-pyrazolo[1,2-a][1,2,4]triazol-4-ium-6-yl)sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylate
-
-
-
-
?
biapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[(6,7-dihydro-5H-pyrazolo[1,2-a][1,2,4]triazol-4-ium-6-yl)sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylate
-
-
-
?
biapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[(6,7-dihydro-5H-pyrazolo[1,2-a][1,2,4]triazol-4-ium-6-yl)sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylate
-
activity in resistant strains
-
-
?
biapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[(6,7-dihydro-5H-pyrazolo[1,2-a][1,2,4]triazol-4-ium-6-yl)sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylate
-
-
-
-
?
biapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[(6,7-dihydro-5H-pyrazolo[1,2-a][1,2,4]triazol-4-ium-6-yl)sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylate
-
-
-
?
carbapenem + H2O
[(2R)-2,3-dihydro-1H-pyrrol-2-yl]acetic acid
-
-
-
?
carbapenem + H2O
[(2R)-2,3-dihydro-1H-pyrrol-2-yl]acetic acid
-
-
-
?
carbapenem + H2O
[(2R)-2,3-dihydro-1H-pyrrol-2-yl]acetic acid
-
-
-
?
carbapenem + H2O
[(2R)-2,3-dihydro-1H-pyrrol-2-yl]acetic acid
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-((R)-carboxy[2-carboxy(phenyl)acetamido]methyl)-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
AB702957
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-((R)-carboxy[2-carboxy(phenyl)acetamido]methyl)-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
low hydrolysis rate
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
Bacillus sp. (in: Bacteria) No. 170
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
66% relative activity to benzylpenicillin
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
cefaclor + H2O
(2R)-2-[(R)-{[(2R)-2-amino-2-phenylacetyl]amino}(carboxy)methyl]-5-chloro-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefaclor + H2O
(2R)-2-[(R)-{[(2R)-2-amino-2-phenylacetyl]amino}(carboxy)methyl]-5-chloro-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefaclor + H2O
(2R)-2-[(R)-{[(2R)-2-amino-2-phenylacetyl]amino}(carboxy)methyl]-5-chloro-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefaclor + H2O
(2R)-2-[(R)-{[(2R)-2-amino-2-phenylacetyl]amino}(carboxy)methyl]-5-chloro-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefaloridine + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cefaloridine + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
3% of the activity with amoxicillin
-
-
?
cefaloridine + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
25% of the activity with amoxicillin
-
-
?
cefalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
3% of the activity with amoxicillin
-
-
?
cefalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
8% of the activity with amoxicillin
-
-
?
cefalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefamandole + H2O
(2R)-2-[(R)-carboxy[[(2R)-2-hydroxy-2-phenylacetyl]amino]methyl]-5-[[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefamandole + H2O
(2R)-2-[(R)-carboxy[[(2R)-2-hydroxy-2-phenylacetyl]amino]methyl]-5-[[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefamandole + H2O
(2R)-2-[(R)-carboxy{[(2R)-2-hydroxy-2-phenylacetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefamandole + H2O
(2R)-2-[(R)-carboxy{[(2R)-2-hydroxy-2-phenylacetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefamandole + H2O
(2R)-2-[(R)-carboxy{[(2R)-2-hydroxy-2-phenylacetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefamandole + H2O
(2R)-2-[(R)-carboxy{[(2R)-2-hydroxy-2-phenylacetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefamandole + H2O
(2R)-2-[(R)-carboxy{[(2R)-2-hydroxy-2-phenylacetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefamandole + H2O
(2R)-2-[(R)-carboxy{[(2R)-2-hydroxy-2-phenylacetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC1e, beta-lactamase ACT-1
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC2e, beta-lactamase MIR-1
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC3e, beta-lactamase CMY-1
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC4e, beta-lactamase CMY-2
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
plasmid pQE32Chl17
-
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[2-(1H-tetrazol-1-yl)acetamido]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[2-(1H-tetrazol-1-yl)acetamido]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[2-(1H-tetrazol-1-yl)acetamido]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
1.05% of the activity with cephaloridine
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefoperazone + H2O
(2R)-2-[(R)-carboxy{[(2S)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-(4-hydroxyphenyl)acetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoperazone + H2O
(2R)-2-[(R)-carboxy{[(2S)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-(4-hydroxyphenyl)acetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoperazone + H2O
(2R)-2-[(R)-carboxy{[(2S)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-(4-hydroxyphenyl)acetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoperazone + H2O
(2R)-2-[(R)-carboxy{[(2S)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-(4-hydroxyphenyl)acetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
11% relative activity to cephaloridine
-
-
?
cefoperazone + H2O
(2R)-2-[(R)-carboxy{[(2S)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-(4-hydroxyphenyl)acetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoperazone + H2O
(2R)-2-[(R)-carboxy{[(2S)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-(4-hydroxyphenyl)acetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoperazone + H2O
(2R)-2-[(R)-carboxy{[(2S)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-(4-hydroxyphenyl)acetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoperazone + H2O
(2R)-2-[(R)-carboxy{[(2S)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-(4-hydroxyphenyl)acetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoperazone + H2O
(2R)-2-[(R)-carboxy{[(2S)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-(4-hydroxyphenyl)acetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
conformational restriction of the extended OMEGA loop in the enzyme is probably responsible for the long-living acyl-enzyme intermediate and transition effects of cefotaxime
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
GC1 beta-lactamase
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
poor substrate for P99 beta-lactamase
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
beta-lactamases CTX-M-25
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC1e, beta-lactamase ACT-1
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC2e, beta-lactamase MIR-1
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC3e, beta-lactamase CMY-1
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC4e, beta-lactamase CMY-2
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
beta-lactamases CTX-M-26
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
Klebsiella pneumoniae MTCC 3384
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
low specific activity
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
plasmid pBC
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
plasmid pQE32Chl17
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
48% relative activity to cephaloridine
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotiam + H2O
(2R)-2-[(R)-[2-(2-amino-1,3-thiazol-4-yl)acetamido](carboxy)methyl]-5-[({1-[2-(dimethylamino)ethyl]-1H-tetrazol-5-yl}sulfanyl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotiam + H2O
(2R)-2-[(R)-[2-(2-amino-1,3-thiazol-4-yl)acetamido](carboxy)methyl]-5-[({1-[2-(dimethylamino)ethyl]-1H-tetrazol-5-yl}sulfanyl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotiam + H2O
(2R)-2-[(R)-[2-(2-amino-1,3-thiazol-4-yl)acetamido](carboxy)methyl]-5-[({1-[2-(dimethylamino)ethyl]-1H-tetrazol-5-yl}sulfanyl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC1e, beta-lactamase ACT-1
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC2e, beta-lactamase MIR-1
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC3e, beta-lactamase CMY-1
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC4e, beta-lactamase CMY-2
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
low activity
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
low activity
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
high activity
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
high activity
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefpirome + H2O
(2S)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino}(carboxy)methyl]-5-[(6,7-dihydro-5H-cyclopenta[b]pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefpirome + H2O
(2S)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino}(carboxy)methyl]-5-[(6,7-dihydro-5H-cyclopenta[b]pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefpirome + H2O
(2S)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino}(carboxy)methyl]-5-[(6,7-dihydro-5H-cyclopenta[b]pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefpirome + H2O
(2S)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino}(carboxy)methyl]-5-[(6,7-dihydro-5H-cyclopenta[b]pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cefpirome + H2O
(2S)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino}(carboxy)methyl]-5-[(6,7-dihydro-5H-cyclopenta[b]pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cefpirome + H2O
(2S)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino}(carboxy)methyl]-5-[(6,7-dihydro-5H-cyclopenta[b]pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefsulodin + H2O
(2R)-5-[(4-carbamoylpyridin-1-ium-1-yl)methyl]-2-[(R)-carboxy{[(2R)-2-phenyl-2-sulfoacetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefsulodin + H2O
(2R)-5-[(4-carbamoylpyridin-1-ium-1-yl)methyl]-2-[(R)-carboxy{[(2R)-2-phenyl-2-sulfoacetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
ceftaxidime + H2O
(2R)-2-[(R)-([(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-([(2-carboxypropan-2-yl)oxy]imino)acetyl]amino)(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftaxidime + H2O
(2R)-2-[(R)-([(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-([(2-carboxypropan-2-yl)oxy]imino)acetyl]amino)(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftaxidime + H2O
(2R)-2-[(R)-([(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-([(2-carboxypropan-2-yl)oxy]imino)acetyl]amino)(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino](carboxy)methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino](carboxy)methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino](carboxy)methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino](carboxy)methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino](carboxy)methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino](carboxy)methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino](carboxy)methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino](carboxy)methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino](carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
low activity
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino](carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
low activity
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino](carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino](carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
cephalosporin antibiotic
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
cephalosporin antibiotic
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
beta-lactamases CTX-M-25
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
poorly active against ceftazidime and aztreonam
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
30°C, pH 7.0. The affinity of MIR-4 beta-lactamase for ceftazidime is quite low
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
30°C, pH 7.0. The affinity of MIR-4 beta-lactamase for ceftazidime is quite low
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
poorly active against ceftazidime and aztreonam
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
preferred and best substrate
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
beta-lactamases CTX-M-26
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
cephalosporin antibiotic
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
cephalosporin antibiotic
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
cephalosporin antibiotic
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
cephalosporin antibiotic
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
5% of the activity with amoxicillin
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftizoxime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino}(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
ceftizoxime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino}(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
ceftriaxone + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[[(6-hydroxy-2-methyl-5-oxo-2,5-dihydro-1,2,4-triazin-3-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
ceftriaxone + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[[(6-hydroxy-2-methyl-5-oxo-2,5-dihydro-1,2,4-triazin-3-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
ceftriaxone + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[[(6-hydroxy-2-methyl-5-oxo-2,5-dihydro-1,2,4-triazin-3-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
ceftriaxone + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[[(6-hydroxy-2-methyl-5-oxo-2,5-dihydro-1,2,4-triazin-3-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
ceftriaxone + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[[(6-hydroxy-2-methyl-5-oxo-2,5-dihydro-1,2,4-triazin-3-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
ceftriaxone + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[[(6-hydroxy-2-methyl-5-oxo-2,5-dihydro-1,2,4-triazin-3-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
23% relative activity to cephaloridine
-
-
?
ceftriaxone + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[[(6-hydroxy-2-methyl-5-oxo-2,5-dihydro-1,2,4-triazin-3-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
ceftriaxone + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[[(6-hydroxy-2-methyl-5-oxo-2,5-dihydro-1,2,4-triazin-3-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
GC1 beta-lactamase
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
poor substrate for P99 beta-lactamase
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
beta-lactamases CTX-M-25
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC1e, beta-lactamase ACT-1
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC2e, beta-lactamase MIR-1
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC3e, beta-lactamase CMY-1
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC4e, beta-lactamase CMY-2
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
beta-lactamases CTX-M-26
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
93% relative activity to cephaloridine
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
2% of the activity with amoxicillin
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
CENTA + H2O
(2R)-5-{[(3-carboxy-4-nitrophenyl)sulfanyl]methyl}-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
CENTA + H2O
(2R)-5-{[(3-carboxy-4-nitrophenyl)sulfanyl]methyl}-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
CENTA + H2O
(2R)-5-{[(3-carboxy-4-nitrophenyl)sulfanyl]methyl}-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
CENTA + H2O
(2R)-5-{[(3-carboxy-4-nitrophenyl)sulfanyl]methyl}-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
CENTA + H2O
(2R)-5-{[(3-carboxy-4-nitrophenyl)sulfanyl]methyl}-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC1e, beta-lactamase ACT-1
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC2e, beta-lactamase MIR-1
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC3e, beta-lactamase CMY-1
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC4e, beta-lactamase CMY-2
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
plasmid pBG66
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephaloglycin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-{[(2R)-2-amino-2-phenylacetyl]amino}(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephaloglycin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-{[(2R)-2-amino-2-phenylacetyl]amino}(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephaloglycin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-{[(2R)-2-amino-2-phenylacetyl]amino}(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephaloglycin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-{[(2R)-2-amino-2-phenylacetyl]amino}(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephaloglycin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-{[(2R)-2-amino-2-phenylacetyl]amino}(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
beta-lactamase III
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
poor substrate, beta-lactamase I
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
poor substrate, beta-lactamase I
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
beta-lactamase III
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
poor substrate, beta-lactamase I
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
Bacillus sp. (in: Bacteria) No. 170
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
plasmid-encoded, pBC1e, beta-lactamase ACT-1
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
plasmid-encoded, pBC2e, beta-lactamase MIR-1
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
plasmid-encoded, pBC3e, beta-lactamase CMY-1
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
plasmid-encoded, pBC4e, beta-lactamase CMY-2
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
plasmid pGEM-T-easy
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
100% relative activity to other substrates tested
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
3% relative activity to benzylpenicillin
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephalosporin + H2O
?
-
the enzyme is responsible for the resistance to extended spectrum cephalosporins
-
-
?
cephalosporin + H2O
?
-
the enzyme is responsible for the resistance to extended spectrum cephalosporins
-
-
?
cephalosporin C + H2O
N6-[(R)-{(2R)-5-[(acetyloxy)methyl]-4-carboxy-3,6-dihydro-2H-1,3-thiazin-2-yl}(carboxy)methyl]-6-oxo-D-lysine
-
poor substrate, beta-lactamse I
-
-
?
cephalosporin C + H2O
N6-[(R)-{(2R)-5-[(acetyloxy)methyl]-4-carboxy-3,6-dihydro-2H-1,3-thiazin-2-yl}(carboxy)methyl]-6-oxo-D-lysine
-
poor substrate, beta-lactamse I
-
-
?
cephalosporin C + H2O
N6-[(R)-{(2R)-5-[(acetyloxy)methyl]-4-carboxy-3,6-dihydro-2H-1,3-thiazin-2-yl}(carboxy)methyl]-6-oxo-D-lysine
-
poor substrate, beta-lactamse I
-
-
?
cephalosporin C + H2O
N6-[(R)-{(2R)-5-[(acetyloxy)methyl]-4-carboxy-3,6-dihydro-2H-1,3-thiazin-2-yl}(carboxy)methyl]-6-oxo-D-lysine
-
-
-
-
?
cephalosporin C + H2O
N6-[(R)-{(2R)-5-[(acetyloxy)methyl]-4-carboxy-3,6-dihydro-2H-1,3-thiazin-2-yl}(carboxy)methyl]-6-oxo-D-lysine
-
-
-
-
?
cephalosporin C + H2O
N6-[(R)-{(2R)-5-[(acetyloxy)methyl]-4-carboxy-3,6-dihydro-2H-1,3-thiazin-2-yl}(carboxy)methyl]-6-oxo-D-lysine
-
-
-
-
?
cephalosporin C + H2O
N6-[(R)-{(2R)-5-[(acetyloxy)methyl]-4-carboxy-3,6-dihydro-2H-1,3-thiazin-2-yl}(carboxy)methyl]-6-oxo-D-lysine
-
-
-
-
?
cephalosporin C + H2O
N6-[(R)-{(2R)-5-[(acetyloxy)methyl]-4-carboxy-3,6-dihydro-2H-1,3-thiazin-2-yl}(carboxy)methyl]-6-oxo-D-lysine
-
-
-
-
?
cephalosporin C + H2O
N6-[(R)-{(2R)-5-[(acetyloxy)methyl]-4-carboxy-3,6-dihydro-2H-1,3-thiazin-2-yl}(carboxy)methyl]-6-oxo-D-lysine
-
-
-
-
?
cephalosporin C + H2O
N6-[(R)-{(2R)-5-[(acetyloxy)methyl]-4-carboxy-3,6-dihydro-2H-1,3-thiazin-2-yl}(carboxy)methyl]-6-oxo-D-lysine
-
-
-
-
?
cephalosporin C + H2O
N6-[(R)-{(2R)-5-[(acetyloxy)methyl]-4-carboxy-3,6-dihydro-2H-1,3-thiazin-2-yl}(carboxy)methyl]-6-oxo-D-lysine
-
-
-
-
?
cephalosporin C + H2O
N6-[(R)-{(2R)-5-[(acetyloxy)methyl]-4-carboxy-3,6-dihydro-2H-1,3-thiazin-2-yl}(carboxy)methyl]-6-oxo-D-lysine
-
-
-
-
?
cephalosporin C + H2O
N6-[(R)-{(2R)-5-[(acetyloxy)methyl]-4-carboxy-3,6-dihydro-2H-1,3-thiazin-2-yl}(carboxy)methyl]-6-oxo-D-lysine
-
-
-
-
?
cephalosporin C + H2O
N6-[(R)-{(2R)-5-[(acetyloxy)methyl]-4-carboxy-3,6-dihydro-2H-1,3-thiazin-2-yl}(carboxy)methyl]-6-oxo-D-lysine
-
-
-
-
?
cephalosporin C + H2O
N6-[(R)-{(2R)-5-[(acetyloxy)methyl]-4-carboxy-3,6-dihydro-2H-1,3-thiazin-2-yl}(carboxy)methyl]-6-oxo-D-lysine
-
-
-
-
?
cephalosporin C + H2O
N6-[(R)-{(2R)-5-[(acetyloxy)methyl]-4-carboxy-3,6-dihydro-2H-1,3-thiazin-2-yl}(carboxy)methyl]-6-oxo-D-lysine
-
poor substrate
-
-
?
cephalosporin C + H2O
N6-[(R)-{(2R)-5-[(acetyloxy)methyl]-4-carboxy-3,6-dihydro-2H-1,3-thiazin-2-yl}(carboxy)methyl]-6-oxo-D-lysine
-
-
-
-
?
cephalosporin C + H2O
N6-[(R)-{(2R)-5-[(acetyloxy)methyl]-4-carboxy-3,6-dihydro-2H-1,3-thiazin-2-yl}(carboxy)methyl]-6-oxo-D-lysine
-
-
-
-
?
cephalosporin C + H2O
N6-[(R)-{(2R)-5-[(acetyloxy)methyl]-4-carboxy-3,6-dihydro-2H-1,3-thiazin-2-yl}(carboxy)methyl]-6-oxo-D-lysine
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
Bacillus sp. (in: Bacteria) No. 170
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
best substrate
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
GC1 beta-lactamase
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
P99 beta-lactamase
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
best substrate
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
GC1 beta-lactamase
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
P99 beta-lactamase
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
best substrate
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
GC1 beta-lactamase
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
P99 beta-lactamase
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
beta-lactamases CTX-M-25
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC1e, beta-lactamase ACT-1
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC2e, beta-lactamase MIR-1
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC3e, beta-lactamase CMY-1
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC4e, beta-lactamase CMY-2
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
beta-lactamases CTX-M-26
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
101% of the activity with cephaloridine
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
plasmid pBC
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
plasmid pBG66
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
plasmid pGEM-T-easy
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
plasmid pQE32Chl17
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
50% relative activity to cephaloridine
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
poor substrate
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
poor substrate
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
1% relative activity to benzylpenicillin
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
binding mode of cephalothin, overview
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephapirin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy{2-[(pyridin-4-yl)sulfanyl]acetamido}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephapirin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy{2-[(pyridin-4-yl)sulfanyl]acetamido}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephradine + H2O
(2R)-2-[(R)-{[(2R)-2-amino-2-(cyclohexa-1,4-dien-1-yl)acetyl]amino}(carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephradine + H2O
(2R)-2-[(R)-{[(2R)-2-amino-2-(cyclohexa-1,4-dien-1-yl)acetyl]amino}(carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephradine + H2O
(2R)-2-[(R)-{[(2R)-2-amino-2-(cyclohexa-1,4-dien-1-yl)acetyl]amino}(carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
clavulanic acid + H2O
(2R,4R,5Z)-2-(carboxymethyl)-5-(2-hydroxyethylidene)-1,3-oxazolidine-4-carboxylic acid
-
-
-
?
clavulanic acid + H2O
(2R,4R,5Z)-2-(carboxymethyl)-5-(2-hydroxyethylidene)-1,3-oxazolidine-4-carboxylic acid
-
-
-
?
clavulanic acid + H2O
(2R,4R,5Z)-2-(carboxymethyl)-5-(2-hydroxyethylidene)-1,3-oxazolidine-4-carboxylic acid
-
-
-
-
?
clavulanic acid + H2O
(2R,4R,5Z)-2-(carboxymethyl)-5-(2-hydroxyethylidene)-1,3-oxazolidine-4-carboxylic acid
-
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
low hydrolysis rate
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
hydrolysis or inhibition, depending on pH, temperature, ratio enzyme/cloaxcillin
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
hydrolysis or inhibition, depending on pH, temperature, ratio enzyme/cloaxcillin
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
Bacillus sp. (in: Bacteria) No. 170
-
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
specific for
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
poor substrate
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
38% relative activity to benzylpenicillin
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
doripenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4-methyl-3-([(3S,5S)-5-[(sulfamoylamino)methyl]pyrrolidin-3-yl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
doripenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4-methyl-3-([(3S,5S)-5-[(sulfamoylamino)methyl]pyrrolidin-3-yl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
doripenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4-methyl-3-([(3S,5S)-5-[(sulfamoylamino)methyl]pyrrolidin-3-yl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
very low activity
-
-
?
doripenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4-methyl-3-([(3S,5S)-5-[(sulfamoylamino)methyl]pyrrolidin-3-yl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
very low activity
-
-
?
doripenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4-methyl-3-([(3S,5S)-5-[(sulfamoylamino)methyl]pyrrolidin-3-yl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
doripenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4-methyl-3-([(3S,5S)-5-[(sulfamoylamino)methyl]pyrrolidin-3-yl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
ertapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl]sulfanyl)-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
ertapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl]sulfanyl)-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
ertapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl]sulfanyl)-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
ertapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl]sulfanyl)-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
ertapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl]sulfanyl)-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
very low activity
-
-
?
ertapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl]sulfanyl)-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
very low activity
-
-
?
ertapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl]sulfanyl)-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
ertapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl]sulfanyl)-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
ertapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl]sulfanyl)-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
ertapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl]sulfanyl)-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
ertapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl}sulfanyl)-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
ertapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl}sulfanyl)-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
faropenem + H2O
(2R)-2-[(1S,2R)-1-carboxy-2-hydroxypropyl]-5-[(2R)-tetrahydrofuran-2-yl]-2,3-dihydro-1,3-thiazole-4-carboxylic acid
-
-
-
?
faropenem + H2O
(2R)-2-[(1S,2R)-1-carboxy-2-hydroxypropyl]-5-[(2R)-tetrahydrofuran-2-yl]-2,3-dihydro-1,3-thiazole-4-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
plasmid pBC
-
-
-
-
?
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([2-[(iminomethyl)amino]ethyl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
the enzyme catalyzes the hydrolysis of the C-N bond of the beta-lactam ring
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([2-[(iminomethyl)amino]ethyl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([2-[(iminomethyl)amino]ethyl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([2-[(iminomethyl)amino]ethyl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([2-[(iminomethyl)amino]ethyl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([2-[(iminomethyl)amino]ethyl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([2-[(iminomethyl)amino]ethyl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([2-[(iminomethyl)amino]ethyl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([2-[(iminomethyl)amino]ethyl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([2-[(iminomethyl)amino]ethyl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([2-[(iminomethyl)amino]ethyl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
beta-lactam antibiotic
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
beta-lactam antibiotic
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
plasmid-encoded, pBC1e, beta-lactamase ACT-1
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
plasmid-encoded, pBC2e, beta-lactamase MIR-1
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
plasmid-encoded, pBC3e, beta-lactamase CMY-1
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
plasmid-encoded, pBC4e, beta-lactamase CMY-2
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
moderate rate of hydrolysis
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
beta-lactam antibiotic
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
moderate rate of hydrolysis
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
activity in resistant strains
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
the enzyme shows carbapenemase activity, e.g. against the carbapenem antibiotics meropenem and imipenem used in treatment of Pseudomonas aeruginosa infection, and contributes to resistance to anti-pseudomonal agents, overview
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
beta-lactam antibiotic
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
high activity of IMP-10
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
beta-lactam antibiotic
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
beta-lactam antibiotic
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
5% of the activity with amoxicillin
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
as active as amoxicillin
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
very low activity
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
low activity
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
very slow substrate and low activity
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
very slow substrate and low activity
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
very low activity
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
meropenem enzyme-bound structure with Zn2+, PDB ID 5AXO
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
activity in resistant strains
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
the enzyme shows carbapenemase activity, e.g. against the carbapenem antibiotics meropenem and imipenem used in treatment of Pseudomonas aeruginosa infection, and contributes to resistance to anti-pseudomonal agents, overview
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
230% of the activity with amoxicillin
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
methicillin + H2O
(2R,4S)-2-[(R)-carboxy(2,6-dimethoxybenzamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
methicillin + H2O
(2R,4S)-2-[(R)-carboxy(2,6-dimethoxybenzamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
ir
methicillin + H2O
(2R,4S)-2-[(R)-carboxy(2,6-dimethoxybenzamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
beta-lactamase III
-
-
?
methicillin + H2O
(2R,4S)-2-[(R)-carboxy(2,6-dimethoxybenzamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
low hydrolysis rate
-
-
?
methicillin + H2O
(2R,4S)-2-[(R)-carboxy(2,6-dimethoxybenzamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
methicillin + H2O
(2R,4S)-2-[(R)-carboxy(2,6-dimethoxybenzamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
beta-lactamase III
-
-
?
methicillin + H2O
(2R,4S)-2-[(R)-carboxy(2,6-dimethoxybenzamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
methicillin + H2O
(2R,4S)-2-[(R)-carboxy(2,6-dimethoxybenzamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
methicillin + H2O
(2R,4S)-2-[(R)-carboxy(2,6-dimethoxybenzamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
ir
methicillin + H2O
(2R,4S)-2-[(R)-carboxy(2,6-dimethoxybenzamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
methicillin + H2O
(2R,4S)-2-[(R)-carboxy(2,6-dimethoxybenzamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
methicillin + H2O
(2R,4S)-2-[(R)-carboxy(2,6-dimethoxybenzamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
methicillin + H2O
(2R,4S)-2-[(R)-carboxy(2,6-dimethoxybenzamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
methicillin + H2O
(2R,4S)-2-[(R)-carboxy(2,6-dimethoxybenzamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
beta-lactamase III
-
-
?
methicillin + H2O
(2R,4S)-2-[(R)-carboxy(2,6-dimethoxybenzamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
beta-lactamase III
-
-
?
methicillin + H2O
(2R,4S)-2-[(R)-carboxy(2,6-dimethoxybenzamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
methicillin + H2O
(2R,4S)-2-[(R)-carboxy(2,6-dimethoxybenzamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
methicillin + H2O
(2R,4S)-2-[(R)-carboxy(2,6-dimethoxybenzamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
poor substrate
-
-
?
methicillin + H2O
(2R,4S)-2-[(R)-carboxy(2,6-dimethoxybenzamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
methicillin + H2O
(2R,4S)-2-[(R)-carboxy(2,6-dimethoxybenzamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
73% relative activity
-
-
?
methicillin + H2O
(2R,4S)-2-[(R)-carboxy(2,6-dimethoxybenzamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
mezlocillin + H2O
(2R,4S)-2-[(R)-carboxy{[(2R)-2-{[3-(methanesulfonyl)-2-oxoimidazolidine-1-carbonyl]amino}-2-phenylacetyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
mezlocillin + H2O
(2R,4S)-2-[(R)-carboxy{[(2R)-2-{[3-(methanesulfonyl)-2-oxoimidazolidine-1-carbonyl]amino}-2-phenylacetyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
moxalactam + H2O
(2R)-2-{(R)-carboxy[2-carboxy(4-hydroxyphenyl)acetamido]methoxymethyl}-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-oxazine-4-carboxylic acid
-
-
-
?
moxalactam + H2O
(2R)-2-{(R)-carboxy[2-carboxy(4-hydroxyphenyl)acetamido]methoxymethyl}-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-oxazine-4-carboxylic acid
-
-
-
?
moxalactam + H2O
(2R)-2-{(R)-carboxy[2-carboxy(4-hydroxyphenyl)acetamido]methoxymethyl}-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-oxazine-4-carboxylic acid
-
-
-
?
moxalactam + H2O
(2R)-2-{(R)-carboxy[2-carboxy(4-hydroxyphenyl)acetamido]methoxymethyl}-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-oxazine-4-carboxylic acid
-
-
-
-
?
moxalactam + H2O
(2R)-2-{(R)-carboxy[2-carboxy(4-hydroxyphenyl)acetamido]methoxymethyl}-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-oxazine-4-carboxylic acid
-
-
-
-
?
moxalactam + H2O
(2R)-2-{(R)-carboxy[2-carboxy(4-hydroxyphenyl)acetamido]methoxymethyl}-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-oxazine-4-carboxylic acid
-
-
-
?
moxalactam + H2O
(2R)-2-{(R)-carboxy[2-carboxy(4-hydroxyphenyl)acetamido]methoxymethyl}-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-oxazine-4-carboxylic acid
-
-
-
?
moxalactam + H2O
(2R)-2-{(R)-carboxy[2-carboxy(4-hydroxyphenyl)acetamido]methoxymethyl}-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-oxazine-4-carboxylic acid
-
-
-
?
moxalactam + H2O
(2R)-2-{(R)-carboxy[2-carboxy(4-hydroxyphenyl)acetamido]methoxymethyl}-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-oxazine-4-carboxylic acid
-
-
-
?
moxalactam + H2O
(2R)-2-{(R)-carboxy[2-carboxy(4-hydroxyphenyl)acetamido]methoxymethyl}-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-oxazine-4-carboxylic acid
230% of the activity with amoxicillin
-
-
?
moxalactam + H2O
(2R)-2-{(R)-carboxy[2-carboxy(4-hydroxyphenyl)acetamido]methoxymethyl}-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-oxazine-4-carboxylic acid
-
-
-
-
?
moxalactam + H2O
(2R)-2-{(R)-carboxy[2-carboxy(4-hydroxyphenyl)acetamido]methoxymethyl}-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-oxazine-4-carboxylic acid
-
-
-
-
?
N-(phenylacetyl)thioglycylglycolic acid + H2O
phenylacetylglycine + glycolate
-
-
-
-
?
N-(phenylacetyl)thioglycylglycolic acid + H2O
phenylacetylglycine + glycolate
-
-
-
-
?
nitrocefin + H2O
(2R)-2-((R)-carboxy[2-(thiophen-2-yl)acetamido]methyl)-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-((R)-carboxy[2-(thiophen-2-yl)acetamido]methyl)-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
plasmid pBC
-
-
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
plasmid pGEM-T-easy
-
-
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
IMP-1 does not stabilize a nitrocefin-derived reaction intermediate, rather, the enzyme follows a simple Michaelis mechanism to hydrolyze nitrocefin
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
high activity
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
ir
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC1e, beta-lactamase ACT-1
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC2e, beta-lactamase MIR-1
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC3e, beta-lactamase CMY-1
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
plasmid-encoded, pBC4e, beta-lactamase CMY-2
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
oxacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(5-methyl-3-phenyl-1,2-oxazol-4-yl)carbonyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
oxacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(5-methyl-3-phenyl-1,2-oxazol-4-yl)carbonyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
oxacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(5-methyl-3-phenyl-1,2-oxazol-4-yl)carbonyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
oxacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(5-methyl-3-phenyl-1,2-oxazol-4-yl)carbonyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
plasmid pGEM-T-easy
-
-
-
-
?
oxacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(5-methyl-3-phenyl-1,2-oxazol-4-yl)carbonyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
oxacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(5-methyl-3-phenyl-1,2-oxazol-4-yl)carbonyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
specific for
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
plasmid-encoded, pBC1e, beta-lactamase ACT-1
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
plasmid-encoded, pBC2e, beta-lactamase MIR-1
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
plasmid-encoded, pBC3e, beta-lactamase CMY-1
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
plasmid-encoded, pBC4e, beta-lactamase CMY-2
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
panipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S)-1-ethanimidoylpyrrolidin-3-yl]sulfanyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
panipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S)-1-ethanimidoylpyrrolidin-3-yl]sulfanyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
AB702957
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
efficient hydrolysis
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
efficient hydrolysis
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
Klebsiella pneumoniae MTCC 3384
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
Klebsiella pneumoniae NDM-7
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
plasmid pBG66
-
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
phenoxymethylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenoxyacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
phenoxymethylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenoxyacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
phenoxymethylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenoxyacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
phenoxymethylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenoxyacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
phenoxymethylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenoxyacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
phenoxymethylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenoxyacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
phenoxymethylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenoxyacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
phenoxymethylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenoxyacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy([(2R)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-phenylacetyl]amino)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy([(2R)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-phenylacetyl]amino)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy([(2R)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-phenylacetyl]amino)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy([(2R)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-phenylacetyl]amino)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
plasmid pBC
-
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
160% of the activity with amoxicillin
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
sanfetrinem + H2O
(1R,4S,7aS)-1-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4-methoxy-2,4,5,6,7,7a-hexahydro-1H-isoindole-3-carboxylic acid
-
-
-
-
?
sanfetrinem + H2O
(1R,4S,7aS)-1-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4-methoxy-2,4,5,6,7,7a-hexahydro-1H-isoindole-3-carboxylic acid
-
-
-
-
?
sulbactam + H2O
(2R,4S)-2-(carboxymethyl)-5,5-dimethyl-1,1-dioxo-1lambda~6~,3-thiazolidine-4-carboxylic acid
-
-
-
?
sulbactam + H2O
(2R,4S)-2-(carboxymethyl)-5,5-dimethyl-1,1-dioxo-1lambda~6~,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
sulbactam + H2O
(2R,4S)-2-(carboxymethyl)-5,5-dimethyl-1,1-dioxo-1lambda~6~,3-thiazolidine-4-carboxylic acid
-
-
-
?
sulbactam + H2O
(2R,4S)-2-(carboxymethyl)-5,5-dimethyl-1,1-dioxo-1lambda~6~,3-thiazolidine-4-carboxylic acid
-
-
-
?
tazobactam + H2O
(2R,4S,5S)-2-(carboxymethyl)-5-methyl-1,1-dioxo-5-[(1H-1,2,3-triazol-1-yl)methyl]-1lambda6,3-thiazolidine-4-carboxylic acid
-
mutant enzyme S130G, hydrolysis of the inhibitor molecule acylated by the mutant enzyme
-
-
?
tazobactam + H2O
(2R,4S,5S)-2-(carboxymethyl)-5-methyl-1,1-dioxo-5-[(1H-1,2,3-triazol-1-yl)methyl]-1lambda6,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
beta-lactamases CTX-M-25
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
beta-lactamases CTX-M-26
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
130% of the activity with amoxicillin
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
additional information
?
-
no hydrolysis of oxacillin, ceftazidime, cefotaxime, and cefoxitin
-
-
?
additional information
?
-
-
no hydrolysis of oxacillin, ceftazidime, cefotaxime, and cefoxitin
-
-
?
additional information
?
-
AB702957
enzyme MacQ has the bifunctional capacity to degrade both N-acylhomoserine lactone (N-acylhomoserine lactone acylase, EC 3.5.1.97) and beta-lactam antibiotics by deacylation activity. MacQ is able to inactivate a variety of beta-lactams, including penicillin derivatives (penicillin G, ampicillin, amoxicillin, and carbenicillin) and cephalosporin derivatives (cephalexin and cefadroxil)
-
-
-
additional information
?
-
no induction by imipenem and cefoxitin
-
-
?
additional information
?
-
-
no induction by imipenem and cefoxitin
-
-
?
additional information
?
-
no hydrolysis of imipenem and aztreonam is detected
-
-
?
additional information
?
-
-
no hydrolysis of imipenem and aztreonam is detected
-
-
?
additional information
?
-
-
negligible hydrolysis of the cephalosporins cephaloridine, nitrocefin, cefoxitin, aztreonam
-
-
?
additional information
?
-
-
negligible hydrolysis of the cephalosporins cephaloridine, nitrocefin, cefoxitin, aztreonam
-
-
?
additional information
?
-
readily hydrolyzes carbapenems
-
-
?
additional information
?
-
the enzyme hydrolyses all beta-lactam antibiotics tested, except for the monobactam aztreonam and the penicillin piperacillin
-
-
?
additional information
?
-
no activity with piperacillin and aztreonam
-
-
?
additional information
?
-
does not interact with oxyimino-cephalosporins, imipenem, or aztreonam
-
-
?
additional information
?
-
does not interact with oxyimino-cephalosporins, imipenem, or aztreonam
-
-
?
additional information
?
-
-
does not interact with oxyimino-cephalosporins, imipenem, or aztreonam
-
-
?
additional information
?
-
no hydrolysis of ceftazidime, cefepime, moxalactam, tazobactam, and aztreonam
-
-
?
additional information
?
-
-
no hydrolysis of ceftazidime, cefepime, moxalactam, tazobactam, and aztreonam
-
-
?
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime is a poor substrate
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime is a poor substrate
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime is a poor substrate
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview. Cefepime is a poor substrate
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime and cefotaxime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime and cefotaxime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime and cefotaxime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime and cefotaxime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime and cefotaxime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime and cefotaxime are poor substrates
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview. Cefepime and cefotaxime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime is a poor substrate
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime is a poor substrate
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime is a poor substrate
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime is a poor substrate
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime is a poor substrate
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime is a poor substrate
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview. Cefepime is a poor substrate
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
-
cephalosporins bearing oximino side chains are resistant to hydrolysis by class C enzymes, the side chain is necessary but not sufficent for production of resistance, it must be combinated with the dihydrothiazine ring
-
-
?
additional information
?
-
-
no activity with the thiono analogue of N-(phenylacetyl)thioglycylglycolic acid
-
-
?
additional information
?
-
-
3-(2-(N-methyl-2-phenylacetamido)acetoxy)benzoate is not a substrate
-
-
?
additional information
?
-
O-(1-carboxy-1-alkyloxycarbonyl) hydroxamates are found to spontaneously decarboxylate in aqueous neutral buffer to form O-(2-hydroxyalkylcarbonyl) hydroxamates.While the former molecules do not react rapidly with serine beta-lactamases, the latter are quite good substrates of representative class A and C, but not D enzymes. The enzymes catalyze hydrolysis of these compounds to a mixture of the R-hydroxy acid and hydroxamate. Although both D- and L-R-hydroxy acid derivatives were substrates, the former are preferred
-
-
?
additional information
?
-
substituted aryl malonamates are substrates of class A and class C beta-lactamases, and of soluble DD-peptidases
-
-
?
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
-
cephalosporins bearing oximino side chains are resistant to hydrolysis by class C enzymes, the side chain is necessary but not sufficent for production of resistance, it must be combinated with the dihydrothiazine ring
-
-
?
additional information
?
-
-
cephalosporins bearing oximino side chains are resistant to hydrolysis by class C enzymes, the side chain is necessary but not sufficent for production of resistance, it must be combinated with the dihydrothiazine ring
-
-
?
additional information
?
-
-
no activity with the thiono analogue of N-(phenylacetyl)thioglycylglycolic acid
-
-
?
additional information
?
-
-
3-(2-(N-methyl-2-phenylacetamido)acetoxy)benzoate is not a substrate
-
-
?
additional information
?
-
-
the substituted lactamases Cu-L1 and ZnNi-L1 hydrolyze cephalosporins and carbapenems, but not penicillins, suggesting that the Zn2+-site modulates substrate preference in mbetal L1
-
-
?
additional information
?
-
-
enzyme FOX-4 possesses broad substrate specificity for beta-lactam hydrolysis, especially cephamycins
-
-
?
additional information
?
-
-
substrate specificity in vivo with different enzymes genotypes, overview
-
-
-
additional information
?
-
ticarcillin and cefuroxime are weakly recognized by the enzyme, while cefotaxime, ceftazidime, and cefepime are not hydrolyzed
-
-
?
additional information
?
-
-
ticarcillin and cefuroxime are weakly recognized by the enzyme, while cefotaxime, ceftazidime, and cefepime are not hydrolyzed
-
-
?
additional information
?
-
-
no hydrolysis of aztreonam, meropenem, ceftazidime, cefoxitin, and cefotaxime
-
-
?
additional information
?
-
the enzyme hydrolyzes penicillins, cephalothin, and the expanded-spectrum cephalosporins cefepime and moxalactam
-
-
?
additional information
?
-
antibiotic sensitivity of recombinant wild-type and mutant blaSHV-14, overview
-
-
-
additional information
?
-
-
antibiotic sensitivity of recombinant wild-type and mutant blaSHV-14, overview
-
-
-
additional information
?
-
resistance to antibiotics of recombinant His-tagged wild-type and mutant enzymes expressed in Escherichia coli strain CS109, overview
-
-
-
additional information
?
-
in vitro activity of 13 antimicrobial agents against 19 multidrug-resistant Klebsiella pneumoniae amikacin resistance isolates, overview
-
-
-
additional information
?
-
in vitro activity of 13 antimicrobial agents against 19 multidrug-resistant Klebsiella pneumoniae amikacin resistance isolates, overview
-
-
-
additional information
?
-
in vitro activity of 13 antimicrobial agents against 19 multidrug-resistant Klebsiella pneumoniae amikacin resistance isolates, overview
-
-
-
additional information
?
-
in vitro activity of 13 antimicrobial agents against 19 multidrug-resistant Klebsiella pneumoniae amikacin resistance isolates, overview
-
-
-
additional information
?
-
in vitro activity of 13 antimicrobial agents against 19 multidrug-resistant Klebsiella pneumoniae amikacin resistance isolates, overview
-
-
-
additional information
?
-
-
in vitro activity of 13 antimicrobial agents against 19 multidrug-resistant Klebsiella pneumoniae amikacin resistance isolates, overview
-
-
-
additional information
?
-
purified enzyme NDM-7 exhibits broad-spectrum enzyme activities with low Km and high kcat values hydrolysing all beta-lactam substrates tested
-
-
-
additional information
?
-
-
no hydrolysis of aztreonam, meropenem, ceftazidime, cefoxitin, and cefotaxime
-
-
?
additional information
?
-
Klebsiella pneumoniae MTCC 3384
antibiotic sensitivity of recombinant wild-type and mutant blaSHV-14, overview
-
-
-
additional information
?
-
Klebsiella pneumoniae NDM-7
resistance to antibiotics of recombinant His-tagged wild-type and mutant enzymes expressed in Escherichia coli strain CS109, overview
-
-
-
additional information
?
-
Klebsiella pneumoniae NDM-7
purified enzyme NDM-7 exhibits broad-spectrum enzyme activities with low Km and high kcat values hydrolysing all beta-lactam substrates tested
-
-
-
additional information
?
-
the enzyme hydrolyzes penicillins, cephalothin, and the expanded-spectrum cephalosporins cefepime and moxalactam
-
-
?
additional information
?
-
-
dicloxacillin, cefoxitin and imipenem behave as poor substrates
-
-
?
additional information
?
-
-
dicloxacillin, cefoxitin and imipenem behave as poor substrates
-
-
?
additional information
?
-
expression of the ampC gene of HLHK5 is regulated by its ampR gene, which acts as a repressor
-
-
?
additional information
?
-
-
expression of the ampC gene of HLHK5 is regulated by its ampR gene, which acts as a repressor
-
-
?
additional information
?
-
the carbapenems doripenem and ertapenem are slow substrates that acylate the enzyme but are only slowly deacylated and can therefore act also as potent inhibitors of BlaC
-
-
?
additional information
?
-
-
the carbapenems doripenem and ertapenem are slow substrates that acylate the enzyme but are only slowly deacylated and can therefore act also as potent inhibitors of BlaC
-
-
?
additional information
?
-
during the acylation reaction of carbapenems catalyzed by BlaC, the ring opening of the beta-lactam yields an initial DELTA2-pyrroline ring, which subsequently isomerizes to a DELTA1-pyrroline ring with stereospecific protonation at C3 to generate the final, stable acylated adduct
-
-
?
additional information
?
-
-
during the acylation reaction of carbapenems catalyzed by BlaC, the ring opening of the beta-lactam yields an initial DELTA2-pyrroline ring, which subsequently isomerizes to a DELTA1-pyrroline ring with stereospecific protonation at C3 to generate the final, stable acylated adduct
-
-
?
additional information
?
-
enzyme BlaC catalyzes the opening of the beta-lactam ring via nucleophilic attack by an active site serine residue (Ser70) to generate the acyl enzyme followed by hydrolysis of the ester bond to generate the inactive ring-opened product. Enzyme BlaC has an extremely broad spectrum of activity against penicillins and cephalosporins but weak activity against newer carbapenems. Carbapenems such as meropenem, doripenem, and ertapenem react with the enzyme to form enzyme-drug covalent complexes that are hydrolyzed extremely slowly
-
-
?
additional information
?
-
the carbapenems doripenem and ertapenem are slow substrates that acylate the enzyme but are only slowly deacylated and can therefore act also as potent inhibitors of BlaC
-
-
?
additional information
?
-
during the acylation reaction of carbapenems catalyzed by BlaC, the ring opening of the beta-lactam yields an initial DELTA2-pyrroline ring, which subsequently isomerizes to a DELTA1-pyrroline ring with stereospecific protonation at C3 to generate the final, stable acylated adduct
-
-
?
additional information
?
-
enzyme BlaC catalyzes the opening of the beta-lactam ring via nucleophilic attack by an active site serine residue (Ser70) to generate the acyl enzyme followed by hydrolysis of the ester bond to generate the inactive ring-opened product. Enzyme BlaC has an extremely broad spectrum of activity against penicillins and cephalosporins but weak activity against newer carbapenems. Carbapenems such as meropenem, doripenem, and ertapenem react with the enzyme to form enzyme-drug covalent complexes that are hydrolyzed extremely slowly
-
-
?
additional information
?
-
does not use ceftazidime as a substrate
-
-
?
additional information
?
-
-
does not use ceftazidime as a substrate
-
-
?
additional information
?
-
no activity with aztreonam and imipenem
-
-
-
additional information
?
-
-
no activity with aztreonam and imipenem
-
-
-
additional information
?
-
no activity with aztreonam and imipenem
-
-
-
additional information
?
-
no activity with aztreonam and imipenem
-
-
-
additional information
?
-
-
a VIM-2 enzyme inserted in integron In58, in an isolate from a female cystic fibrosis patient, is resistant to all antimicrobial agents tested except colistin, overview
-
-
?
additional information
?
-
-
antibiotic resistance rates and mechanisms of beta-lactam and aminoglycoside resistance, e.g. against ticarcillin, among human isolates of Pseudomonas aeruginosa isolated in the extra-hospital setting, MIC values of diverse beta-lactam antibiotics, resistance mechanisms, overview
-
-
?
additional information
?
-
-
carbapenem resistance screening of diverse clinical strains by a 2-mercaptopropionic acid inhibition test method, determination of MIC values, overview
-
-
?
additional information
?
-
-
determination of MIC values of SHV-1 for several antibiotics, overview
-
-
?
additional information
?
-
-
genetic variants of beta-lactamases cause resistance to antibiotics cefepime and/or ceftazidime, overview
-
-
?
additional information
?
-
-
occurrence and mechanisms of amikacin resistance and its association with beta-lactamases in Pseudomonas aeruginosa, a Korean nationwide study, gene blaOXA-10 is involved in amikain resistance, overview
-
-
?
additional information
?
-
-
production of beta-lactamases is the main mechanism of resistance to beta-lactams in Gram-negative bacteria, the phenomenon of continuing suppression of bacterial growth after removal of beta-lactamase inhibitors is termed post-beta-lactamase inhibitor effect, PLIE. EDTA combined with carbapenems produces a significant PLIE on VIM-MBL-positive Pseudomonas aeruginosa strains
-
-
?
additional information
?
-
-
screening for beta-lactamase genes in clincal isolates using Etest MBL screening test, The blaVIM-13-producing isolate shows resistance to all beta-lactams, except aztreonam, gentamicin, tobramycin, and ciprofloxacin, VIM-13 confers slightly higher levels of resistance to piperacillin and lower levels of resistance to ceftazidime and cefepime than VIM-1, MIC values, overview
-
-
?
additional information
?
-
screening for beta-lactamase genes in clincal isolates using Etest MBL screening test, The blaVIM-13-producing isolate shows resistance to all beta-lactams, except aztreonam, gentamicin, tobramycin, and ciprofloxacin, VIM-13 confers slightly higher levels of resistance to piperacillin and lower levels of resistance to ceftazidime and cefepime than VIM-1, MIC values, overview
-
-
?
additional information
?
-
screening for beta-lactamase genes in clincal isolates using Etest MBL screening test, The blaVIM-13-producing isolate shows resistance to all beta-lactams, except aztreonam, gentamicin, tobramycin, and ciprofloxacin, VIM-13 confers slightly higher levels of resistance to piperacillin and lower levels of resistance to ceftazidime and cefepime than VIM-1, MIC values, overview
-
-
?
additional information
?
-
-
screening for strains expressing IMP-15 beta-lactamases in clinical human isolates from a Mexican tertiary-care hospital, overview
-
-
?
additional information
?
-
screening for strains expressing IMP-15 beta-lactamases in clinical human isolates from a Mexican tertiary-care hospital, overview
-
-
?
additional information
?
-
screening for strains expressing IMP-15 beta-lactamases in clinical human isolates from a Mexican tertiary-care hospital, overview
-
-
?
additional information
?
-
-
screening for strains expressing VIM-1, and other beta-lactamases in clinical human isolates from a Mexican tertiary-care hospital, overview
-
-
?
additional information
?
-
screening for strains expressing VIM-1, and other beta-lactamases in clinical human isolates from a Mexican tertiary-care hospital, overview
-
-
?
additional information
?
-
screening for strains expressing VIM-1, and other beta-lactamases in clinical human isolates from a Mexican tertiary-care hospital, overview
-
-
?
additional information
?
-
susceptibility and enzymatic activity of metallo-beta-lactamases in Pseudomonas aeruginosa-producing metallo-beta-lactamases, overview
-
-
?
additional information
?
-
-
susceptibility and enzymatic activity of metallo-beta-lactamases in Pseudomonas aeruginosa-producing metallo-beta-lactamases, overview
-
-
?
additional information
?
-
the IMP-9 variant of metallo-beta-lactamases show a broad spectrum antibiotic resistance resulting in an out break in 2005-2007 in China, multidrug-resistant profile of IMP-9 MBL variants, overview
-
-
?
additional information
?
-
-
the IMP-9 variant of metallo-beta-lactamases show a broad spectrum antibiotic resistance resulting in an out break in 2005-2007 in China, multidrug-resistant profile of IMP-9 MBL variants, overview
-
-
?
additional information
?
-
the Pseudomonas aeruginosa strain that contains the mobile metallo-beta-lactamase gene, designated blaVIM-7, located on a plasmid (p07-406), is resistant to all tested antimicrobials except polymyxin B causing an outbreak of infections in Houston, USA, overview
-
-
?
additional information
?
-
-
the Pseudomonas aeruginosa strain that contains the mobile metallo-beta-lactamase gene, designated blaVIM-7, located on a plasmid (p07-406), is resistant to all tested antimicrobials except polymyxin B causing an outbreak of infections in Houston, USA, overview
-
-
?
additional information
?
-
-
screening for MBL and ESBL variants using different test methods, overview
-
-
?
additional information
?
-
VIM-2 has a broad substrate hydrolysis range, which includes penicillins, cephalosporins, cephamycins, oxacephamycins and carbapenems but not monobactams. Amongst the carbapenems, VIM-2 better hydrolyses meropenem than imipenem
-
-
?
additional information
?
-
-
VIM-2 has a broad substrate hydrolysis range, which includes penicillins, cephalosporins, cephamycins, oxacephamycins and carbapenems but not monobactams. Amongst the carbapenems, VIM-2 better hydrolyses meropenem than imipenem
-
-
?
additional information
?
-
a single amino acid difference at position 170 of the GES-1, GES-2, and GES-5 enzymes is responsible for the expansion of their substrate profile to include carbapenem antibiotics. The catalytic efficiency of the enzymes with carbapenems meropenem, ertapenem, and doripenem progressively increases 100fold from GES-1 to -5, mainly due to an increase in the rate of acylation. While acylation is rate limiting for GES-1 and GES-2 for all three carbapenems, acylation and deacylation are indistinguishable for GES-5. Only the core structure of the antibiotic interacts with the active site of the GES-2 beta-lactamase. The identical core structures of ertapenem, doripenem, and meropenem are likely responsible for the observed similarities in the kinetics with these carbapenems. The lack of a methyl group in the core structure of imipenem may provide a structural rationale for the increase in turnover of this carbapenem by the GES beta-lactamases
-
-
?
additional information
?
-
a single amino acid difference at position 170 of the GES-1, GES-2, and GES-5 enzymes is responsible for the expansion of their substrate profile to include carbapenem antibiotics. The catalytic efficiency of the enzymes with carbapenems meropenem, ertapenem, and doripenem progressively increases 100fold from GES-1 to -5, mainly due to an increase in the rate of acylation. While acylation is rate limiting for GES-1 and GES-2 for all three carbapenems, acylation and deacylation are indistinguishable for GES-5. Only the core structure of the antibiotic interacts with the active site of the GES-2 beta-lactamase. The identical core structures of ertapenem, doripenem, and meropenem are likely responsible for the observed similarities in the kinetics with these carbapenems. The lack of a methyl group in the core structure of imipenem may provide a structural rationale for the increase in turnover of this carbapenem by the GES beta-lactamases
-
-
?
additional information
?
-
a single amino acid difference at position 170 of the GES-1, GES-2, and GES-5 enzymes is responsible for the expansion of their substrate profile to include carbapenem antibiotics. The catalytic efficiency of the enzymes with carbapenems meropenem, ertapenem, and doripenem progressively increases 100fold from GES-1 to -5, mainly due to an increase in the rate of acylation. While acylation is rate limiting for GES-1 and GES-2 for all three carbapenems, acylation and deacylation are indistinguishable for GES-5. Only the core structure of the antibiotic interacts with the active site of the GES-2 beta-lactamase. The identical core structures of ertapenem, doripenem, and meropenem are likely responsible for the observed similarities in the kinetics with these carbapenems. The lack of a methyl group in the core structure of imipenem may provide a structural rationale for the increase in turnover of this carbapenem by the GES beta-lactamases
-
-
?
additional information
?
-
a single amino acid difference at position 170 of the GES-1, GES-2, and GES-5 enzymes is responsible for the expansion of their substrate profile to include carbapenem antibiotics. The catalytic efficiency of the enzymes with carbapenems meropenem, ertapenem, and doripenem progressively increases 100fold from GES-1 to -5, mainly due to an increase in the rate of acylation. While acylation is rate limiting for GES-1 and GES-2 for all three carbapenems, acylation and deacylation are indistinguishable for GES-5. The identical core structures of ertapenem, doripenem, and meropenem are likely responsible for the observed similarities in the kinetics with these carbapenems. The lack of a methyl group in the core structure of imipenem may provide a structural rationale for the increase in turnover of this carbapenem by the GES beta-lactamases
-
-
?
additional information
?
-
a single amino acid difference at position 170 of the GES-1, GES-2, and GES-5 enzymes is responsible for the expansion of their substrate profile to include carbapenem antibiotics. The catalytic efficiency of the enzymes with carbapenems meropenem, ertapenem, and doripenem progressively increases 100fold from GES-1 to -5, mainly due to an increase in the rate of acylation. While acylation is rate limiting for GES-1 and GES-2 for all three carbapenems, acylation and deacylation are indistinguishable for GES-5. The identical core structures of ertapenem, doripenem, and meropenem are likely responsible for the observed similarities in the kinetics with these carbapenems. The lack of a methyl group in the core structure of imipenem may provide a structural rationale for the increase in turnover of this carbapenem by the GES beta-lactamases
-
-
?
additional information
?
-
a single amino acid difference at position 170 of the GES-1, GES-2, and GES-5 enzymes is responsible for the expansion of their substrate profile to include carbapenem antibiotics. The catalytic efficiency of the enzymes with carbapenems meropenem, ertapenem, and doripenem progressively increases 100fold from GES-1 to -5, mainly due to an increase in the rate of acylation. While acylation is rate limiting for GES-1 and GES-2 for all three carbapenems, acylation and deacylation are indistinguishable for GES-5. The identical core structures of ertapenem, doripenem, and meropenem are likely responsible for the observed similarities in the kinetics with these carbapenems. The lack of a methyl group in the core structure of imipenem may provide a structural rationale for the increase in turnover of this carbapenem by the GES beta-lactamases
-
-
?
additional information
?
-
the recombinant enzyme shows broad substrate specificity with higher catalytic activities with penicillins and carbapenems than with cephalosporins. Poor activity with ceftazidime and cefepime
-
-
?
additional information
?
-
-
the recombinant enzyme shows broad substrate specificity with higher catalytic activities with penicillins and carbapenems than with cephalosporins. Poor activity with ceftazidime and cefepime
-
-
?
additional information
?
-
enzyme hydrolyses all tested penicillins, cephalosporins and carbapenems with the exception of aztreonam
-
-
?
additional information
?
-
-
enzyme hydrolyses all tested penicillins, cephalosporins and carbapenems with the exception of aztreonam
-
-
?
additional information
?
-
-
oxyimino-cephalosporin substrates, interaction and binding structure, modeling, overview
-
-
?
additional information
?
-
-
hydrolytic activities of two metagenome-derived family VIII carboxylesterases (EstSRT1 and EstU1) toward diverse esters and beta-lactam antibiotics, overview. Although EstSRT1 and EstU1 exhibit similar activities toward the hydrolysis of ester substrates, their activities toward beta-lactam antibiotics differ. EstU1 hydrolyzes first-generation cephalosporins, whereas EstSRT1 has activity toward first-, third-, and fourth-generation cephalosporins
-
-
?
additional information
?
-
hydrolytic activities of two metagenome-derived family VIII carboxylesterases (EstSRT1 and EstU1) toward diverse esters and beta-lactam antibiotics, overview. Although EstSRT1 and EstU1 exhibit similar activities toward the hydrolysis of ester substrates, their activities toward beta-lactam antibiotics differ. EstU1 hydrolyzes first-generation cephalosporins, whereas EstSRT1 has activity toward first-, third-, and fourth-generation cephalosporins
-
-
?
additional information
?
-
-
enzyme EstSRT1 displays the broadest substrate specificity among family VIII carboxylesterases with beta-lactamase activity
-
-
?
additional information
?
-
enzyme EstSRT1 displays the broadest substrate specificity among family VIII carboxylesterases with beta-lactamase activity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
amoxicillin + H2O
(2R,4S)-2-[[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
ampicilin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-azaniumyl-1,3-thiazol-4-yl)-2- [[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-azaniumyl-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
biapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[(6,7-dihydro-5H-pyrazolo[1,2-a][1,2,4]triazol-4-ium-6-yl)sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylate
-
activity in resistant strains
-
-
?
carbenicillin + H2O
(2R,4S)-2-((R)-carboxy[2-carboxy(phenyl)acetamido]methyl)-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
AB702957
-
-
-
?
cefadroxil + H2O
(2R)-2-[((R)-([(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino)carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
AB702957
-
-
-
?
cefalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cefamandole + H2O
(2R)-2-[(R)-carboxy[[(2R)-2-hydroxy-2-phenylacetyl]amino]methyl]-5-[[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cefamandole + H2O
(2R)-2-[(R)-carboxy{[(2R)-2-hydroxy-2-phenylacetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cefoperazone + H2O
(2R)-2-[(R)-carboxy([(2S)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-(4-hydroxyphenyl)acetyl]amino)methyl]-5-([(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoperazone + H2O
(2R)-2-[(R)-carboxy{[(2S)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-(4-hydroxyphenyl)acetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cefotiam + H2O
(2R)-2-[(R)-[2-(2-amino-1,3-thiazol-4-yl)acetamido](carboxy)methyl]-5-[({1-[2-(dimethylamino)ethyl]-1H-tetrazol-5-yl}sulfanyl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
ceftaxidime + H2O
(2R)-2-[(R)-([(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-([(2-carboxypropan-2-yl)oxy]imino)acetyl]amino)(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
ceftazidime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino](carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftriaxone + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[[(2-methyl-5,6-dioxo-1,2,5,6-tetrahydro-1,2,4-triazin-3-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy[[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
doripenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4-methyl-3-(((3S,5S)-5-[(sulfamoylamino)methyl]pyrrolidin-3-yl)sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
doripenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4-methyl-3-([(3S,5S)-5-[(sulfamoylamino)methyl]pyrrolidin-3-yl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
ertapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl]sulfanyl)-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([2-[(iminomethyl)amino]ethyl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
nitrocefin + H2O
(2R)-2-((R)-carboxy[2-(thiophen-2-yl)acetamido]methyl)-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy([(2R)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-phenylacetyl]amino)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
Klebsiella pneumoniae MTCC 3384
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
Klebsiella pneumoniae NDM-7
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
AB702957
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
AB702957
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
Klebsiella pneumoniae MTCC 3384
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-azaniumyl-1,3-thiazol-4-yl)-2- [[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-azaniumyl-1,3-thiazol-4-yl)-2- [[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-azaniumyl-1,3-thiazol-4-yl)-2- [[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-azaniumyl-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-azaniumyl-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
the enzyme catalyzes the hydrolysis of the C-N bond of the beta-lactam ring
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbapenem + H2O
[(2R)-2,3-dihydro-1H-pyrrol-2-yl]acetic acid
-
-
-
?
carbapenem + H2O
[(2R)-2,3-dihydro-1H-pyrrol-2-yl]acetic acid
-
-
-
?
cefalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefamandole + H2O
(2R)-2-[(R)-carboxy[[(2R)-2-hydroxy-2-phenylacetyl]amino]methyl]-5-[[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefamandole + H2O
(2R)-2-[(R)-carboxy[[(2R)-2-hydroxy-2-phenylacetyl]amino]methyl]-5-[[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefoperazone + H2O
(2R)-2-[(R)-carboxy{[(2S)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-(4-hydroxyphenyl)acetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoperazone + H2O
(2R)-2-[(R)-carboxy{[(2S)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-(4-hydroxyphenyl)acetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoperazone + H2O
(2R)-2-[(R)-carboxy{[(2S)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-(4-hydroxyphenyl)acetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
Klebsiella pneumoniae MTCC 3384
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
ceftaxidime + H2O
(2R)-2-[(R)-([(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-([(2-carboxypropan-2-yl)oxy]imino)acetyl]amino)(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftaxidime + H2O
(2R)-2-[(R)-([(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-([(2-carboxypropan-2-yl)oxy]imino)acetyl]amino)(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftaxidime + H2O
(2R)-2-[(R)-([(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-([(2-carboxypropan-2-yl)oxy]imino)acetyl]amino)(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephalosporin + H2O
?
-
the enzyme is responsible for the resistance to extended spectrum cephalosporins
-
-
?
cephalosporin + H2O
?
-
the enzyme is responsible for the resistance to extended spectrum cephalosporins
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([2-[(iminomethyl)amino]ethyl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
the enzyme catalyzes the hydrolysis of the C-N bond of the beta-lactam ring
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([2-[(iminomethyl)amino]ethyl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
activity in resistant strains
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
the enzyme shows carbapenemase activity, e.g. against the carbapenem antibiotics meropenem and imipenem used in treatment of Pseudomonas aeruginosa infection, and contributes to resistance to anti-pseudomonal agents, overview
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
activity in resistant strains
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
the enzyme shows carbapenemase activity, e.g. against the carbapenem antibiotics meropenem and imipenem used in treatment of Pseudomonas aeruginosa infection, and contributes to resistance to anti-pseudomonal agents, overview
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
AB702957
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
Klebsiella pneumoniae MTCC 3384
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
Klebsiella pneumoniae NDM-7
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy([(2R)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-phenylacetyl]amino)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy([(2R)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-phenylacetyl]amino)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
additional information
?
-
AB702957
enzyme MacQ has the bifunctional capacity to degrade both N-acylhomoserine lactone (N-acylhomoserine lactone acylase, EC 3.5.1.97) and beta-lactam antibiotics by deacylation activity. MacQ is able to inactivate a variety of beta-lactams, including penicillin derivatives (penicillin G, ampicillin, amoxicillin, and carbenicillin) and cephalosporin derivatives (cephalexin and cefadroxil)
-
-
-
additional information
?
-
no induction by imipenem and cefoxitin
-
-
?
additional information
?
-
-
no induction by imipenem and cefoxitin
-
-
?
additional information
?
-
readily hydrolyzes carbapenems
-
-
?
additional information
?
-
the enzyme hydrolyses all beta-lactam antibiotics tested, except for the monobactam aztreonam and the penicillin piperacillin
-
-
?
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime is a poor substrate
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime is a poor substrate
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime is a poor substrate
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview. Cefepime is a poor substrate
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime and cefotaxime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime and cefotaxime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime and cefotaxime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime and cefotaxime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime and cefotaxime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime and cefotaxime are poor substrates
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview. Cefepime and cefotaxime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime is a poor substrate
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime is a poor substrate
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime is a poor substrate
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime is a poor substrate
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime is a poor substrate
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefepime is a poor substrate
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview. Cefepime is a poor substrate
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
-
cephalosporins bearing oximino side chains are resistant to hydrolysis by class C enzymes, the side chain is necessary but not sufficent for production of resistance, it must be combinated with the dihydrothiazine ring
-
-
?
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
-
cephalosporins bearing oximino side chains are resistant to hydrolysis by class C enzymes, the side chain is necessary but not sufficent for production of resistance, it must be combinated with the dihydrothiazine ring
-
-
?
additional information
?
-
-
cephalosporins bearing oximino side chains are resistant to hydrolysis by class C enzymes, the side chain is necessary but not sufficent for production of resistance, it must be combinated with the dihydrothiazine ring
-
-
?
additional information
?
-
-
substrate specificity in vivo with different enzymes genotypes, overview
-
-
-
additional information
?
-
the enzyme hydrolyzes penicillins, cephalothin, and the expanded-spectrum cephalosporins cefepime and moxalactam
-
-
?
additional information
?
-
antibiotic sensitivity of recombinant wild-type and mutant blaSHV-14, overview
-
-
-
additional information
?
-
-
antibiotic sensitivity of recombinant wild-type and mutant blaSHV-14, overview
-
-
-
additional information
?
-
resistance to antibiotics of recombinant His-tagged wild-type and mutant enzymes expressed in Escherichia coli strain CS109, overview
-
-
-
additional information
?
-
Klebsiella pneumoniae MTCC 3384
antibiotic sensitivity of recombinant wild-type and mutant blaSHV-14, overview
-
-
-
additional information
?
-
Klebsiella pneumoniae NDM-7
resistance to antibiotics of recombinant His-tagged wild-type and mutant enzymes expressed in Escherichia coli strain CS109, overview
-
-
-
additional information
?
-
the enzyme hydrolyzes penicillins, cephalothin, and the expanded-spectrum cephalosporins cefepime and moxalactam
-
-
?
additional information
?
-
expression of the ampC gene of HLHK5 is regulated by its ampR gene, which acts as a repressor
-
-
?
additional information
?
-
-
expression of the ampC gene of HLHK5 is regulated by its ampR gene, which acts as a repressor
-
-
?
additional information
?
-
-
a VIM-2 enzyme inserted in integron In58, in an isolate from a female cystic fibrosis patient, is resistant to all antimicrobial agents tested except colistin, overview
-
-
?
additional information
?
-
-
antibiotic resistance rates and mechanisms of beta-lactam and aminoglycoside resistance, e.g. against ticarcillin, among human isolates of Pseudomonas aeruginosa isolated in the extra-hospital setting, MIC values of diverse beta-lactam antibiotics, resistance mechanisms, overview
-
-
?
additional information
?
-
-
carbapenem resistance screening of diverse clinical strains by a 2-mercaptopropionic acid inhibition test method, determination of MIC values, overview
-
-
?
additional information
?
-
-
determination of MIC values of SHV-1 for several antibiotics, overview
-
-
?
additional information
?
-
-
genetic variants of beta-lactamases cause resistance to antibiotics cefepime and/or ceftazidime, overview
-
-
?
additional information
?
-
-
occurrence and mechanisms of amikacin resistance and its association with beta-lactamases in Pseudomonas aeruginosa, a Korean nationwide study, gene blaOXA-10 is involved in amikain resistance, overview
-
-
?
additional information
?
-
-
production of beta-lactamases is the main mechanism of resistance to beta-lactams in Gram-negative bacteria, the phenomenon of continuing suppression of bacterial growth after removal of beta-lactamase inhibitors is termed post-beta-lactamase inhibitor effect, PLIE. EDTA combined with carbapenems produces a significant PLIE on VIM-MBL-positive Pseudomonas aeruginosa strains
-
-
?
additional information
?
-
-
screening for beta-lactamase genes in clincal isolates using Etest MBL screening test, The blaVIM-13-producing isolate shows resistance to all beta-lactams, except aztreonam, gentamicin, tobramycin, and ciprofloxacin, VIM-13 confers slightly higher levels of resistance to piperacillin and lower levels of resistance to ceftazidime and cefepime than VIM-1, MIC values, overview
-
-
?
additional information
?
-
screening for beta-lactamase genes in clincal isolates using Etest MBL screening test, The blaVIM-13-producing isolate shows resistance to all beta-lactams, except aztreonam, gentamicin, tobramycin, and ciprofloxacin, VIM-13 confers slightly higher levels of resistance to piperacillin and lower levels of resistance to ceftazidime and cefepime than VIM-1, MIC values, overview
-
-
?
additional information
?
-
screening for beta-lactamase genes in clincal isolates using Etest MBL screening test, The blaVIM-13-producing isolate shows resistance to all beta-lactams, except aztreonam, gentamicin, tobramycin, and ciprofloxacin, VIM-13 confers slightly higher levels of resistance to piperacillin and lower levels of resistance to ceftazidime and cefepime than VIM-1, MIC values, overview
-
-
?
additional information
?
-
-
screening for strains expressing IMP-15 beta-lactamases in clinical human isolates from a Mexican tertiary-care hospital, overview
-
-
?
additional information
?
-
screening for strains expressing IMP-15 beta-lactamases in clinical human isolates from a Mexican tertiary-care hospital, overview
-
-
?
additional information
?
-
screening for strains expressing IMP-15 beta-lactamases in clinical human isolates from a Mexican tertiary-care hospital, overview
-
-
?
additional information
?
-
-
screening for strains expressing VIM-1, and other beta-lactamases in clinical human isolates from a Mexican tertiary-care hospital, overview
-
-
?
additional information
?
-
screening for strains expressing VIM-1, and other beta-lactamases in clinical human isolates from a Mexican tertiary-care hospital, overview
-
-
?
additional information
?
-
screening for strains expressing VIM-1, and other beta-lactamases in clinical human isolates from a Mexican tertiary-care hospital, overview
-
-
?
additional information
?
-
susceptibility and enzymatic activity of metallo-beta-lactamases in Pseudomonas aeruginosa-producing metallo-beta-lactamases, overview
-
-
?
additional information
?
-
-
susceptibility and enzymatic activity of metallo-beta-lactamases in Pseudomonas aeruginosa-producing metallo-beta-lactamases, overview
-
-
?
additional information
?
-
the IMP-9 variant of metallo-beta-lactamases show a broad spectrum antibiotic resistance resulting in an out break in 2005-2007 in China, multidrug-resistant profile of IMP-9 MBL variants, overview
-
-
?
additional information
?
-
-
the IMP-9 variant of metallo-beta-lactamases show a broad spectrum antibiotic resistance resulting in an out break in 2005-2007 in China, multidrug-resistant profile of IMP-9 MBL variants, overview
-
-
?
additional information
?
-
the Pseudomonas aeruginosa strain that contains the mobile metallo-beta-lactamase gene, designated blaVIM-7, located on a plasmid (p07-406), is resistant to all tested antimicrobials except polymyxin B causing an outbreak of infections in Houston, USA, overview
-
-
?
additional information
?
-
-
the Pseudomonas aeruginosa strain that contains the mobile metallo-beta-lactamase gene, designated blaVIM-7, located on a plasmid (p07-406), is resistant to all tested antimicrobials except polymyxin B causing an outbreak of infections in Houston, USA, overview
-
-
?
additional information
?
-
enzyme hydrolyses all tested penicillins, cephalosporins and carbapenems with the exception of aztreonam
-
-
?
additional information
?
-
-
enzyme hydrolyses all tested penicillins, cephalosporins and carbapenems with the exception of aztreonam
-
-
?
additional information
?
-
-
hydrolytic activities of two metagenome-derived family VIII carboxylesterases (EstSRT1 and EstU1) toward diverse esters and beta-lactam antibiotics, overview. Although EstSRT1 and EstU1 exhibit similar activities toward the hydrolysis of ester substrates, their activities toward beta-lactam antibiotics differ. EstU1 hydrolyzes first-generation cephalosporins, whereas EstSRT1 has activity toward first-, third-, and fourth-generation cephalosporins
-
-
?
additional information
?
-
hydrolytic activities of two metagenome-derived family VIII carboxylesterases (EstSRT1 and EstU1) toward diverse esters and beta-lactam antibiotics, overview. Although EstSRT1 and EstU1 exhibit similar activities toward the hydrolysis of ester substrates, their activities toward beta-lactam antibiotics differ. EstU1 hydrolyzes first-generation cephalosporins, whereas EstSRT1 has activity toward first-, third-, and fourth-generation cephalosporins
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
Co2+
Cu2+
Fe3+
mononuclear Co(2+)- and Fe(3+)-containing lactamase L1 are essentially inactive
Mn2+
NaCl
Ni2+
Zinc
Zn2+
additional information
Co2+
preparation of a Co(II)-substituted VIM-2 analogue, crystal structure analysis, overview
Co2+
UV-vis studies on IMP-1 containing 1 equivalent of Co(II) show a strong ligand-to-metal charge transition at 340 nm, and the intensity of this feature increases when the second equivalent of Co(II) is added to the enzyme
Co2+
mononuclear Co(2+)- and Fe(3+)-containing lactamase L1 are essentially inactive
Ni2+
-
Ni2+ binds in the Zn2+-site and the ring-opened product coordinates Ni2+
Zinc
the Zn-Zn distance in D120E mutant is increased by 0.3 A compared with wild-type enzyme
Zn2+
a di-Zn(II)-containing hydrolase, coordination geometry of Zn2 in IMP-2 is different from that of IMP-1, unlike Zn1, the electron density map at Zn2 shows the existence of partially dissociated Zn(II) ion from the active site structure, overview
Zn2+
zinc content is determined by ICP-MS. Position of the second inhibitory zinc ion has not been identified
Zn2+
metalloenzyme, E152C mutant contains 0.80 equivalents of Zn, which is similar to the metal content of wild type enzyme
Zn2+
metalloenzyme, dependent, exist either as mononuclear or as dinuclear enzymes
Zn2+
a zinc metalloenzyme
Zn2+
the active-site residues His120, His122 and His189 are co-ordinated to Zn1 metal ion, whereas Asp124, Cys208 and His250 are co-ordinated to Zn2 metal ion for their catalytic activity. The di-zinc centre of NDM-7 is located at the bottom of the shallow groove and is a part of the binding pocket of the enzyme. The two Zn metal ions present in the active-site cleft take part in the catalytic activity of the NDM-7 via bridging to different active-site residues by forming strong interactions
Zn2+
VIM metallo-beta-lactamases, VIM-1 and VIM-13 inactivation by Zn2+ removal
Zn2+
enzyme has a a fourcoordinate Zn2 site and both tetrahedral and pentacoordinated Zn1 sites
Zn2+
Zn2+ ions have a pronounced stabilizing effect and are necessary for preserving the structure
Zn2+
protein binds one equivalent of zinc, no inhibition by a second equivalent of zinc
Zn2+
a di-zinc enzyme, meropenem enzyme-bound structure with Zn2+, PDB ID 5AXO, overview. Zn1 and Zn2 at the active site pocket bind in a distance of 3.5A. The zinc ions are involved in inhibitor binding
Zn2+
absolutely required, dinuclear zinc-metalloenzyme, metal-binding Asp, the wild-type conatins 1.9 mol of Zn2+ per mol of subunit, D120 mutant enzymes show reduced metal content, overview
Zn2+
-
enzyme possesses a binding site motif unique for metallo-beta-lactamases
Zn2+
two zinc ions are coordinated with conserved amino acid residues located in segments 2 to 5
additional information
two metal ions are required for the hydrolytic activity of native zinc class B1 MBL BcII and highlight the importance of the Zn2 site during turnover
additional information
-
two metal ions are required for the hydrolytic activity of native zinc class B1 MBL BcII and highlight the importance of the Zn2 site during turnover
additional information
-
the metal binding sites, particularly the Zn2 site, in metallo-beta-lactamase L1 are very flexible and can accommodate a number of different divalent metal ions
additional information
analysis of the metal content of enzyme VIM-2, metal binding kinetics, overview
additional information
metal-binding to metal-free IMP-1 follows a positive-cooperative mode
additional information
mononuclear metal ion containing and heterobimetallic analogues of the enzyme are generated and characterized using kinetic and spectroscopic studies. Heterobimetallic analogues (ZnCoL1, ZnFeL1, FeFeL1, and CoCoL1) analogues of L1 are generated, and stopped flow kinetic studies revealed that these enzymes rapidly hydrolyze nitrocefin and that there are large amounts of the reaction intermediate formed during the reaction
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R,3E)-2-([amino(phenyl)acetyl]amino)-3-[(1,2-dihydroxy-3-mercaptoprop-1-en-1-yl)imino]propanoic acid
-
competitive
(2Z)-2-(((E)-2-carboxy-2-[(2-thienylacetyl)amino]vinyl)imino)-3-mercaptobut-3-enoic acid
-
-
(6Z)-7-oxo-6-(4H-pyrazolo[1,5-c][1,3]thiazol-2-ylmethylidene)-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
-
-
1-(2S)-3-mercapto-2-methyl-propionyl-D-proline
competitive inhibitor
2-(((3-mercapto-5-(2-methylphenyl)-4H-1,2,4-triazol-4-yl)imino)methyl)benzoic acid
most effective inhibitor
2-(7-(4-methoxyphenyl)-5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidin-4-ylidene)-malononitrile
-
-
2-picolinic acid
competitive inhibitor, 8% residual activity at 0.1 mM
3-((benzyloxycarbonylaminooxy)carbonyloxy)benzoic acid
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
3-hydroxy-5-(hydroxycarbamoyl)benzoic acid
-
92% residual activity at 0.1 mM
3-hydroxy-5-[(4-hydroxyphenyl)carbonyl]benzoic acid
-
67% residual activity at 0.1 mM
3-[(2R)-2-(dihydroxyboranyl)-2-[[(thiophen-2-ylmethyl)sulfonyl]amino]ethyl]benzoic acid
-
3-[(2R)-2-[(benzylsulfonyl)amino]-2-(dihydroxyboranyl)ethyl]benzoic acid
-
4-chloro-7-(4-methoxyphenyl)-5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidine
-
-
4-chloro-7-(4-methylphenyl)-5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidine
-
-
7-(4-methylphenyl)-8,9-diphenyl-7H-pyrrolo[3,2-e][1,2,4]triazolo[4,3-c]pyrimidine-3-thione
-
-
AAGHYY
-
synthetic peptide, derived from screenings using phage display and peptide arrays
amoxicillin
susceptible to amoxicillin in combination with clavulanic acid
benzyl (4-chlorophenoxy)carbonyloxycarbamate
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
benzyl (4-methoxyphenoxy)carbonyloxycarbamate
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
benzyl (4-nitrophenoxy)carbonyloxycarbamate
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
benzyl (naphthalen-2-yloxy)carbonyloxycarbamate
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
benzyl carbonylbis(oxy)dicarbamate
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
benzyl methoxycarbonyloxycarbamate
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
benzyl methyl(phenoxycarbonyloxy)carbamate
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits slightly, 20fold less effectiv than benzyl phenoxycarbonyloxycarbamate
benzyl phenoxycarbonothioyloxycarbamate
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits slightly
benzyl phenoxycarbonyloxycarbamate
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
benzyl phenylcarbamoyloxycarbamate
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
beta-lactamase inhibitory protein
i.e. BLIP. Structures of two thermodynamically distinctive complexes of BLIP mutants with TEM-1 beta-lactamase. The complex BLIP Y51ATEM-1 is a tight binding complex with the most negative binding heat capacity change among all of the mutants, whereas BLIP W150ATEM-1 is a weak complex with one of the least negative binding heat capacity changes. BLIP Tyr51 is a canonical and Trp150 an anti-canonical TEM-1-contact residue (canonical refers to the alanine substitution resulting in a matched change in the hydrophobicity of binding free energy). Structure determination indicates a rearrangement of the interactions between Asp49 of the W150A BLIP mutant and the catalytic pocket of TEM-1. The Asp49 of W150A moves more than 4 A to form two new hydrogen bonds while losing four original hydrogen bonds
-
biphenyl-4-ylmethyl phenoxycarbonyloxycarbamate
-
completely inactivated, 2 micro M concentration, o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
carbapenem antibiotics
-
EDTA combined with carbapenems produces a significant PLIE on VIM-MBL-positive Pseudomonas aeruginosa strains
D-captopril
-
acts by displacing the catalytic hydroxyl ion required for antibiotic hydrolysis and by intercalating its sulfhydryl group between the 2 Zn2+ ions, the inhibitor molecule is located on one side of the active site cleft
eupalitin
binding to the enzyme involves residues Leu176, Thr177, Leu196, Ile245, and Leu253
fosfomycin
-
determination of MIC values for the different isolates: range of 0.004 to over 0.512 mg/ml, MIC50 is 0.032 mg/ml and MIC90 is 0.128 mg/ml
galangin
-
flavonoid, inhibition is not reversible by addition of Zn2+, orientation in the active site, the 4-keto and the 5-hydroxy groups bind to the Zn1 atom of the enzyme
KCl
-
concentrations of KCl higher than 20 mM weaken slightly the hydrolytic ability of VIM-12
L-captopril
binding to the enzyme involves residues His72, His74, Asp76, His77, and His150
lactivicin
inhibits penicillin-binding proteins and serine beta-lactamases
luteolin
binding to the enzyme involves residues His72, HIS74, Phe114, His150, and Pro216
N',5-dihydroxy-N,N-dipyrrolidin-1-ylbenzene-1,3-dicarboxamide
-
64% residual activity at 0.1 mM
N,3-dihydroxy-5-[(4-hydroxyphenyl)carbonyl]benzamide
-
15% residual activity at 0.1 mM
N,5-dihydroxy-N'-methylbenzene-1,3-dicarboxamide
-
47% residual activity at 0.1 mM
N,5-dihydroxy-N'-phenylbenzene-1,3-dicarboxamide
-
42% residual activity at 0.1 mM
N,N-diethyl-N',5-dihydroxybenzene-1,3-dicarboxamide
-
66% residual activity at 0.1 mM
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
-
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
-
N-(phenoxycarbonyloxy)benzenesulfonamide
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
N-benzyl-N',5-dihydroxybenzene-1,3-dicarboxamide
-
46% residual activity at 0.1 mM
N-benzylidene-N'-(7-(4-methylphenyl)-5,6-diphenyl-7Hpyrrolo[2,3-d]pyramidin-4-yl)-hydrazine
-
-
Phenanthroline
-
phenanthroline shows no growth inhibition activity on Pseudomonas aeruginosa ATCC 27583 at all tested concentrations between 1.0 and 8.0 mM
phosphate
competitive inhibition. 50 mM, 30% decrease of wild-type activity. 5 mM, 90% decrease of activity of mutant enzyme D120A
pyridine-2,4-dicarboxylic acid
competitive inhibitor, 38% residual activity at 0.1 mM
rosmarinic acid
binding to the enzyme involves residues Thr177, Ala178, Val179, Val218, and Ile245
tazobactam fragment
five-atom vinyl carboxylic acid fragment of tazobactam, bonded to Ser130
-
tebipenem
Michaelis-Menten complex, exhibits slow tight-binding inhibition at low micromolar concentrations versus the chromogenic substrate nitrocefin, binding structure analysis, overview. TBPM-PI is a prodrug that is quickly hydrolyzed to tebipenem (TEBI). Active site of BlaC-tebipenem Michaelis-Menten complex showing interactions and interatomic distances between tebipenem and active site residues, overview
thiono derivative of N-(phenylacetyl)thioglycylglycolic acid
-
weak reversible inhibition
-
trans-7-oxo-6-(sulfooxy)-1,6-diazabicyclo[3.2.1]octan-2-carboxamide
-
NXL104, inhibits both class A and class C beta-lactamases, irreversible inhibition of enzyme BlaC by the inhibitor with a non-lactam structural scaffold, forming a carbamyl adduct with the enzyme, the enzyme-inhibitor adduct remains stable for at least 48 hours, three-dimensional crystal structure of the BlaC-NXL104 carbamyl adduct, overview. Inhibition kinetics and mechanism, modeling, overview
vanadate/hydroxamic acid complexes
competitive inhibition mechanism, low concentrations of 1:1 complexes of vanadate with hydroxamic acids, the hydroxamic acid functional group is essential for inhibition, complex structure, overview, complex modeling
-
ZINC01807204
ZINC01807204 might be useful as a lead molecule for further optimization and development of more potent non beta-lactam inhibitors against KPC-2
[(phenoxycarbonyl)oxy][(phenylacetyl)oxy]amine
-
0.01 mM, irreversible inhibition
2-mercaptoethanol
-
mercaptoethanol shows no growth inhibition activity on Pseudomonas aeruginosa ATCC 27583 at all tested concentrations between 7.0 and 55 mM
2-[[5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-yl]sulfanyl]-N-phenylacetamide
-
2-[[5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-yl]sulfanyl]-N-phenylacetamide
-
2-[[5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-yl]sulfanyl]-N-phenylacetamide
-
2-[[5-(2-hydroxyphenyl)-1,3,4-thiadiazol-2-yl]sulfanyl]-N-phenylacetamide
-
2-[[5-(2-hydroxyphenyl)-1,3,4-thiadiazol-2-yl]sulfanyl]-N-phenylacetamide
-
2-[[5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-yl]sulfanyl]-N-phenylacetamide
-
2-[[5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-yl]sulfanyl]-N-phenylacetamide
-
2-[[5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-yl]sulfanyl]-N-phenylacetamide
-
4,7-dichloro benzothien-2-yl sulfonylaminomethyl boronic acid
inhibitor synergizes with imipenem against Acintobacter baumannii
4,7-dichloro benzothien-2-yl sulfonylaminomethyl boronic acid
-
6-beta-iodopenicillanic acid
-
the nature of the interactions of the rearranged inhibitor with conserved active site residues, the position of the inhibitor carboxylate and its interactions with Asn132, Asn104, and Asn170
avibactam
efficiently inactivates enzyme BlaMab via the reversible formation of a covalent adduct. Efficacy of the amoxicillin/avibactam combination in Mycobacterium abscessus-infected zebrafish, overview
aztreonam
effective inhibitor; effective inhibitor; effective inhibitor
beta-lactamase inhibitor protein
-
i.e. BLIP, 17 kDa protein produced by Streptomyces clavuligerus, specific for class A enzymes, construction of diverse mutants of BLIP for identification of functional epitopes, enzyme-inhibitor complex modeling
-
beta-lactamase inhibitor protein
i.e. BLIP, 17 kDa protein produced by Streptomyces clavuligerus, specific for class A enzymes, construction of diverse mutants of BLIP for identification of functional epitopes, enzyme-inhibitor complex modeling
-
beta-lactamase inhibitor protein
i.e. BLIP, 17 kDa protein produced by Streptomyces clavuligerus, specific for class A enzymes, construction of diverse mutants of BLIP for identification of functional epitopes, enzyme-inhibitor complex modeling
-
beta-lactamase inhibitor protein
-
BLIP, competitive inhibitor of a number of class A beta-lactamases
-
beta-lactamase inhibitor protein
-
i.e. BLIP, 17 kDa protein produced by Streptomyces clavuligerus, specific for class A enzymes, construction of diverse mutants of BLIP for identification of functional epitopes, enzyme-inhibitor complex modeling
-
bulgecin A
-
competitive inhibition of the enzyme in its two-zinc form, but fails to inhibit when the enzyme is in the single-zinc form. The competitive inhibition is restored by restoring the second zinc ion
carbenicillin
effective inhibitor; effective inhibitor; effective inhibitor
cefotaxime
-
competitive inhibition of cephalothin hydrolysis; inhibits hydrolysis of cephalothin, P99 beta-lactamase
cefoxitin
perturbs the active site structure and the conformation of the omega-loop bearing the catalytic residue Glu166, inhibition mechanism
clavulanate
-
the enzyme-inhibitor adduct is completely hydrolyzed within 48 h, binding structure comparison, inhibition kinetics and mechanism, modeling, overview
clavulanate
-
strong inhibition by the mechanism-based inhibitor, Gln69, Arg220, Thr237, and probably Arg240A might be important in the stabilization of the clavulanate molecule, simulations, overview
clavulanate
-
62.2-92.1% of activity is inhibited after preincubation with 0.1 mM clavulanate
clavulanic acid
-
mechanism-based inhibitor, specific for class A beta-lactamases
clavulanic acid
-
after 20min 20% remaining activity; inactivation in 20 min
clavulanic acid
-
after 20 min 55% remaining activity; inactivation in 20 min
clavulanic acid
-
mechanism-based inhibitor, specific for class A beta-lactamases
clavulanic acid
-
shows 8fold reduction with clavulanic acid when combined with ceftriaxone, cefpodoxime and cefotaxime
clavulanic acid
-
after 20 min 90% remaining activity; inactivation in 20 min
clavulanic acid
-
shows 8fold reduction with clavulanic acid when combined with ceftriaxone, cefpodoxime and cefotaxime
clavulanic acid
-
shows 8fold reduction with clavulanic acid when combined with ceftriaxone, cefpodoxime and cefotaxime
clavulanic acid
reduces the hydrolysis rate of 100 microM nitrocefin by 50% when the enzyme is preincubated with various concentrations of the inhibitor for 5 min at 37°C before the addition of the substrate
Cloxacillin
-
hydrolysis or inhibition, depending on pH, temperature, ratio enzyme/cloaxacillin
doripenem
the carbapenems doripenem and ertapenem are slow substrates that acylate the enzyme but are only slowly deacylated and can therefore act also as potent inhibitors of BlaC
EDTA
inactivation of CphA wild-type and the H118A, H196A, H263A and D120A mutants by EDTA is studied in 15 mM sodium cacodylate (pH 6.5) at 30°C in the presence of different concentrations of EDTA
EDTA
EDTA inhibits the activity of VIM-13 approximately 25 times less than it inhibits the activity of VIM-1
EDTA
-
EDTA combined with carbapenems produces a significant PLIE on VIM-MBL-positive Pseudomonas aeruginosa strains
EDTA
-
EDTA, PHEN, and MET present weak bactericidal activity against Pseudomonas aeruginosa with substrate ceftazidime
EDTA
-
0.1 mM EDTA inhibits only 4.8-26.8% of the activity of the TEM-type beta-lactamase
ertapenem
the carbapenems doripenem and ertapenem are slow substrates that acylate the enzyme but are only slowly deacylated and can therefore act also as potent inhibitors of BlaC
ethyl 3-(benzyloxycarbonyl)amino-2-oxo-1,1-difluoropropylphosphonate
-
-
HSAYSDTRRGDYG
-
synthetic peptide, derived from screens using phage display and peptide arrays
HSAYSDTRRGDYG
-
synthetic peptide, derived from screenings using phage display and peptide arrays
HSAYSDTRRGDYG
-
synthetic peptide, derived from screens using phage display and peptide arrays
Imipenem
binding to the enzyme involves residues His72, His74, His150, His215, and Arg252
Mercaptoacetic acid
-
mercaptoacetic acid demonstrates hydrolytic activity against imipenem but not against ceftazidime
Mercaptopropionic acid
-
1.4 mM mercaptopropionic acid demonstrates hydrolytic activity against imipenem but not against ceftazidime, mercaptopropionic acid provided the best results by using imipenem as substrate
Mercaptopropionic acid
-
1.4 mM mercaptopropionic acid demonstrates hydrolytic activity against imipenem but not against ceftazidime, mercaptopropionic acid provided the best results by using imipenem as substrate
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
-
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
-
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
-
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
-
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
-
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
-
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
-
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
-
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
-
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
-
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
-
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
-
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
-
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
-
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
-
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
-
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
-
N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
-
N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
-
N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
-
N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
-
N-phenyl-2-[[5-(pyridin-4-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
-
N-phenyl-2-[[5-(pyridin-4-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
-
N-[2-(7-chloro-quinolin-4-ylamino)-ethyl]-3-mercapto-propionamide
-
IC50: 0.0063 mM
N-[2-(7-chloro-quinolin-4-ylamino)-ethyl]-3-mercapto-propionamide
-
IC50: 0.0142 mM
N-[3-(7-chloro-quinolin-4-ylamino)-propyl]-3-mercapto-propionamide
-
IC50: 0.0065 mM
N-[3-(7-chloro-quinolin-4-ylamino)-propyl]-3-mercapto-propionamide
-
IC50: 0.0066 mM
N-[4-(7-chloro-quinolin-4-ylamino)-butyl]-3-mercapto-propionamide
-
IC50: 0.0024 mM
N-[4-(7-chloro-quinolin-4-ylamino)-butyl]-3-mercapto-propionamide
-
IC50: 0.0025 mM
N-[5-(7-chloro-quinolin-4-ylamino)-pentyl]-3-mercapto-propionamide
-
IC50: 0.0076 mM
N-[5-(7-chloro-quinolin-4-ylamino)-pentyl]-3-mercapto-propionamide
-
IC50: 0.0067 mM
N-[6-(7-cloro-quinolin-4-ylamino)-hexyl]-3-mercapto-propionamide
-
IC50: 0.0049 mM
N-[6-(7-cloro-quinolin-4-ylamino)-hexyl]-3-mercapto-propionamide
-
IC50: 0.0034 mM
nitrocefin
substrate inhibition, NaHCO3 can reactivate the enzyme
nitrocefin
substrate inhibition; substrate inhibition; substrate inhibition; substrate inhibition
penem 1
a 6-methylidene penem, the carboxylated Lys84 in the active site of OXA-24 utilizes a catalytic water molecule to deacylate the Ser81, resulting in hydrolysis of the penem 1 inhibitor, and the enzyme is regenerated because Lys84 is not decarboxylated and hydrolyzes the next arriving inhibitor molecule, proposed mechanism for penem 1 and OXA-24, overview
penem 1
a 6-methylidene penem, proposed mechanism for penem 1 and OXA-1, overview. Penem 1 can also cause the essentially irreversible decarboxylation of OXA-1
RRGHYY
-
synthetic peptide, derived from screens using phage display and peptide arrays; synthetic peptide, derived from screens using phage display and peptide arrays, inhibition mechanism
RRGHYY
-
synthetic peptide, derived from screenings using phage display and peptide arrays, inhibition mechanism
RRGHYY
-
synthetic peptide, derived from screens using phage display and peptide arrays; synthetic peptide, derived from screens using phage display and peptide arrays, inhibition mechanism
SA-1-204
a penam sulfone inhibitor, can effectively inhibit OXA-24 by decarboxylating the Lys84 in the active site
sodium benzyl 2-(1',3'-benzothiazol-2'-yl)-2-oxo-ethylphosphonate
-
sodium benzyl 2-(1',3'-benzothiazol-2'-yl)-2-oxo-ethylphosphonate
-
sodium benzyl [2-oxo-2-(2-oxo-2,3-dihydro-1,3-benzoxazol-6-yl)ethyl]phosphonate
-
sodium benzyl [2-oxo-2-(2-oxo-2,3-dihydro-1,3-benzoxazol-6-yl)ethyl]phosphonate
-
sodium benzyl {2-[3-(2-chlorophenyl)-5-methyl-1,2-oxazol-4-yl]-2-oxoethyl}phosphonate
-
sodium benzyl {2-[3-(2-chlorophenyl)-5-methyl-1,2-oxazol-4-yl]-2-oxoethyl}phosphonate
-
sodium biphenyl-4-ylmethyl [2-(biphenyl-4-yl)-2-oxoethyl]phosphonate
-
sodium biphenyl-4-ylmethyl [2-(biphenyl-4-yl)-2-oxoethyl]phosphonate
-
Sulbactam
-
shows 8fold reduction of activity with sulbactam when combined with ceftriaxone, cefpodoxime and cefotaxime
Sulbactam
-
shows 8fold reduction of activity with sulbactam when combined with ceftriaxone, cefpodoxime and cefotaxime
Sulbactam
-
0.1 mM inhibit the enzyme competitively and reversibly with respect to nitrocefin
Sulbactam
-
shows 8fold reduction of activity with sulbactam when combined with ceftriaxone, cefpodoxime and cefotaxime
tazobactam
-
IC50 deoendent on enzyme concentration; inactivation after 1 h , IC50 0.00005 mM
tazobactam
-
after 1 h 90% remaining activity; inactivation after 1-2 h
tazobactam
-
IC50 deoendent on enzyme concentration; inactivation after 1-2 h
tazobactam
-
after 1 h 20% remaining activity; inactivation after 1-2 h
tazobactam
-
IC50 deoendent on enzyme concentration; inactivation after 1-2 h
tazobactam
sulfone inhibitor, acyclic form is covalently bound to ctalytic Ser70 side chain
tazobactam
-
class A-specific inhibitor, inactivation of the wild-type enzyme, binds to Ser70 of the active site, mutant S130G is resistant, inhibition mechanism, the mutation S130G is not essential for resistance but for acylation of the inhibitor molecule, which initiates the fragmentation of tazobactam by the mutant enzyme, mass spectrometry analysis
tazobactam
effective inhibitor; effective inhibitor; effective inhibitor
tazobactam
-
0.1 mM inhibit the enzyme in a time-dependent manner, but the activity of the enzyme reappears due to the slow hydrolysis of the covalently acylated enzyme
vanadate/(3,4-dihydroxyphenyl)methanaminium complex
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/(3,4-dihydroxyphenyl)methanaminium complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/2,3,5,6-tetrahydroxycyclohexa-2,5-diene-1,4-dione complex
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/2,3,5,6-tetrahydroxycyclohexa-2,5-diene-1,4-dione complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/2,3-dihydroxynaphthalene-1,4-dione complex
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/2,3-dihydroxynaphthalene-1,4-dione complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/2-(3,4-dihydroxyphenyl)acetate complex
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/2-(3,4-dihydroxyphenyl)acetate complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/2-methoxyphenol complex
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/2-methoxyphenol complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/3,4,5,6-tetrafluorobenzene-1,2-diol complex
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/3,4,5,6-tetrafluorobenzene-1,2-diol complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/3,4-dihydroxybenzoate complex
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/3,4-dihydroxybenzoate complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/3-phenylcatechol complex
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols, most effective
vanadate/3-phenylcatechol complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols, most effective
vanadate/4-nitrobenzene-1,2-diol complex
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/4-nitrobenzene-1,2-diol complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/biphenyl-3,4-diol complex
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/biphenyl-3,4-diol complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/naphthalene-1,2-diol complex
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/naphthalene-1,2-diol complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/naphthalene-2,3-diol complex
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/naphthalene-2,3-diol complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/phenol complex
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/phenol complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/pyrocatechol complex
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/pyrocatechol complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
Zn2+
protein binds one equivalent of zinc, no inhibition by a second equivalent of zinc
additional information
-
development of diaryl-substituted azolylthioacetamides as metallo-beta-lactamase-1 enzyme inhibitors, overview no inhibition by N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide, N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide, N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide, N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide, N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide, and N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide, poor inhibition by N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide, 2-[[5-(2-hydroxyphenyl)-1,3,4-thiadiazol-2-yl]sulfanyl]-N-phenylacetamide, N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide, N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide, N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide, and N-phenyl-2-[[5-(pyridin-4-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide; development of eighteen diaryl-substituted azolylthioacetamides as metallo-beta-lactamase enzyme inhibitors, overview. No inhibition by N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide, N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide, N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide, and N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide. Docking studies reveal that the azolylthioacetamides, which have the broadest inhibitory activity, coordinate to the ZnII ion(s) preferentially via the triazole moiety, while other moieties interact mostly with the conserved active site residues
-
additional information
development of diaryl-substituted azolylthioacetamides as metallo-beta-lactamase-1 enzyme inhibitors, overview no inhibition by N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide, N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide, N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide, N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide, N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide, and N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide, poor inhibition by N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide, 2-[[5-(2-hydroxyphenyl)-1,3,4-thiadiazol-2-yl]sulfanyl]-N-phenylacetamide, N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide, N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide, N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide, and N-phenyl-2-[[5-(pyridin-4-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide; development of eighteen diaryl-substituted azolylthioacetamides as metallo-beta-lactamase enzyme inhibitors, overview. No inhibition by N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide, N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide, N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide, and N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide. Docking studies reveal that the azolylthioacetamides, which have the broadest inhibitory activity, coordinate to the ZnII ion(s) preferentially via the triazole moiety, while other moieties interact mostly with the conserved active site residues
-
additional information
-
pH dependence of inhibition, mechanism, the thiol anion of the cysteinyl peptide inhibitors displaces the hydroxide ion from the active site Zn2+, D,D-peptides bind to the enzyme better than other diastereomers due to the stereochemistry of the active site
-
additional information
-
hydrolysis of cephalosporin beta-lactam antibiotics generates dihydrothiazines which subsequently undergo isomerization at C6 by C-S bond cleavage and through the intermediacy of a thiol. These thiols can be trapped by the beta-lactamase from Bacillus cereus, causing inhibition of the enzyme. The rate of production of the thiol corresponds to the rate of inhibition, and the inhibition constants are in the micromolar range but vary with the nature of the cephalosporin derivative. The thiol binds to the zinc ion, which in turn perturbs the metal-bound histidines. Inhibition is slowly removed as the thiol becomes oxidized or undergoes further degradation. The thiol intermediate generated from cephalothin is a slow binding inhibitor. There is no observed inhibition from the analogous degradation products from penicillins
-
additional information
development of diaryl-substituted azolylthioacetamides as metallo-beta-lactamase-1 enzyme inhibitors, overview
-
additional information
-
development of diaryl-substituted azolylthioacetamides as metallo-beta-lactamase-1 enzyme inhibitors, overview
-
additional information
-
no inhibition of wild-type enzyme and mutant enzymes D170N and K232N by NaCl up to 1 M
-
additional information
-
Citrobacter freundii has a cefepime and cefpirome resistance
-
additional information
inhibition by vanadate-catechol complex. 0.1 mM vanadate, varied catechol; vanadate alone (to 1.0 mM) and catechol alone (to 2.0 mM) do not inhibit. Compounds that afford no inhibition are 2,3-dihydroxybenzoic acid, 2,3-dihydroxypyridine (3-hydroxypyrid-2-one), cis-1,2-dihydroxycyclohexane, and L-mandelic acid
-
additional information
beta-ketophosphonates are less effective against OXA-10 enzyme, effective inhibitors of the class D OXA-1 enzyme and the class C P99 enzyme
-
additional information
inhibition mechanism, wild-type and mutant N152A enzyme
-
additional information
-
inhibition mechanism, wild-type and mutant N152A enzyme
-
additional information
-
imipenem, meropenem or doripenem do not behave as inactivators
-
additional information
-
inhibition by vanadate-catechol complex. 0.1 mM vanadate, varied catechol; vanadate alone (to 1.0 mM) and catechol alone (to 2.0 mM) do not inhibit. Compounds that afford no inhibition are 2,3-dihydroxybenzoic acid, 2,3-dihydroxypyridine (3-hydroxypyrid-2-one), cis-1,2-dihydroxycyclohexane, and L-mandelic acid
-
additional information
-
beta-ketophosphonates are less effective against OXA-10 enzyme, effective inhibitors of the class D OXA-1 enzyme and the class C P99 enzyme; beta-ketophosphonates are less effective against OXA-10 enzyme, effective inhibitors of the class D OXA-1 enzyme and the class C P99 enzyme; beta-ketophosphonates are less effective against OXA-10 enzyme, effective inhibitors of the class D OXA-1 enzyme and the class C P99 enzyme
-
additional information
beta-ketophosphonates are less effective against OXA-10 enzyme, effective inhibitors of the class D OXA-1 enzyme and the class C P99 enzyme; beta-ketophosphonates are less effective against OXA-10 enzyme, effective inhibitors of the class D OXA-1 enzyme and the class C P99 enzyme; beta-ketophosphonates are less effective against OXA-10 enzyme, effective inhibitors of the class D OXA-1 enzyme and the class C P99 enzyme
-
additional information
beta-ketophosphonates are less effective against OXA-10 enzyme, effective inhibitors of the class D OXA-1 enzyme and the class C P99 enzyme; beta-ketophosphonates are less effective against OXA-10 enzyme, effective inhibitors of the class D OXA-1 enzyme and the class C P99 enzyme; beta-ketophosphonates are less effective against OXA-10 enzyme, effective inhibitors of the class D OXA-1 enzyme and the class C P99 enzyme
-
additional information
-
kinetic inhibitory profiles of monocyclic beta-lactams and carbapenems against FOX-4, overview
-
additional information
the PWP triad is an evolutionarily conserved motif unique to class A beta-lactamases aligning its allosteric site and hence is an effective potential target for enzyme regulation and selective drug design
-
additional information
poor inhibitory potencies of classic beta-lactamase inhibitors clavulanic acid, tazobactam, and sulbactam, which rather act as substrate with the enzyme. Non beta-lactam inhibitors by structure-based virtual screening of ZINC database. MIC values for cytotoxic effects on Escherichia coli and HeLa cells, overview
-
additional information
-
poor inhibitory potencies of classic beta-lactamase inhibitors clavulanic acid, tazobactam, and sulbactam, which rather act as substrate with the enzyme. Non beta-lactam inhibitors by structure-based virtual screening of ZINC database. MIC values for cytotoxic effects on Escherichia coli and HeLa cells, overview
-
additional information
mutation at the glutamate residues in the omega-loop of SHV-14, i.e. E126, E164, and E167, render beta-lactamase inhibitors more efficient
-
additional information
-
mutation at the glutamate residues in the omega-loop of SHV-14, i.e. E126, E164, and E167, render beta-lactamase inhibitors more efficient
-
additional information
carbapenems such as meropenem, doripenem, and ertapenem react with the enzyme to form enzyme-drug covalent complexes that are hydrolyzed extremely slowly
-
additional information
synthesis and structure-activity-relationship data for the first-generation library of bis(benzoyl)phosphates as enzyme inhibitors, overview. Phosphorylated Ser70 in BlaC following inactivation by dibenzoyl phosphate
-
additional information
-
synthesis and structure-activity-relationship data for the first-generation library of bis(benzoyl)phosphates as enzyme inhibitors, overview. Phosphorylated Ser70 in BlaC following inactivation by dibenzoyl phosphate
-
additional information
-
blaIMP-positive Pseudomonas aeruginosa strains ,obtained from clinical specimens, are resistant to beta-lactam, fluoroquinolone and aminoglycoside agents. Efficacies of polymyxin B, colistin, and other antipseudomonal agents against IMP-type MBL-producing Pseudomonas aeruginosa both in vitro and in vivo, MIC values, overview
-
additional information
-
the bactericidal effect of inhibitors of MBL is not influenced by the production of the MBL variants IMP, VIM, SPM, GIM, or SIM
-
additional information
-
carbapenem resistance screening of diverse clinical strains by a 2-mercaptopropionic acid inhibition test method, determination of MIC values, overview
-
additional information
metallo-beta-lactamases are not inhibited by clinical beta-lactamase inhibitors
-
additional information
-
shows high-level resistance to expanded-spectrum cephalosporins and beta-lactam clavulanate combinations
-
additional information
dynamic behavior of the enzyme over simulation time with natural inhibitors using molecular dynamics studies, molecular docking, overview. The zinc ions are involved in inhibitor binding. Inhibitor binding alters the enzyme conformation. The natural inhibitors impairs the substrate binding by occupying a part of enzyme active site
-
additional information
-
no inhibition: Cys-Val-His-Ser-Pro-Asn-Arg-Glu-Cys
-
additional information
development of eighteen diaryl-substituted azolylthioacetamides as New Delhi metallo-beta-lactamase-1 enzyme inhibitors, overview
-
additional information
-
development of eighteen diaryl-substituted azolylthioacetamides as New Delhi metallo-beta-lactamase-1 enzyme inhibitors, overview
-
additional information
-
no inhibition by boric acid, cefotaxime, PMSF
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridine-2,3-dicarboxylic acid
30% increase of activity at 0.1 mM
pyridine-2,5-dicarboxylic acid
14% increase of activity at 0.1 mM
pyridine-3,4-dicarboxylic acid
16% increase of activity at 0.1 mM
additional information
imipenem and cefoxitin do not induce OXA-114 expression
-
additional information
-
imipenem and cefoxitin do not induce OXA-114 expression
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0023 - 0.027
(2S,5R,6R)-6-[[(2R)-2-carboxy-2-thiophen-3-ylacetyl]amino]-3,3-dimethyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylic acid
0.315 - 0.323
(6R,7R)-3-[(acetyloxy)methyl]-7-(formylamino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
1.45
(6R,7R)-3-[(acetyloxy)methyl]-7-(hydroxyamino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
0.29
(6R,7R)-3-[(acetyloxy)methyl]-7-amino-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
0.24
(6R,7R)-3-[(acetyloxy)methyl]-7-[formyl(hydroxy)amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
0.005 - 0.06
(6R,7R)-3-[(acetyloxy)methyl]-7-[hydroxy(phenylacetyl)amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
0.031 - 0.21
(6R,7R)-3-[(acetyloxy)methyl]-7-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
0.014 - 0.0154
(6R,7R)-3-[(acetyloxy)methyl]-8-oxo-7-[(thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
0.002 - 0.013
(6R,7S)-3-[(3-carboxy-4-nitro-phenyl)sulfanylmethyl]-8-oxo-7-[(2-thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo-[4.2.0]-oct-2-ene-2-carboxylic acid
0.366
(6R,7Z)-3-[(acetyloxy)methyl]-7-(hydroxyimino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
0.0045
(6R,7Z)-7-(hydroxyimino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate 5,5-dioxide
-
pH and temperature not specified in the publication
0.05 - 0.42
2,2-dimethyl-6beta-({[5-methyl-3-(2-chlorophenyl)isoxazol-4-yl]carbonyl}amino)penam-3alpha-carboxylic acid
0.032
3-([3-dibenzylamino-3-oxopropanoyl]oxy)benzoic acid
pH 7.5, 25°C
0.7
3-([3-[benzyl(methyl)amino]-3-oxopropanoyl]oxy)benzoic acid
pH 7.5, 25°C
0.13 - 0.59
3-([N-[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]glycyl]oxy)benzoic acid
0.06
3-([[(2R)-3-(benzylamino)-2-methyl-3-oxopropanoyl]oxy]methyl)benzoic acid
pH 7.5, 25°C
2.8
3-([[(2S)-3-(benzylamino)-2-methyl-3-oxopropanoyl]oxy]methyl)benzoic acid
pH 7.5, 25°C
0.0026
3-([[2-benzyl-3-oxo-3-(benzylamino)propanoyl]oxy]methyl)benzoic acid
pH 7.5, 25°C
0.32
3-nitrophenyl (2S)-2-hydroxy-3-phenylpropanoate
pH not specified in the publication, temperature not specified in the publication
0.172
3-[[(2S)-2-hydroxy-3-phenylpropanoyl]oxy]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.14
7-(thienyl-2-acetamido)-3-[2-(4-,N,N-dimethylaminophenylazo)pyridinium-methyl]-3-cephem-4-carboxylic acid
-
wild type
0.075
7-(thienyl-2-acetamido)-3-[2-(4-N,N-dimethylaminophenylazo)pyridinium-methyl]-3-cephem-4-carboxylic acid
-
-
0.34
benzyl [[(2R)-2-hydroxy-3-phenylpropanoyl]oxy]carbamate
pH not specified in the publication, temperature not specified in the publication
0.46
benzyl [[(2S)-2-hydroxy-2-phenylacetyl]oxy]carbamate
pH not specified in the publication, temperature not specified in the publication
0.071
benzyl [[(2S)-2-hydroxy-3-phenylpropanoyl]oxy]carbamate
pH not specified in the publication, temperature not specified in the publication
0.02
benzyl [[(2S)-2-hydroxy-4-phenylbutanoyl]oxy]carbamate
pH not specified in the publication, temperature not specified in the publication
0.52
benzyl [[(2S)-2-hydroxypropanoyl]oxy]carbamate
pH not specified in the publication, temperature not specified in the publication
0.394
ceftaxidime
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
0.0023
(2S,5R,6R)-6-[[(2R)-2-carboxy-2-thiophen-3-ylacetyl]amino]-3,3-dimethyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylic acid
beta-lactamases CTX-M-25
0.027
(2S,5R,6R)-6-[[(2R)-2-carboxy-2-thiophen-3-ylacetyl]amino]-3,3-dimethyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylic acid
beta-lactamases CTX-M-26
0.315
(6R,7R)-3-[(acetyloxy)methyl]-7-(formylamino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
0.323
(6R,7R)-3-[(acetyloxy)methyl]-7-(formylamino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
0.005
(6R,7R)-3-[(acetyloxy)methyl]-7-[hydroxy(phenylacetyl)amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
0.06
(6R,7R)-3-[(acetyloxy)methyl]-7-[hydroxy(phenylacetyl)amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
0.031
(6R,7R)-3-[(acetyloxy)methyl]-7-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
-
wild-type enzyme
0.21
(6R,7R)-3-[(acetyloxy)methyl]-7-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
-
mutant enzyme S164R
0.014
(6R,7R)-3-[(acetyloxy)methyl]-8-oxo-7-[(thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
0.0154
(6R,7R)-3-[(acetyloxy)methyl]-8-oxo-7-[(thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
0.002
(6R,7S)-3-[(3-carboxy-4-nitro-phenyl)sulfanylmethyl]-8-oxo-7-[(2-thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo-[4.2.0]-oct-2-ene-2-carboxylic acid
D66N mutant, pH 7.4, room temperature
0.0024
(6R,7S)-3-[(3-carboxy-4-nitro-phenyl)sulfanylmethyl]-8-oxo-7-[(2-thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo-[4.2.0]-oct-2-ene-2-carboxylic acid
wild type, pH 7.4, room temperature
0.0032
(6R,7S)-3-[(3-carboxy-4-nitro-phenyl)sulfanylmethyl]-8-oxo-7-[(2-thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo-[4.2.0]-oct-2-ene-2-carboxylic acid
D66M mutant, pH 7.4, room temperature
0.006
(6R,7S)-3-[(3-carboxy-4-nitro-phenyl)sulfanylmethyl]-8-oxo-7-[(2-thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo-[4.2.0]-oct-2-ene-2-carboxylic acid
D66W mutant, pH 7.4, room temperature
0.007
(6R,7S)-3-[(3-carboxy-4-nitro-phenyl)sulfanylmethyl]-8-oxo-7-[(2-thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo-[4.2.0]-oct-2-ene-2-carboxylic acid
D66Y mutant, pH 7.4, room temperature
0.013
(6R,7S)-3-[(3-carboxy-4-nitro-phenyl)sulfanylmethyl]-8-oxo-7-[(2-thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo-[4.2.0]-oct-2-ene-2-carboxylic acid
D66A mutant, pH 7.4, room temperature
0.05
2,2-dimethyl-6beta-({[5-methyl-3-(2-chlorophenyl)isoxazol-4-yl]carbonyl}amino)penam-3alpha-carboxylic acid
-
-
0.087
2,2-dimethyl-6beta-({[5-methyl-3-(2-chlorophenyl)isoxazol-4-yl]carbonyl}amino)penam-3alpha-carboxylic acid
-
-
0.155
2,2-dimethyl-6beta-({[5-methyl-3-(2-chlorophenyl)isoxazol-4-yl]carbonyl}amino)penam-3alpha-carboxylic acid
-
penicillinase I
0.159
2,2-dimethyl-6beta-({[5-methyl-3-(2-chlorophenyl)isoxazol-4-yl]carbonyl}amino)penam-3alpha-carboxylic acid
-
penicillinase II
0.25
2,2-dimethyl-6beta-({[5-methyl-3-(2-chlorophenyl)isoxazol-4-yl]carbonyl}amino)penam-3alpha-carboxylic acid
-
-
0.42
2,2-dimethyl-6beta-({[5-methyl-3-(2-chlorophenyl)isoxazol-4-yl]carbonyl}amino)penam-3alpha-carboxylic acid
-
-
0.13
3-([N-(phenylacetyl)glycyl]oxy)benzoic acid
-
pH 7.5, 25°C, strain GCI
0.23
3-([N-(phenylacetyl)glycyl]oxy)benzoic acid
-
pH 7.5, 25°C, strain P99
0.13
3-([N-[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]glycyl]oxy)benzoic acid
-
GC1 beta-lactamase
0.59
3-([N-[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]glycyl]oxy)benzoic acid
-
P99 beta-lactamase
0.046
3-[2-(2-aminothiazol-4-yl)2-(Z)-methoxyiminoacetylglycyl]oxybenzoic acid
-
pH 7.5, 25°C, strain GCI
0.059
3-[2-(2-aminothiazol-4-yl)2-(Z)-methoxyiminoacetylglycyl]oxybenzoic acid
-
pH 7.5, 25°C, strain P99
0.00649
amoxicillin
pH 8.0, 30°C, recombinant wild-type enzyme
0.02
amoxicillin
pH and temperature not specified in the publication
0.022
amoxicillin
at 30°C in 100 mM sodium phosphate (pH 7)
0.041
amoxicillin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
0.05414
amoxicillin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
0.0697
amoxicillin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
0.00006
ampicillin
in 20 mM phosphate buffer, (pH 7.0) at 30°C
0.00008
ampicillin
in 20 mM phosphate buffer, (pH 7.0) at 30°C
0.00013
ampicillin
in 20 mM phosphate buffer, (pH 7.0) at 30°C
0.00016
ampicillin
-
30°C, pH 7.0, plasmid-encoded, pBC2e, beta-lactamase MIR-1
0.00016
ampicillin
-
30°C, pH 7.0, plasmid-encoded, pBC4e, beta-lactamase CMY-2
0.0017
ampicillin
-
30°C, pH 7.0, plasmid-encoded, pBC1e, beta-lactamase ACT-1
0.0022
ampicillin
-
30°C, pH 7.0, plasmid-encoded, pBC3e, beta-lactamase CMY-1
0.004
ampicillin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
0.005
ampicillin
100 microM nitrocefin as the reporter substrate, TEM-149 wild-type, pH 7.0, 25°C
0.0051
ampicillin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
0.00954
ampicillin
pH 8.0, 30°C, recombinant wild-type enzyme
0.019
ampicillin
100 microM nitrocefin as the reporter substrate, TEM-149 mutant T182M, pH 7.0, 25°C
0.023
ampicillin
pH not specified in the publication, 30°C, recombinant enzyme
0.024
ampicillin
plasmid pBG66
-
pH and temperature not specified in the publication, mutant enzyme N166A/N170G
0.03
ampicillin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.032
ampicillin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
0.035
ampicillin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.036
ampicillin
His6-tagged wild type OXA-1, pH 7.4, room temperature
0.038
ampicillin
plasmid pBG66
-
pH and temperature not specified in the publication, wild-type enzyme
0.04
ampicillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.056
ampicillin
plasmid pBG66
-
pH and temperature not specified in the publication, mutant enzyme N170G
0.06
ampicillin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.064
ampicillin
-
pH and temperature not specified in the publication, OXA-1 beta-lactamase
0.125
ampicillin
plasmid pGEM-T-easy
-
mutant enzyme W154F, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.13
ampicillin
plasmid pBG66
-
pH and temperature not specified in the publication, mutant enzyme N170A
0.15
ampicillin
in 30 mM sodium cacodylate buffer (pH 6.5) plus 0.05 mM ZnSO4
0.15
ampicillin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.156
ampicillin
pH 7.2, 25°C, recombinant enzyme
0.18
ampicillin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.207
ampicillin
pH 7.2, 25°C, recombinant enzyme
0.229
ampicillin
pH 7.2, 25°C, recombinant enzyme
0.23
ampicillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.25
ampicillin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.258
ampicillin
pH 7.2, 25°C, recombinant enzyme
0.305
ampicillin
pH 7.2, 25°C, recombinant enzyme
0.414
ampicillin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
0.455
ampicillin
pH 7.2, 25°C, recombinant enzyme
0.615
ampicillin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
0.000004
aztreonam
-
30°C, pH 7.0, plasmid-encoded, pBC2e, beta-lactamase MIR-1
0.00001
aztreonam
-
30°C, pH 7.0, plasmid-encoded, pBC3e, beta-lactamase CMY-1
0.04
aztreonam
pH and temperature not specified in the publication
0.00025
benzylpenicillin
30°C, pH 7.0
0.0004
benzylpenicillin
-
30°C, pH 7.0, plasmid-encoded, pBC2e, beta-lactamase MIR-1
0.0004
benzylpenicillin
-
30°C, pH 7.0, plasmid-encoded, pBC4e, beta-lactamase CMY-2
0.0005
benzylpenicillin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
0.0006
benzylpenicillin
100 microM nitrocefin as the reporter substrate, TEM-149 wild-type, pH 7.0, 25°C
0.0007
benzylpenicillin
100 microM nitrocefin as the reporter substrate, TEM-149 mutant T182M, pH 7.0, 25°C
0.001
benzylpenicillin
-
30°C, pH 7.0, plasmid-encoded, pBC3e, beta-lactamase CMY-1
0.0017
benzylpenicillin
-
at 30°C in 50 mM sodium phosphate buffer (pH 7.0)
0.0017
benzylpenicillin
-
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
0.0021
benzylpenicillin
-
30°C, pH 7.0, plasmid-encoded, pBC1e, beta-lactamase ACT-1
0.0023
benzylpenicillin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
0.01
benzylpenicillin
in 100 mM Tris-H2SO4, 300 mM K2SO4 (pH 7.0), at 30°C
0.01
benzylpenicillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.012
benzylpenicillin
at 30°C in 100 mM sodium phosphate (pH 7)
0.013
benzylpenicillin
in 30 mM sodium cacodylate buffer (pH 6.5) plus 0.05 mM ZnSO4
0.017
benzylpenicillin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.019
benzylpenicillin
at 25°C in 100 mM sodium phosphate (pH 7.0)
0.02
benzylpenicillin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.055
benzylpenicillin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.06
benzylpenicillin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.07
benzylpenicillin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.1
benzylpenicillin
plasmid pGEM-T-easy
-
mutant enzyme W154F, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.15
benzylpenicillin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.37
benzylpenicillin
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
0.6
benzylpenicillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.0037
carbenicillin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
0.017
carbenicillin
at 25°C in 100 mM sodium phosphate (pH 7.0)
0.02174
carbenicillin
pH 8.0, 30°C, recombinant wild-type enzyme
0.32
carbenicillin
in 30 mM sodium cacodylate buffer (pH 6.5) plus 0.05 mM ZnSO4
0.005
cefalotin
pH 7.2, 25°C, recombinant enzyme
0.01
cefalotin
pH 7.2, 25°C, recombinant enzyme
0.011
cefalotin
pH 7.2, 25°C, recombinant enzyme
0.013
cefalotin
pH 7.2, 25°C, recombinant enzyme
0.015
cefalotin
pH 7.2, 25°C, recombinant enzyme
0.025
cefazolin
in 30 mM sodium cacodylate buffer (pH 6.5) plus 0.05 mM ZnSO4
0.054
cefazolin
-
30°C, pH 7.0, plasmid-encoded, pBC3e, beta-lactamase CMY-1
0.15
cefazolin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
1
cefepime
Km above 1.0 mM at 30°C in 100 mM sodium phosphate (pH 7)
1
cefepime
-
Km above 1.0 mM, in 0.01 M phosphate buffer (pH 7.0), at 25°C
0.0383
cefoperazone
pH 7.5, 25°C, recombinant His-tagged mutant E162A
0.0574
cefoperazone
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
0.0962
cefoperazone
pH 7.5, 25°C, recombinant His-tagged mutant E164A
0.000015
cefotaxime
-
30°C, pH 7.0, plasmid-encoded, pBC3e, beta-lactamase CMY-1
0.00002
cefotaxime
in 20 mM phosphate buffer, (pH 7.0) at 30°C
0.00007
cefotaxime
-
30°C, pH 7.0, plasmid-encoded, pBC1e, beta-lactamase ACT-1
0.00009
cefotaxime
in 20 mM phosphate buffer, (pH 7.0) at 30°C
0.0005
cefotaxime
in 20 mM phosphate buffer, (pH 7.0) at 30°C
0.004
cefotaxime
-
30°C, pH 7.0, plasmid-encoded, pBC2e, beta-lactamase MIR-1
0.021
cefotaxime
His6-tagged wild type OXA-1, pH 7.4, room temperature
0.049
cefotaxime
in 30 mM sodium cacodylate buffer (pH 6.5) plus 0.05 mM ZnSO4
0.063
cefotaxime
pH not specified in the publication, 30°C, recombinant enzyme
0.086
cefotaxime
pH and temperature not specified in the publication
0.341
cefotaxime
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
0.3647
cefotaxime
pH 8.0, 30°C, recombinant wild-type enzyme
0.0000011
cefoxitin
-
30°C, pH 7.0, plasmid-encoded, pBC4e, beta-lactamase CMY-2
0.00001
cefoxitin
Km less than 0.00001 mM at 30°C in 100 mM sodium phosphate (pH 7)
0.000055
cefoxitin
-
30°C, pH 7.0, plasmid-encoded, pBC3e, beta-lactamase CMY-1
0.0005
cefoxitin
-
30°C, pH 7.0, plasmid-encoded, pBC1e, beta-lactamase ACT-1
0.00075
cefoxitin
-
30°C, pH 7.0, plasmid-encoded, pBC2e, beta-lactamase MIR-1
0.016
cefoxitin
pH 7.2, 25°C, recombinant enzyme
0.023
cefoxitin
pH 7.2, 25°C, recombinant enzyme
0.027
cefoxitin
pH 7.2, 25°C, recombinant enzyme
0.05
cefoxitin
pH 7.2, 25°C, recombinant enzyme
0.063
cefoxitin
pH 7.2, 25°C, recombinant enzyme
0.107
cefoxitin
pH 7.2, 25°C, recombinant enzyme
0.65
cefoxitin
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
0.019
ceftazidime
pH 7.2, 25°C, recombinant enzyme
0.035
ceftazidime
pH and temperature not specified in the publication
0.079
ceftazidime
pH 7.2, 25°C, recombinant enzyme
0.086
ceftazidime
pH 7.2, 25°C, recombinant enzyme
0.115
ceftazidime
pH 7.2, 25°C, recombinant enzyme
0.115
ceftazidime
30°C, pH 7.0. The affinity of MIR-4 beta-lactamase for ceftazidime is quite low
0.133
ceftazidime
pH 7.2, 25°C, recombinant enzyme
0.144
ceftazidime
pH 7.2, 25°C, recombinant enzyme
1
ceftazidime
Km above 1.0 mM at 30°C in 100 mM sodium phosphate (pH 7)
1
ceftazidime
-
Km above 1.0 mM, in 0.01 M phosphate buffer (pH 7.0), at 25°C
0.01176
ceftriaxone
pH 8.0, 30°C, recombinant wild-type enzyme
0.0000012
cefuroxime
-
30°C, pH 7.0, plasmid-encoded, pBC4e, beta-lactamase CMY-2
0.000005
cefuroxime
-
30°C, pH 7.0, plasmid-encoded, pBC3e, beta-lactamase CMY-1
0.000019
cefuroxime
-
30°C, pH 7.0, plasmid-encoded, pBC1e, beta-lactamase ACT-1
0.0006
cefuroxime
-
30°C, pH 7.0, plasmid-encoded, pBC2e, beta-lactamase MIR-1
0.024
cefuroxime
pH and temperature not specified in the publication
0.0085
cephalexin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
0.00897
cephalexin
pH 8.0, 30°C, recombinant wild-type enzyme
0.014
cephalexin
-
30°C, pH 7.0, plasmid-encoded, pBC3e, beta-lactamase CMY-1
0.016
cephalexin
-
30°C, pH 7.0, plasmid-encoded, pBC2e, beta-lactamase MIR-1
0.016
cephalexin
-
30°C, pH 7.0, plasmid-encoded, pBC4e, beta-lactamase CMY-2
0.042
cephalexin
-
30°C, pH 7.0, plasmid-encoded, pBC1e, beta-lactamase ACT-1
0.05
cephalexin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
1.162
cephalexin
plasmid pBG66
-
pH and temperature not specified in the publication, wild-type enzyme
1.56
cephalexin
plasmid pBG66
-
pH and temperature not specified in the publication, mutant enzyme N170A
2.59
cephalexin
plasmid pBG66
-
pH and temperature not specified in the publication, mutant enzyme N170G
0.045
cephaloridine
at 30°C in 100 mM sodium phosphate (pH 7)
0.05
cephaloridine
plasmid pGEM-T-easy
-
mutant enzyme W154F, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.06
cephaloridine
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.065
cephaloridine
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.08
cephaloridine
-
pH and temperature not specified in the publication, OXA-1 beta-lactamase
0.093
cephaloridine
-
30°C, pH 7.0, plasmid-encoded, pBC2e, beta-lactamase MIR-1
0.093
cephaloridine
-
30°C, pH 7.0, plasmid-encoded, pBC4e, beta-lactamase CMY-2
0.11
cephaloridine
-
30°C, pH 7.0, plasmid-encoded, pBC3e, beta-lactamase CMY-1
0.29
cephaloridine
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.4
cephaloridine
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.45
cephaloridine
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.506
cephaloridine
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
2
cephaloridine
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.0021
cephalothin
-
30°C, pH 7.0, plasmid-encoded, pBC2e, beta-lactamase MIR-1
0.0021
cephalothin
-
30°C, pH 7.0, plasmid-encoded, pBC4e, beta-lactamase CMY-2
0.004
cephalothin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.005
cephalothin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.005
cephalothin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.007
cephalothin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.007
cephalothin
pH not specified in the publication, 30°C, recombinant enzyme
0.015
cephalothin
at 30°C in 100 mM sodium phosphate (pH 7)
0.015
cephalothin
in 100 mM Tris-H2SO4, 300 mM K2SO4 (pH 7.0), at 30°C
0.021
cephalothin
pH and temperature not specified in the publication
0.025
cephalothin
plasmid pGEM-T-easy
-
mutant enzyme W154F, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.03
cephalothin
-
30°C, pH 7.0, plasmid-encoded, pBC3e, beta-lactamase CMY-1
0.038
cephalothin
-
30°C, pH 7.0, plasmid-encoded, pBC1e, beta-lactamase ACT-1
0.04
cephalothin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.045
cephalothin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
0.046
cephalothin
in 20 mM phosphate buffer, (pH 7.0) at 30°C
0.057
cephalothin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
0.106
cephalothin
in 20 mM phosphate buffer, (pH 7.0) at 30°C
0.148
cephalothin
in 20 mM phosphate buffer, (pH 7.0) at 30°C
0.182
cephalothin
plasmid pBG66
-
pH and temperature not specified in the publication, wild-type enzyme
0.21
cephalothin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.21
cephalothin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.227
cephalothin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
0.45
cephalothin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.577
cephalothin
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
0.655
cephalothin
pH 8.0, 30°C, recombinant wild-type enzyme
1.5
cephalothin
plasmid pBG66
-
pH and temperature not specified in the publication, mutant enzyme N170G
0.0000005
Cloxacillin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
0.00016
Cloxacillin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
0.03
Cloxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.1
Cloxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.11
Cloxacillin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.14
Cloxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154F, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.2
Cloxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.22
Cloxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.25
Cloxacillin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.007
doripenem
pH not specified in the publication, 30°C, recombinant enzyme
0.064
doripenem
pH 7.2, 25°C, recombinant enzyme
0.083
doripenem
pH 7.2, 25°C, recombinant enzyme
0.119
doripenem
pH 7.2, 25°C, recombinant enzyme
0.125
doripenem
pH 7.2, 25°C, recombinant enzyme
0.126
doripenem
pH 7.2, 25°C, recombinant enzyme
0.151
doripenem
pH 7.2, 25°C, recombinant enzyme
0.004
ertapenem
pH not specified in the publication, 30°C, recombinant enzyme
0.017
ertapenem
pH 7.2, 37°C, recombinant enzyme, in presence of NaCl
0.00005
Imipenem
-
30°C, pH 7.0, plasmid-encoded, pBC3e, beta-lactamase CMY-1
0.00015
Imipenem
-
30°C, pH 7.0, plasmid-encoded, pBC2e, beta-lactamase MIR-1
0.00037
Imipenem
-
30°C, pH 7.0, plasmid-encoded, pBC1e, beta-lactamase ACT-1
0.001
Imipenem
in 20 mM phosphate buffer, (pH 7.0) at 30°C
0.002
Imipenem
in 20 mM phosphate buffer, (pH 7.0) at 30°C
0.004
Imipenem
in 20 mM phosphate buffer, (pH 7.0) at 30°C
0.0042
Imipenem
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
0.02
Imipenem
pH 7.2, 25°C, recombinant enzyme
0.052
Imipenem
pH not specified in the publication, 30°C, recombinant enzyme
0.056
Imipenem
pH 7.2, 25°C, recombinant enzyme
0.062
Imipenem
pH 7.2, 25°C, recombinant enzyme
0.082
Imipenem
pH 7.2, 25°C, recombinant enzyme
0.148
Imipenem
pH 7.2, 25°C, recombinant enzyme
0.3
Imipenem
in 30 mM sodium cacodylate buffer (pH 6.5) plus 0.05 mM ZnSO4
2
Imipenem
Km above 2 mM, in 100 mM Tris-H2SO4, 300 mM K2SO4 (pH 7.0), at 30°C
0.016
meropenem
pH not specified in the publication, 30°C, recombinant enzyme
0.045
meropenem
pH 7.2, 25°C, recombinant enzyme
0.049
meropenem
pH 7.2, 25°C, recombinant enzyme
0.054
meropenem
pH 7.2, 25°C, recombinant enzyme
0.058
meropenem
pH 7.2, 25°C, recombinant enzyme
0.099
meropenem
pH 7.2, 25°C, recombinant enzyme
0.119
meropenem
pH 7.2, 25°C, recombinant enzyme
0.28
meropenem
in 30 mM sodium cacodylate buffer (pH 6.5) plus 0.05 mM ZnSO4
0.0023
nitrocefin
lactamase ZnCo-L1, 1.0 Zn(2+), 1.0 Co(2+)
0.0036
nitrocefin
lactamase ZnFe-L1, 1.0 Zn(2+), 1.0 Fe(3+)
0.004
nitrocefin
pH 7.2, 25°C, recombinant enzyme
0.004
nitrocefin
lactamase ZnFe-L1, 1.2 Zn(2+), 0.9 Fe(3+)
0.0043
nitrocefin
lactamase 1Co-L1, 0.9 Co(2+), 0.10 Zn(2+)
0.005
nitrocefin
pH 7.2, 25°C, recombinant enzyme
0.006
nitrocefin
pH 7.2, 25°C, recombinant enzyme
0.008
nitrocefin
-
30°C, pH 7.0, plasmid-encoded, pBC2e, beta-lactamase MIR-1
0.008
nitrocefin
-
30°C, pH 7.0, plasmid-encoded, pBC4e, beta-lactamase CMY-2
0.008
nitrocefin
in 30 mM sodium cacodylate buffer (pH 6.5) plus 0.05 mM ZnSO4
0.008
nitrocefin
pH 7.2, 25°C, recombinant enzyme
0.0083
nitrocefin
pH 7.2, temperature not specified in the publication, recombinant enzyme
0.009
nitrocefin
-
pH and temperature not specified in the publication, OXA-1 beta-lactamase
0.00948
nitrocefin
pH 8.0, 30°C, recombinant wild-type enzyme
0.01
nitrocefin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.01
nitrocefin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.011
nitrocefin
pH 7.2, 25°C, recombinant enzyme
0.013
nitrocefin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.022
nitrocefin
-
30°C, pH 7.0, plasmid-encoded, pBC1e, beta-lactamase ACT-1
0.023
nitrocefin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
0.025
nitrocefin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.028
nitrocefin
pH 7.2, temperature not specified in the publication, recombinant enzyme
0.035
nitrocefin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.038
nitrocefin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
0.045
nitrocefin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
0.05
nitrocefin
plasmid pGEM-T-easy
-
mutant enzyme W154F, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.053
nitrocefin
lactamase 1Fe-L1, 0.9 Co(2+), 0.20 Zn(2+)
0.06
nitrocefin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.1
nitrocefin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.11
nitrocefin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.116
nitrocefin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
0.1893
nitrocefin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
0.23
nitrocefin
-
30°C, pH 7.0, plasmid-encoded, pBC3e, beta-lactamase CMY-1
0.0000006
Oxacillin
-
30°C, pH 7.0, plasmid-encoded, pBC4e, beta-lactamase CMY-2
0.00002
Oxacillin
-
30°C, pH 7.0, plasmid-encoded, pBC3e, beta-lactamase CMY-1
0.00009
Oxacillin
-
30°C, pH 7.0, plasmid-encoded, pBC1e, beta-lactamase ACT-1
0.0001
Oxacillin
-
30°C, pH 7.0, plasmid-encoded, pBC2e, beta-lactamase MIR-1
0.000118
Oxacillin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
0.02
Oxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.031
Oxacillin
-
pH and temperature not specified in the publication, OXA-1 beta-lactamase
0.06
Oxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.1
Oxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.1
Oxacillin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.125
Oxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154F, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.13
Oxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.1931
Oxacillin
pH 8.0, 30°C, recombinant wild-type enzyme
0.2
Oxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.2
Oxacillin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.65
Oxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.102
panipenem
pH not specified in the publication, 30°C, recombinant enzyme
0.003
penicillin G
plasmid pBG66
-
pH and temperature not specified in the publication, mutant enzyme N170G
0.00335
penicillin G
pH 8.0, 30°C, recombinant wild-type enzyme
0.0079
penicillin G
mutant E166C, carrying 6-bromoacetyl-2-dimethylaminonaphthalene label, pH 7.0, 22°C
0.008
penicillin G
pH and temperature not specified in the publication
0.008
penicillin G
plasmid pBG66
-
pH and temperature not specified in the publication, mutant enzyme N170A
0.02
penicillin G
plasmid pBG66
-
pH and temperature not specified in the publication, mutant enzyme N166A/N170G
0.028
penicillin G
plasmid pBG66
-
pH and temperature not specified in the publication, wild-type enzyme
0.05
penicillin G
-
mutant R61H/E64H/43H, 25°C, pH not specified in the publication
0.0568
penicillin G
-
mutant M182T/T195S/A224V, 25°C, pH not specified in the publication
0.001
piperacillin
in 100 mM Tris-H2SO4, 300 mM K2SO4 (pH 7.0), at 30°C
0.0014
piperacillin
100 microM nitrocefin as the reporter substrate, TEM-149 wild-type, pH 7.0, 25°C
0.0034
piperacillin
100 microM nitrocefin as the reporter substrate, TEM-149 mutant T182M, pH 7.0, 25°C
0.007
piperacillin
pH and temperature not specified in the publication
0.01256
piperacillin
pH 8.0, 30°C, recombinant wild-type enzyme
0.021
piperacillin
at 30°C in 100 mM sodium phosphate (pH 7)
0.053
piperacillin
pH not specified in the publication, 30°C, recombinant enzyme
0.0557
piperacillin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
0.058
piperacillin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
0.0716
piperacillin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
0.375
piperacillin
in 30 mM sodium cacodylate buffer (pH 6.5) plus 0.05 mM ZnSO4
0.454
piperacillin
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
1.3
Sulbactam
in 30 mM sodium cacodylate buffer (pH 6.5) plus 0.05 mM ZnSO4
0.006
ticarcillin
at 30°C in 100 mM sodium phosphate (pH 7)
0.00792
ticarcillin
pH 8.0, 30°C, recombinant wild-type enzyme
0.014
ticarcillin
pH and temperature not specified in the publication
0.04
ticarcillin
in 100 mM Tris-H2SO4, 300 mM K2SO4 (pH 7.0), at 30°C
0.5
ticarcillin
pH not specified in the publication, 30°C, recombinant enzyme
additional information
additional information
steady-state kinetics
-
additional information
additional information
steady-state kinetics
-
additional information
additional information
steady-state kinetics
-
additional information
additional information
-
combination of detailed post- and pre-steady state kinetics
-
additional information
additional information
-
enzyme-ligand interaction kinetics and energies
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
for substrate cefepime, wild-type AmpC-B2 and AmpC-A, Km-value is above 1000 mM
-
additional information
additional information
-
for substrate cefepime, wild-type AmpC-B2 and AmpC-A, Km-value is above 1000 mM
-
additional information
additional information
pre-steady-state and steady-state kinetics, overview
-
additional information
additional information
pre-steady-state, stopped-flow experiments with cefoxitin, solvent kinetic isotope effects and kinetic analysis with different substrates, kinetic mechanism, overview
-
additional information
additional information
-
pre-steady-state, stopped-flow experiments with cefoxitin, solvent kinetic isotope effects and kinetic analysis with different substrates, kinetic mechanism, overview
-
additional information
additional information
enzyme kinetics and thermodynamics
-
additional information
additional information
Michaelis-Menten steady-state kinetics studies
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics studies
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.2 - 84
(2S,5R,6R)-6-[[(2R)-2-carboxy-2-thiophen-3-ylacetyl]amino]-3,3-dimethyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylic acid
1.02 - 1180
(6R,7R)-3-[(acetyloxy)methyl]-7-(formylamino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
1.6
(6R,7R)-3-[(acetyloxy)methyl]-7-(hydroxyamino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
0.46
(6R,7R)-3-[(acetyloxy)methyl]-7-amino-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
0.32
(6R,7R)-3-[(acetyloxy)methyl]-7-[formyl(hydroxy)amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
0.121 - 0.49
(6R,7R)-3-[(acetyloxy)methyl]-7-[hydroxy(phenylacetyl)amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
0.45 - 1.5
(6R,7R)-3-[(acetyloxy)methyl]-7-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
1.81 - 690
(6R,7R)-3-[(acetyloxy)methyl]-8-oxo-7-[(thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
0.08 - 1.6
(6R,7S)-3-[(3-carboxy-4-nitro-phenyl)sulfanylmethyl]-8-oxo-7-[(2-thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo-[4.2.0]-oct-2-ene-2-carboxylic acid
2.56
(6R,7Z)-3-[(acetyloxy)methyl]-7-(hydroxyimino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
0.54
(6R,7Z)-7-(hydroxyimino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate 5,5-dioxide
-
pH and temperature not specified in the publication
0.25
3-([3-dibenzylamino-3-oxopropanoyl]oxy)benzoic acid
pH 7.5, 25°C
0.33
3-([3-[benzyl(methyl)amino]-3-oxopropanoyl]oxy)benzoic acid
pH 7.5, 25°C
11 - 19
3-([N-[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]glycyl]oxy)benzoic acid
2.9
3-([[(2R)-3-(benzylamino)-2-methoxy-3-oxopropanoyl]oxy]methyl)benzoic acid
pH 7.5, 25°C
1.17
3-([[(2R)-3-(benzylamino)-2-methyl-3-oxopropanoyl]oxy]methyl)benzoic acid
pH 7.5, 25°C
7.4
3-([[(2S)-3-(benzylamino)-2-methoxy-3-oxopropanoyl]oxy]methyl)benzoic acid
pH 7.5, 25°C
6.6
3-([[(2S)-3-(benzylamino)-2-methyl-3-oxopropanoyl]oxy]methyl)benzoic acid
pH 7.5, 25°C
0.05
3-([[2-benzyl-3-oxo-3-(benzylamino)propanoyl]oxy]methyl)benzoic acid
pH 7.5, 25°C
10.9
3-nitrophenyl (2S)-2-hydroxy-3-phenylpropanoate
pH not specified in the publication, temperature not specified in the publication
6.9
3-[[(2S)-2-hydroxy-3-phenylpropanoyl]oxy]benzoic acid
pH not specified in the publication, temperature not specified in the publication
667
7-(thienyl-2-acetamido)-3-[2-(4-,N,N-dimethylaminophenylazo)pyridinium-methyl]-3-cephem-4-carboxylic acid
-
-
50
7-(thienyl-2-acetamido)-3-[2-(4-N,N-dimethylaminophenylazo)pyridinium-methyl]-3-cephem-4-carboxylic acid
-
-
5.9
benzyl [[(2R)-2-hydroxy-3-phenylpropanoyl]oxy]carbamate
pH not specified in the publication, temperature not specified in the publication
3.5
benzyl [[(2S)-2-hydroxy-2-phenylacetyl]oxy]carbamate
pH not specified in the publication, temperature not specified in the publication
8.7
benzyl [[(2S)-2-hydroxy-3-phenylpropanoyl]oxy]carbamate
pH not specified in the publication, temperature not specified in the publication
1.5
benzyl [[(2S)-2-hydroxy-4-phenylbutanoyl]oxy]carbamate
pH not specified in the publication, temperature not specified in the publication
1.5
benzyl [[(2S)-2-hydroxypropanoyl]oxy]carbamate
pH not specified in the publication, temperature not specified in the publication
0.3
ceftaxidime
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
8.2
(2S,5R,6R)-6-[[(2R)-2-carboxy-2-thiophen-3-ylacetyl]amino]-3,3-dimethyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylic acid
beta-lactamases CTX-M-25
84
(2S,5R,6R)-6-[[(2R)-2-carboxy-2-thiophen-3-ylacetyl]amino]-3,3-dimethyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylic acid
beta-lactamases CTX-M-26
1.02
(6R,7R)-3-[(acetyloxy)methyl]-7-(formylamino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
1180
(6R,7R)-3-[(acetyloxy)methyl]-7-(formylamino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
0.121
(6R,7R)-3-[(acetyloxy)methyl]-7-[hydroxy(phenylacetyl)amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
0.49
(6R,7R)-3-[(acetyloxy)methyl]-7-[hydroxy(phenylacetyl)amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
0.45
(6R,7R)-3-[(acetyloxy)methyl]-7-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
-
mutant enzyme S164R
1.5
(6R,7R)-3-[(acetyloxy)methyl]-7-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
-
wild-type enzyme
1.81
(6R,7R)-3-[(acetyloxy)methyl]-8-oxo-7-[(thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
690
(6R,7R)-3-[(acetyloxy)methyl]-8-oxo-7-[(thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
0.08
(6R,7S)-3-[(3-carboxy-4-nitro-phenyl)sulfanylmethyl]-8-oxo-7-[(2-thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo-[4.2.0]-oct-2-ene-2-carboxylic acid
D66W mutant, pH 7.4, room temperature
0.17
(6R,7S)-3-[(3-carboxy-4-nitro-phenyl)sulfanylmethyl]-8-oxo-7-[(2-thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo-[4.2.0]-oct-2-ene-2-carboxylic acid
D66M mutant, pH 7.4, room temperature
0.19
(6R,7S)-3-[(3-carboxy-4-nitro-phenyl)sulfanylmethyl]-8-oxo-7-[(2-thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo-[4.2.0]-oct-2-ene-2-carboxylic acid
D66A mutant, pH 7.4, room temperature
0.25
(6R,7S)-3-[(3-carboxy-4-nitro-phenyl)sulfanylmethyl]-8-oxo-7-[(2-thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo-[4.2.0]-oct-2-ene-2-carboxylic acid
D66Y mutant, pH 7.4, room temperature
1.2
(6R,7S)-3-[(3-carboxy-4-nitro-phenyl)sulfanylmethyl]-8-oxo-7-[(2-thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo-[4.2.0]-oct-2-ene-2-carboxylic acid
D66N mutant, pH 7.4, room temperature
1.6
(6R,7S)-3-[(3-carboxy-4-nitro-phenyl)sulfanylmethyl]-8-oxo-7-[(2-thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo-[4.2.0]-oct-2-ene-2-carboxylic acid
wild type, pH 7.4, room temperature
25
3-([N-(phenylacetyl)glycyl]oxy)benzoic acid
-
pH 7.5, 25°C, strain GCI
125
3-([N-(phenylacetyl)glycyl]oxy)benzoic acid
-
pH 7.5, 25°C, strain P99
11
3-([N-[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]glycyl]oxy)benzoic acid
-
GC1 beta-lactamase
19
3-([N-[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]glycyl]oxy)benzoic acid
-
P99 beta-lactamase
11
3-[2-(2-aminothiazol-4-yl)2-(Z)-methoxyiminoacetylglycyl]oxybenzoic acid
-
pH 7.5, 25°C, strain GCI
19
3-[2-(2-aminothiazol-4-yl)2-(Z)-methoxyiminoacetylglycyl]oxybenzoic acid
-
pH 7.5, 25°C, strain P99
1.77
amoxicillin
pH 8.0, 30°C, recombinant wild-type enzyme
2.03
amoxicillin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
2.38
amoxicillin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
21
amoxicillin
pH and temperature not specified in the publication
532.5
amoxicillin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
0.0126
ampicillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.06
ampicillin
in 20 mM phosphate buffer, (pH 7.0) at 30°C
0.07
ampicillin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.132
ampicillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.55
ampicillin
-
30°C, pH 7.0, plasmid-encoded, pBC2e, beta-lactamase MIR-1
0.55
ampicillin
-
30°C, pH 7.0, plasmid-encoded, pBC3e, beta-lactamase CMY-1
0.55
ampicillin
-
30°C, pH 7.0, plasmid-encoded, pBC4e, beta-lactamase CMY-2
0.65
ampicillin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
0.9
ampicillin
plasmid pBG66
-
pH and temperature not specified in the publication, mutant enzyme N166A/N170G
1.4
ampicillin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
2.4
ampicillin
plasmid pGEM-T-easy
-
mutant enzyme W154F, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
3
ampicillin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
9.62
ampicillin
pH 8.0, 30°C, recombinant wild-type enzyme
10.3
ampicillin
in 30 mM sodium cacodylate buffer (pH 6.5) plus 0.05 mM ZnSO4
18
ampicillin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
21.5
ampicillin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
22
ampicillin
plasmid pBG66
-
pH and temperature not specified in the publication, mutant enzyme N170A
160
ampicillin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
190
ampicillin
pH not specified in the publication, 30°C, recombinant enzyme
220
ampicillin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
273
ampicillin
pH 7.2, 25°C, recombinant enzyme
357
ampicillin
-
pH and temperature not specified in the publication, OXA-1 beta-lactamase
408
ampicillin
pH 7.2, 25°C, recombinant enzyme
467
ampicillin
plasmid pBG66
-
pH and temperature not specified in the publication, mutant enzyme N170G
477
ampicillin
pH 7.2, 25°C, recombinant enzyme
544
ampicillin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
560
ampicillin
enzyme diluted in HEPES buffer containing 50 microM ZnCl2 supplemented with bovine serum albumin
724
ampicillin
pH 7.2, 25°C, recombinant enzyme
900
ampicillin
pH 7.2, 25°C, recombinant enzyme
1085
ampicillin
plasmid pBG66
-
pH and temperature not specified in the publication, wild-type enzyme
1375
ampicillin
pH 7.2, 25°C, recombinant enzyme
0.3
aztreonam
kcat less than 0.3/sec at 30°C in 100 mM sodium phosphate (pH 7)
0.0074
benzylpenicillin
30°C, pH 7.0
0.04
benzylpenicillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.08
benzylpenicillin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.1
benzylpenicillin
in 100 mM Tris-H2SO4, 300 mM K2SO4 (pH 7.0), at 30°C
0.13
benzylpenicillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.7
benzylpenicillin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
1.5
benzylpenicillin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
2.5
benzylpenicillin
plasmid pGEM-T-easy
-
mutant enzyme W154F, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
4
benzylpenicillin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
4.9
benzylpenicillin
at 25°C in 100 mM sodium phosphate (pH 7.0)
10.92
benzylpenicillin
in 30 mM sodium cacodylate buffer (pH 6.5) plus 0.05 mM ZnSO4
11
benzylpenicillin
30°C, pH not specified in the publication
13
benzylpenicillin
-
30°C, pH 7.0, plasmid-encoded, pBC3e, beta-lactamase CMY-1
14
benzylpenicillin
-
30°C, pH 7.0, plasmid-encoded, pBC2e, beta-lactamase MIR-1
14
benzylpenicillin
-
30°C, pH 7.0, plasmid-encoded, pBC4e, beta-lactamase CMY-2
18
benzylpenicillin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
20
benzylpenicillin
-
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
34.3
benzylpenicillin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
55
benzylpenicillin
-
30°C, pH 7.0, plasmid-encoded, pBC1e, beta-lactamase ACT-1
85
benzylpenicillin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
97
benzylpenicillin
at 30°C in 100 mM sodium phosphate (pH 7)
120
benzylpenicillin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
317
benzylpenicillin
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
0.004
carbenicillin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
0.52
carbenicillin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
10.22
carbenicillin
pH 8.0, 30°C, recombinant wild-type enzyme
16.96
carbenicillin
in 30 mM sodium cacodylate buffer (pH 6.5) plus 0.05 mM ZnSO4
440
cefalothin
enzyme diluted in HEPES buffer containing 50 microM ZnCl2 supplemented with bovine serum albumin
9
cefalotin
pH 7.2, 25°C, recombinant enzyme
18
cefalotin
pH 7.2, 25°C, recombinant enzyme
25
cefalotin
pH 7.2, 25°C, recombinant enzyme
45
cefalotin
pH 7.2, 25°C, recombinant enzyme
53
cefalotin
pH 7.2, 25°C, recombinant enzyme
63
cefalotin
pH 7.2, 25°C, recombinant enzyme
0.46
cefazolin
in 30 mM sodium cacodylate buffer (pH 6.5) plus 0.05 mM ZnSO4
40
cefepime
kcat above 40/sec at 30°C in 100 mM sodium phosphate (pH 7)
0.21
cefoperazone
pH 7.5, 25°C, recombinant His-tagged mutant E162A
0.705
cefoperazone
pH 7.5, 25°C, recombinant His-tagged mutant E164A
229.5
cefoperazone
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
0.004
cefotaxime
-
30°C, pH 7.0, plasmid-encoded, pBC4e, beta-lactamase CMY-2
0.01
cefotaxime
-
30°C, pH 7.0, plasmid-encoded, pBC3e, beta-lactamase CMY-1
0.032
cefotaxime
in 20 mM phosphate buffer, (pH 7.0) at 30°C
0.05
cefotaxime
-
30°C, pH 7.0, plasmid-encoded, pBC1e, beta-lactamase ACT-1
0.07
cefotaxime
in 20 mM phosphate buffer, (pH 7.0) at 30°C
0.09
cefotaxime
in 20 mM phosphate buffer, (pH 7.0) at 30°C
1.53
cefotaxime
in 30 mM sodium cacodylate buffer (pH 6.5) plus 0.05 mM ZnSO4
1.572
cefotaxime
pH 8.0, 30°C, recombinant wild-type enzyme
2.9
cefotaxime
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
56
cefotaxime
pH not specified in the publication, 30°C, recombinant enzyme
398
cefotaxime
enzyme diluted in HEPES buffer containing 50 microM ZnCl2 supplemented with bovine serum albumin
452
cefotaxime
pH and temperature not specified in the publication
0.01
cefoxitin
kcat less than 0.01/sec at 30°C in 100 mM sodium phosphate (pH 7)
3
cefoxitin
pH 7.2, 25°C, recombinant enzyme
4
cefoxitin
pH 7.2, 25°C, recombinant enzyme
6
cefoxitin
pH 7.2, 25°C, recombinant enzyme
7
cefoxitin
enzyme diluted in HEPES buffer containing 50 microM ZnCl2 supplemented with bovine serum albumin
14
cefoxitin
pH 7.2, 25°C, recombinant enzyme
18
cefoxitin
pH 7.2, 25°C, recombinant enzyme
1.3
ceftazidime
pH and temperature not specified in the publication
2 - 8
ceftazidime
pH 7.2, 25°C, recombinant enzyme
3.3
ceftazidime
kcat above than 3.3/sec at 30°C in 100 mM sodium phosphate (pH 7)
5
ceftazidime
pH 7.2, 25°C, recombinant enzyme
12
ceftazidime
enzyme diluted in HEPES buffer containing 50 microM ZnCl2 supplemented with bovine serum albumin
15
ceftazidime
pH 7.2, 25°C, recombinant enzyme
16
ceftazidime
pH 7.2, 25°C, recombinant enzyme
23
ceftazidime
pH 7.2, 25°C, recombinant enzyme
29
ceftazidime
pH 7.2, 25°C, recombinant enzyme
1.825
ceftriaxone
pH 8.0, 30°C, recombinant wild-type enzyme
0.017
cefuroxime
-
30°C, pH 7.0, plasmid-encoded, pBC4e, beta-lactamase CMY-2
0.02
cefuroxime
-
30°C, pH 7.0, plasmid-encoded, pBC3e, beta-lactamase CMY-1
0.12
cefuroxime
-
30°C, pH 7.0, plasmid-encoded, pBC1e, beta-lactamase ACT-1
286
cefuroxime
pH and temperature not specified in the publication
0.079
cephalexin
pH 8.0, 30°C, recombinant wild-type enzyme
1
cephalexin
plasmid pBG66
-
pH and temperature not specified in the publication, mutant enzyme N170A
13
cephalexin
plasmid pBG66
-
pH and temperature not specified in the publication, wild-type enzyme
16
cephalexin
plasmid pBG66
-
pH and temperature not specified in the publication, mutant enzyme N170G
31
cephalexin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
0.002
cephaloridine
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.0036
cephaloridine
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.004
cephaloridine
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.015
cephaloridine
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
1.3
cephaloridine
plasmid pGEM-T-easy
-
mutant enzyme W154F, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
16
cephaloridine
-
pH and temperature not specified in the publication, OXA-1 beta-lactamase
35
cephaloridine
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
70
cephaloridine
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
115
cephaloridine
at 30°C in 100 mM sodium phosphate (pH 7)
155
cephaloridine
-
30°C, pH 7.0, plasmid-encoded, pBC3e, beta-lactamase CMY-1
190
cephaloridine
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
215
cephaloridine
-
30°C, pH 7.0, plasmid-encoded, pBC2e, beta-lactamase MIR-1
215
cephaloridine
-
30°C, pH 7.0, plasmid-encoded, pBC4e, beta-lactamase CMY-2
0.0023
cephalothin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.003
cephalothin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.003
cephalothin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.012
cephalothin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.1
cephalothin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.15
cephalothin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.43
cephalothin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
0.44
cephalothin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
0.5
cephalothin
in 100 mM Tris-H2SO4, 300 mM K2SO4 (pH 7.0), at 30°C
1.031
cephalothin
pH 8.0, 30°C, recombinant wild-type enzyme
2
cephalothin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
2.5
cephalothin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
6
cephalothin
in 20 mM phosphate buffer, (pH 7.0) at 30°C
8
cephalothin
plasmid pGEM-T-easy
-
mutant enzyme W154F, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
14
cephalothin
in 20 mM phosphate buffer, (pH 7.0) at 30°C
31
cephalothin
plasmid pBG66
-
pH and temperature not specified in the publication, mutant enzyme N170G
49.7
cephalothin
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
60
cephalothin
pH not specified in the publication, 30°C, recombinant enzyme
113
cephalothin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
140
cephalothin
in 20 mM phosphate buffer, (pH 7.0) at 30°C
146
cephalothin
plasmid pBG66
-
pH and temperature not specified in the publication, wild-type enzyme
160
cephalothin
-
30°C, pH 7.0, plasmid-encoded, pBC2e, beta-lactamase MIR-1
160
cephalothin
-
30°C, pH 7.0, plasmid-encoded, pBC4e, beta-lactamase CMY-2
460
cephalothin
-
30°C, pH 7.0, plasmid-encoded, pBC1e, beta-lactamase ACT-1
480
cephalothin
-
30°C, pH 7.0, plasmid-encoded, pBC3e, beta-lactamase CMY-1
543
cephalothin
pH and temperature not specified in the publication
0.004
Cloxacillin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
0.2
Cloxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.42
Cloxacillin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
1.8
Cloxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154F, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
2.5
Cloxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
3.5
Cloxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
4
Cloxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
120
Cloxacillin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
500
Cloxacillin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
51
doripenem
pH not specified in the publication, 30°C, recombinant enzyme
75
doripenem
pH 7.2, 25°C, recombinant enzyme
170
doripenem
pH 7.2, 25°C, recombinant enzyme
267
doripenem
pH 7.2, 25°C, recombinant enzyme
348
doripenem
pH 7.2, 25°C, recombinant enzyme
743
doripenem
pH 7.2, 25°C, recombinant enzyme
1032
doripenem
pH 7.2, 25°C, recombinant enzyme
4.3
ertapenem
pH 7.2, 37°C, recombinant enzyme, in presence of NaCl
69
ertapenem
pH not specified in the publication, 30°C, recombinant enzyme
0.07
Imipenem
in 20 mM phosphate buffer, (pH 7.0) at 30°C
0.11
Imipenem
in 20 mM phosphate buffer, (pH 7.0) at 30°C
7.28
Imipenem
in 30 mM sodium cacodylate buffer (pH 6.5) plus 0.05 mM ZnSO4
54
Imipenem
pH 7.2, 25°C, recombinant enzyme
127
Imipenem
pH 7.2, 25°C, recombinant enzyme
214
Imipenem
enzyme diluted in HEPES buffer containing 50 microM ZnCl2 supplemented with bovine serum albumin
252
Imipenem
pH 7.2, 25°C, recombinant enzyme
312
Imipenem
pH not specified in the publication, 30°C, recombinant enzyme
332
Imipenem
pH 7.2, 25°C, recombinant enzyme
355
Imipenem
pH 7.2, 25°C, recombinant enzyme
757
Imipenem
pH 7.2, 25°C, recombinant enzyme
4.13
meropenem
in 30 mM sodium cacodylate buffer (pH 6.5) plus 0.05 mM ZnSO4
40
meropenem
enzyme diluted in HEPES buffer containing 50 microM ZnCl2 supplemented with bovine serum albumin
142
meropenem
pH 7.2, 25°C, recombinant enzyme
194
meropenem
pH 7.2, 25°C, recombinant enzyme
220
meropenem
pH not specified in the publication, 30°C, recombinant enzyme
238
meropenem
pH 7.2, 25°C, recombinant enzyme
362
meropenem
pH 7.2, 25°C, recombinant enzyme
413
meropenem
pH 7.2, 25°C, recombinant enzyme
583
meropenem
pH 7.2, 25°C, recombinant enzyme
0.01
moxalactam
kcat less than 0.01/sec at 30°C in 100 mM sodium phosphate (pH 7)
0.014
nitrocefin
pH 8.0, 30°C, recombinant wild-type enzyme
0.08
nitrocefin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
0.125
nitrocefin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
0.6
nitrocefin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
1
nitrocefin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
2
nitrocefin
plasmid pGEM-T-easy
-
mutant enzyme W154F, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
2.5
nitrocefin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
4
nitrocefin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
4.4
nitrocefin
in 30 mM sodium cacodylate buffer (pH 6.5) plus 0.05 mM ZnSO4
5.85
nitrocefin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
6
nitrocefin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
8
nitrocefin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
15
nitrocefin
pH 7.2, 25°C, recombinant enzyme
30
nitrocefin
pH 7.2, 25°C, recombinant enzyme
33
nitrocefin
pH 7.2, 25°C, recombinant enzyme
38
nitrocefin
pH 7.2, 25°C, recombinant enzyme
44
nitrocefin
pH 7.2, 25°C, recombinant enzyme
49
nitrocefin
pH 7.2, 25°C, recombinant enzyme
96
nitrocefin
-
pH and temperature not specified in the publication, OXA-1 beta-lactamase
330
nitrocefin
enzyme diluted in HEPES buffer containing 50 microM ZnCl2 supplemented with bovine serum albumin
550
nitrocefin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
1300
nitrocefin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
1700
nitrocefin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
2220
nitrocefin
-
30°C, pH 7.0, plasmid-encoded, pBC3e, beta-lactamase CMY-1
0.009
Oxacillin
-
30°C, pH 7.0, plasmid-encoded, pBC3e, beta-lactamase CMY-1
0.015
Oxacillin
-
30°C, pH 7.0, plasmid-encoded, pBC4e, beta-lactamase CMY-2
0.044
Oxacillin
-
30°C, pH 7.0, plasmid-encoded, pBC1e, beta-lactamase ACT-1
0.21
Oxacillin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
0.25
Oxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
2
Oxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154F, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
3.5
Oxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
4
Oxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
4.5
Oxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
35
Oxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
90
Oxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
300
Oxacillin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
577
Oxacillin
-
pH and temperature not specified in the publication, OXA-1 beta-lactamase
600
Oxacillin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
500
panipenem
pH not specified in the publication, 30°C, recombinant enzyme
0.32
penicillin G
mutant E166C, carrying 6-bromoacetyl-2-dimethylaminonaphthalene label, pH 7.0, 22°C
0.8
penicillin G
plasmid pBG66
-
pH and temperature not specified in the publication, mutant enzyme N166A/N170G
12.3
penicillin G
-
mutant R61H/E64H/43H, 25°C, pH not specified in the publication
24.8
penicillin G
-
mutant M182T/T195S/A224V, 25°C, pH not specified in the publication
27.6
penicillin G
pH 8.0, 30°C, recombinant wild-type enzyme
31
penicillin G
pH and temperature not specified in the publication
45
penicillin G
plasmid pBG66
-
pH and temperature not specified in the publication, mutant enzyme N170A
64
penicillin G
plasmid pBG66
-
pH and temperature not specified in the publication, mutant enzyme N170G
950
penicillin G
plasmid pBG66
-
pH and temperature not specified in the publication, wild-type enzyme
0.5
piperacillin
in 100 mM Tris-H2SO4, 300 mM K2SO4 (pH 7.0), at 30°C
2.2
piperacillin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
2.46
piperacillin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
4
piperacillin
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
8
piperacillin
pH and temperature not specified in the publication
9
piperacillin
pH not specified in the publication, 30°C, recombinant enzyme
14.61
piperacillin
in 30 mM sodium cacodylate buffer (pH 6.5) plus 0.05 mM ZnSO4
22.02
piperacillin
pH 8.0, 30°C, recombinant wild-type enzyme
328
piperacillin
enzyme diluted in HEPES buffer containing 50 microM ZnCl2 supplemented with bovine serum albumin
677
piperacillin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
3.3
Sulbactam
in 30 mM sodium cacodylate buffer (pH 6.5) plus 0.05 mM ZnSO4
8.2
tazobactam
enzyme diluted in HEPES buffer containing 50 microM ZnCl2 supplemented with bovine serum albumin
0.1
ticarcillin
in 100 mM Tris-H2SO4, 300 mM K2SO4 (pH 7.0), at 30°C
1.722
ticarcillin
pH 8.0, 30°C, recombinant wild-type enzyme
190
ticarcillin
pH not specified in the publication, 30°C, recombinant enzyme
additional information
aztreonam
unable to determine as Km is too high
additional information
cefepime
above 8, enzyme diluted in HEPES buffer containing 50 microM ZnCl2 supplemented with bovine serum albumin
additional information
cefepime
-
above 8, enzyme diluted in HEPES buffer containing 50 microM ZnCl2 supplemented with bovine serum albumin
additional information
ertapenem
above 25, enzyme diluted in HEPES buffer containing 50 microM ZnCl2 supplemented with bovine serum albumin
additional information
ertapenem
-
above 25, enzyme diluted in HEPES buffer containing 50 microM ZnCl2 supplemented with bovine serum albumin
additional information
additional information
no hydrolysis detected with enzyme concentrations up to 4 microM for temocillin, cefepime, imipenem, and aztreonam
-
additional information
additional information
-
no hydrolysis detected with enzyme concentrations up to 4 microM for temocillin, cefepime, imipenem, and aztreonam
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.16 - 3700
(6R,7R)-3-[(acetyloxy)methyl]-7-(formylamino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
1.1
(6R,7R)-3-[(acetyloxy)methyl]-7-(hydroxyamino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
1.59
(6R,7R)-3-[(acetyloxy)methyl]-7-amino-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
1.38
(6R,7R)-3-[(acetyloxy)methyl]-7-[formyl(hydroxy)amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
2.02 - 100
(6R,7R)-3-[(acetyloxy)methyl]-7-[hydroxy(phenylacetyl)amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
85.1 - 45000
(6R,7R)-3-[(acetyloxy)methyl]-8-oxo-7-[(thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
7.01
(6R,7Z)-3-[(acetyloxy)methyl]-7-(hydroxyimino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
120
(6R,7Z)-7-(hydroxyimino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate 5,5-dioxide
-
pH and temperature not specified in the publication
7.9
3-([3-dibenzylamino-3-oxopropanoyl]oxy)benzoic acid
pH 7.5, 25°C
0.47
3-([3-[benzyl(methyl)amino]-3-oxopropanoyl]oxy)benzoic acid
pH 7.5, 25°C
245
3-([[(2R)-3-(benzylamino)-2-methyl-3-oxopropanoyl]oxy]methyl)benzoic acid
pH 7.5, 25°C
21.3
3-([[(2S)-3-(benzylamino)-2-methyl-3-oxopropanoyl]oxy]methyl)benzoic acid
pH 7.5, 25°C
2.36
3-([[2-benzyl-3-oxo-3-(benzylamino)propanoyl]oxy]methyl)benzoic acid
pH 7.5, 25°C
109
3-nitrophenyl (2S)-2-hydroxy-3-phenylpropanoate
pH not specified in the publication, temperature not specified in the publication
69
3-[[(2S)-2-hydroxy-3-phenylpropanoyl]oxy]benzoic acid
pH not specified in the publication, temperature not specified in the publication
17.4
benzyl [[(2R)-2-hydroxy-3-phenylpropanoyl]oxy]carbamate
pH not specified in the publication, temperature not specified in the publication
7.5
benzyl [[(2S)-2-hydroxy-2-phenylacetyl]oxy]carbamate
pH not specified in the publication, temperature not specified in the publication
120
benzyl [[(2S)-2-hydroxy-3-phenylpropanoyl]oxy]carbamate
pH not specified in the publication, temperature not specified in the publication
55
benzyl [[(2S)-2-hydroxy-4-phenylbutanoyl]oxy]carbamate
pH not specified in the publication, temperature not specified in the publication
2.8
benzyl [[(2S)-2-hydroxypropanoyl]oxy]carbamate
pH not specified in the publication, temperature not specified in the publication
3.16
(6R,7R)-3-[(acetyloxy)methyl]-7-(formylamino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
3700
(6R,7R)-3-[(acetyloxy)methyl]-7-(formylamino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
2.02
(6R,7R)-3-[(acetyloxy)methyl]-7-[hydroxy(phenylacetyl)amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
100
(6R,7R)-3-[(acetyloxy)methyl]-7-[hydroxy(phenylacetyl)amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
85.1
(6R,7R)-3-[(acetyloxy)methyl]-8-oxo-7-[(thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
45000
(6R,7R)-3-[(acetyloxy)methyl]-8-oxo-7-[(thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
43.96
amoxicillin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
49.51
amoxicillin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
272.7
amoxicillin
pH 8.0, 30°C, recombinant wild-type enzyme
1050
amoxicillin
pH and temperature not specified in the publication
36334.3
amoxicillin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
0.056
ampicillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
1.15
ampicillin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
3.3
ampicillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
12
ampicillin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
13
ampicillin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
19
ampicillin
plasmid pGEM-T-easy
-
mutant enzyme W154F, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
34.96
ampicillin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
36.23
ampicillin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
120
ampicillin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
900
ampicillin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
1008.4
ampicillin
pH 8.0, 30°C, recombinant wild-type enzyme
1200
ampicillin
pH 7.2, 25°C, recombinant enzyme
2300
ampicillin
pH 7.2, 25°C, recombinant enzyme
2600
ampicillin
pH 7.2, 25°C, recombinant enzyme
2800
ampicillin
pH 7.2, 25°C, recombinant enzyme
2900
ampicillin
pH 7.2, 25°C, recombinant enzyme
3000
ampicillin
pH 7.2, 25°C, recombinant enzyme
5578
ampicillin
-
pH and temperature not specified in the publication, OXA-1 beta-lactamase
6200
ampicillin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
8100
ampicillin
pH not specified in the publication, 30°C, recombinant enzyme
17000
ampicillin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
29000
ampicillin
plasmid pBG66
-
pH and temperature not specified in the publication, wild-type enzyme
0.067
benzylpenicillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
0.53
benzylpenicillin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
13
benzylpenicillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
25
benzylpenicillin
plasmid pGEM-T-easy
-
mutant enzyme W154F, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
57
benzylpenicillin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
80
benzylpenicillin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
130
benzylpenicillin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
150
benzylpenicillin
30°C, pH not specified in the publication
1500
benzylpenicillin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
6000
benzylpenicillin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
470.1
carbenicillin
pH 8.0, 30°C, recombinant wild-type enzyme
1500
cefalotin
pH 7.2, 25°C, recombinant enzyme
1600
cefalotin
pH 7.2, 25°C, recombinant enzyme
1900
cefalotin
pH 7.2, 25°C, recombinant enzyme
4100
cefalotin
pH 7.2, 25°C, recombinant enzyme
4600
cefalotin
pH 7.2, 25°C, recombinant enzyme
6100
cefalotin
pH 7.2, 25°C, recombinant enzyme
5.48
cefoperazone
pH 7.5, 25°C, recombinant His-tagged mutant E162A
7.33
cefoperazone
pH 7.5, 25°C, recombinant His-tagged mutant E164A
3998.3
cefoperazone
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
4.31
cefotaxime
pH 8.0, 30°C, recombinant wild-type enzyme
900
cefotaxime
pH not specified in the publication, 30°C, recombinant enzyme
5250
cefotaxime
pH and temperature not specified in the publication
130
cefoxitin
pH 7.2, 25°C, recombinant enzyme
140
cefoxitin
pH 7.2, 25°C, recombinant enzyme
150
cefoxitin
pH 7.2, 25°C, recombinant enzyme
170
cefoxitin
pH 7.2, 25°C, recombinant enzyme
180
cefoxitin
pH 7.2, 25°C, recombinant enzyme
220
cefoxitin
pH 7.2, 25°C, recombinant enzyme
40
ceftazidime
pH and temperature not specified in the publication
180
ceftazidime
pH 7.2, 25°C, recombinant enzyme
200
ceftazidime
pH 7.2, 25°C, recombinant enzyme
210
ceftazidime
pH 7.2, 25°C, recombinant enzyme
260
ceftazidime
pH 7.2, 25°C, recombinant enzyme
155.2
ceftriaxone
pH 8.0, 30°C, recombinant wild-type enzyme
11910
cefuroxime
pH and temperature not specified in the publication
8.81
cephalexin
pH 8.0, 30°C, recombinant wild-type enzyme
10
cephalexin
plasmid pBG66
-
pH and temperature not specified in the publication, wild-type enzyme
0.03
cephaloridine
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
10
cephaloridine
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
12
cephaloridine
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
16
cephaloridine
plasmid pGEM-T-easy
-
mutant enzyme W154F, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
18
cephaloridine
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
23
cephaloridine
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
180
cephaloridine
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
200
cephaloridine
-
pH and temperature not specified in the publication, OXA-1 beta-lactamase
0.014
cephalothin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.25
cephalothin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
1.57
cephalothin
pH 8.0, 30°C, recombinant wild-type enzyme
1.89
cephalothin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
5
cephalothin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
7.72
cephalothin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
14
cephalothin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
20
cephalothin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
35
cephalothin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
320
cephalothin
plasmid pGEM-T-easy
-
mutant enzyme W154F, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
380
cephalothin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
400
cephalothin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
800
cephalothin
plasmid pBG66
-
pH and temperature not specified in the publication, wild-type enzyme
2511.1
cephalothin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
8900
cephalothin
pH not specified in the publication, 30°C, recombinant enzyme
25860
cephalothin
pH and temperature not specified in the publication
2
Cloxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
12
Cloxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154F, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
13
Cloxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
18
Cloxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
47
Cloxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
1000
Cloxacillin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
2000
Cloxacillin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
1700
doripenem
pH 7.2, 25°C, recombinant enzyme
2000
doripenem
pH 7.2, 25°C, recombinant enzyme
4500
doripenem
pH 7.2, 25°C, recombinant enzyme
5400
doripenem
pH 7.2, 25°C, recombinant enzyme
6000
doripenem
pH 7.2, 25°C, recombinant enzyme
6800
doripenem
pH not specified in the publication, 30°C, recombinant enzyme
8600
doripenem
pH 7.2, 25°C, recombinant enzyme
250
ertapenem
pH 7.2, 37°C, recombinant enzyme, in presence of NaCl
15000
ertapenem
pH not specified in the publication, 30°C, recombinant enzyme
2200
Imipenem
pH 7.2, 25°C, recombinant enzyme
2300
Imipenem
pH 7.2, 25°C, recombinant enzyme
2900
Imipenem
pH 7.2, 25°C, recombinant enzyme
4100
Imipenem
pH 7.2, 25°C, recombinant enzyme
5800
Imipenem
pH 7.2, 25°C, recombinant enzyme
6000
Imipenem
pH not specified in the publication, 30°C, recombinant enzyme
9200
Imipenem
pH 7.2, 25°C, recombinant enzyme
2600
meropenem
pH 7.2, 25°C, recombinant enzyme
4100
meropenem
pH 7.2, 25°C, recombinant enzyme
4200
meropenem
pH 7.2, 25°C, recombinant enzyme
4300
meropenem
pH 7.2, 25°C, recombinant enzyme
4900
meropenem
pH 7.2, 25°C, recombinant enzyme
7400
meropenem
pH 7.2, 25°C, recombinant enzyme
14000
meropenem
pH not specified in the publication, 30°C, recombinant enzyme
0.21
nitrocefin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
0.3
nitrocefin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
0.66
nitrocefin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
1.48
nitrocefin
pH 8.0, 30°C, recombinant wild-type enzyme
5.5
nitrocefin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
30
nitrocefin
plasmid pGEM-T-easy
-
mutant enzyme W154F, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
40
nitrocefin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
100
nitrocefin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
130
nitrocefin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
130
nitrocefin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
190
nitrocefin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
3100
nitrocefin
pH 7.2, 25°C, recombinant enzyme
5600
nitrocefin
pH 7.2, 25°C, recombinant enzyme
6100
nitrocefin
pH 7.2, 25°C, recombinant enzyme
6300
nitrocefin
pH 7.2, 25°C, recombinant enzyme
7500
nitrocefin
pH 7.2, 25°C, recombinant enzyme
10450
nitrocefin
-
pH and temperature not specified in the publication, OXA-1 beta-lactamase
10900
nitrocefin
pH 7.2, 25°C, recombinant enzyme
52000
nitrocefin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
170000
nitrocefin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
4.2
Oxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
16
Oxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154F, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
17.5
Oxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
40
Oxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154G, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
53
Oxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
130
Oxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154A, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
700
Oxacillin
plasmid pGEM-T-easy
-
mutant enzyme W154H, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
3000
Oxacillin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate
3000
Oxacillin
plasmid pGEM-T-easy
-
wild-type, 25°C, pH 7, in presence of 50 mM sodium bicarbonate
18610
Oxacillin
-
pH and temperature not specified in the publication, OXA-1 beta-lactamase
4900
panipenem
pH not specified in the publication, 30°C, recombinant enzyme
40
penicillin G
mutant E166C, carrying 6-bromoacetyl-2-dimethylaminonaphthalene label, pH 7.0, 22°C
210
penicillin G
-
mutant R61H/E64H/43H, 25°C, pH not specified in the publication
437
penicillin G
-
mutant M182T/T195S/A224V, 25°C, pH not specified in the publication
3870
penicillin G
pH and temperature not specified in the publication
8238.8
penicillin G
pH 8.0, 30°C, recombinant wild-type enzyme
34000
penicillin G
plasmid pBG66
-
pH and temperature not specified in the publication, wild-type enzyme
30.73
piperacillin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
44.17
piperacillin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
170
piperacillin
pH not specified in the publication, 30°C, recombinant enzyme
1140
piperacillin
pH and temperature not specified in the publication
1753.2
piperacillin
pH 8.0, 30°C, recombinant wild-type enzyme
11672.4
piperacillin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
217.4
ticarcillin
pH 8.0, 30°C, recombinant wild-type enzyme
360
ticarcillin
pH and temperature not specified in the publication
390
ticarcillin
pH not specified in the publication, 30°C, recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00374
(2Z)-2-(((E)-2-carboxy-2-[(2-thienylacetyl)amino]vinyl)imino)-3-mercaptobut-3-enoic acid
-
-
0.000033
([[(2-ethoxynaphthalen-1-yl)carbonyl]amino]methyl)boronic acid
pH 6.5, 22°C
0.029
2-(7-(4-methoxyphenyl)-5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidin-4-ylidene)-malononitrile
-
pH 7.0, temperature not specified in the publication
0.00051 - 0.00064
2-[[5-(2-hydroxyphenyl)-1,3,4-thiadiazol-2-yl]sulfanyl]-N-phenylacetamide
0.000073 - 0.0022
2-[[5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-yl]sulfanyl]-N-phenylacetamide
0.086
3-aminophenyl boronic acid
-
30°C, pH 7.0, plasmid-encoded, pBC1e, beta-lactamase ACT-1
0.000001
3-[(2R)-2-(dihydroxyboranyl)-2-[[(thiophen-2-ylmethyl)sulfonyl]amino]ethyl]benzoic acid
pH 6.5, 22°C
0.00043
3-[(2R)-2-[(benzylsulfonyl)amino]-2-(dihydroxyboranyl)ethyl]benzoic acid
pH 6.5, 22°C
0.000025
4-([[(dihydroxyboranyl)methyl]sulfamoyl]methyl)benzoic acid
pH 6.5, 22°C
0.012
4-chloro-7-(4-methoxyphenyl)-5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidine
-
pH 7.0, temperature not specified in the publication
0.019
4-chloro-7-(4-methylphenyl)-5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidine
-
pH 7.0, temperature not specified in the publication
0.033
4-chloro-7-(4-methylphenyl)-5-phenyl-7H-pyrrolo[2,3-d]pyrimidine
-
pH 7.0, temperature not specified in the publication
0.015
7-(4-methylphenyl)-8,9-diphenyl-7H-pyrrolo[3,2-e][1,2,4]triazolo[4,3-c]pyrimidine-3-thione
-
pH 7.0, temperature not specified in the publication
0.056
N(2-mercaptoethyl)phenylacetamide
-
pH 7.0, 30°C, 1.0 M NaCl, 0.002 mM Zn2+
0.00065 - 0.015
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
0.00081 - 0.0018
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
0.00025 - 0.0063
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
0.001
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.0014
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.00086 - 0.0053
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
0.00082 - 0.045
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
0.00033 - 0.0068
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
0.00034 - 0.0085
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
0.018
N-benzylidene-N'-(7-(4-methylphenyl)-5,6-diphenyl-7Hpyrrolo[2,3-d]pyramidin-4-yl)-hydrazine
-
pH 7.0, temperature not specified in the publication
0.003
N-carbobenzoxy-D-cysteinyl-D-phenylalanine
-
pH 7.0, 30°C, 1.0 M NaCl, 0.002 mM Zn2+
-
0.011
N-carbobenzoxy-D-cysteinyl-L-phenylalanine
-
pH 7.0, 30°C, 1.0 M NaCl, 0.002 mM Zn2+
-
0.046
N-carbobenzoxy-DL-cysteinyl-glycine
-
pH 7.0, 30°C, 1.0 M NaCl, 0.002 mM Zn2+
-
0.009
N-carbobenzoxy-L-cysteinyl-D-phenylalanine
-
pH 7.0, 30°C, 1.0 M NaCl, 0.002 mM Zn2+
-
0.062
N-carbobenzoxy-L-cysteinyl-DL-alanine
-
pH 7.0, 30°C, 1.0 M NaCl, 0.002 mM Zn2+
-
0.017
N-carbobenzoxy-L-cysteinyl-DL-phenylalanine
-
pH 7.0, 30°C, 1.0 M NaCl, 0.002 mM Zn2+
-
0.095
N-carbobenzoxy-L-cysteinyl-DL-proline
-
pH 7.0, 30°C, 1.0 M NaCl, 0.002 mM Zn2+
-
0.073
N-carbobenzoxy-L-cysteinyl-DL-serine
-
pH 7.0, 30°C, 1.0 M NaCl, 0.002 mM Zn2+
-
0.048
N-carbobenzoxy-L-cysteinyl-DL-valine
-
pH 7.0, 30°C, 1.0 M NaCl, 0.002 mM Zn2+
-
0.042
N-carbobenzoxy-L-cysteinyl-glycine
-
pH 7.0, 30°C, 1.0 M NaCl, 0.002 mM Zn2+
-
0.136
N-carbobenzoxy-L-cysteinyl-L-leucine
-
pH 7.0, 30°C, 1.0 M NaCl, 0.002 mM Zn2+
-
0.027
N-carbobenzoxy-L-cysteinyl-L-phenylalanine
-
pH 7.0, 30°C, 1.0 M NaCl, 0.002 mM Zn2+
-
0.084
N-carbobenzoxy-L-cysteinyl-L-serine
-
pH 7.0, 30°C, 1.0 M NaCl, 0.002 mM Zn2+
-
0.515
N-phenylacetyl-DL-penicillamine
-
pH 7.0, 30°C, 1.0 M NaCl, 0.002 mM Zn2+
0.07 - 1.5
sodium benzyl [2-oxo-2-(2-oxo-2,3-dihydro-1,3-benzoxazol-6-yl)ethyl]phosphonate
0.43 - 1
sodium benzyl {2-[3-(2-chlorophenyl)-5-methyl-1,2-oxazol-4-yl]-2-oxoethyl}phosphonate
5.5
thiono derivative of N-(phenylacetyl)thioglycylglycolic acid
-
pH 7.5, 25°C
-
0.01
vanadate/2,3,5,6-tetrahydroxycyclohexa-2,5-diene-1,4-dione complex
pH 7.0, 25°C
0.00065
vanadate/2,3-dihydroxynaphthalene-1,4-dione complex
pH 7.0, 25°C
0.0019
vanadate/3,4,5,6-tetrafluorobenzene-1,2-diol complex
pH 7.0, 25°C
0.0016
vanadate/4-methoxybenzohydroxamic acid complex
pH 7.5, 25°C
-
0.00048
vanadate/4-nitrobenzohydroxamic acid complex
pH 7.5, 25°C
-
0.00115
vanadate/N-methylbenzohydroxamic acid complex
pH 7.5, 25°C
-
0.0057
2-picolinic acid
wild type enzyme, in 20 mM sodium cacodylate buffer, pH 6.5
0.013
2-picolinic acid
mutant enzyme N116H/N220G, in 20 mM sodium cacodylate buffer, pH 6.5
0.00034
2-[[5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-yl]sulfanyl]-N-phenylacetamide
pH and temperature not specified in the publication
0.0006
2-[[5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-yl]sulfanyl]-N-phenylacetamide
pH and temperature not specified in the publication
0.0033
2-[[5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-yl]sulfanyl]-N-phenylacetamide
pH and temperature not specified in the publication
0.052
2-[[5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-yl]sulfanyl]-N-phenylacetamide
pH and temperature not specified in the publication
0.00051
2-[[5-(2-hydroxyphenyl)-1,3,4-thiadiazol-2-yl]sulfanyl]-N-phenylacetamide
pH and temperature not specified in the publication
0.00064
2-[[5-(2-hydroxyphenyl)-1,3,4-thiadiazol-2-yl]sulfanyl]-N-phenylacetamide
pH and temperature not specified in the publication
0.000073
2-[[5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-yl]sulfanyl]-N-phenylacetamide
pH and temperature not specified in the publication
0.0003
2-[[5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-yl]sulfanyl]-N-phenylacetamide
pH and temperature not specified in the publication
0.00043
2-[[5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-yl]sulfanyl]-N-phenylacetamide
pH and temperature not specified in the publication
0.0022
2-[[5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-yl]sulfanyl]-N-phenylacetamide
pH and temperature not specified in the publication
3.6
aztreonam
inhibitor binding constant (Ki) using 10 microM nitrocefin as indicator substrate
0.0000005
beta-lactamase inhibitor protein
wild-type inhibitor protein, pH 7.5, 25°C
-
0.0000024
beta-lactamase inhibitor protein
-
wild-type inhibitor protein, pH 7.5, 25°C
-
0.0000025
beta-lactamase inhibitor protein
-
wild-type inhibitor protein, pH 7.5, 25°C
-
0.0011
beta-lactamase inhibitor protein
wild-type inhibitor protein, pH 7.5, 25°C
-
0.019
clavulanic acid
-
pH and temperature not specified in the publication, OXA-10 beta-lactamase
0.104
clavulanic acid
-
pH and temperature not specified in the publication, OXA-10 beta-lactamase
0.195
clavulanic acid
-
pH and temperature not specified in the publication
0.195
clavulanic acid
-
pH and temperature not specified in the publication, OXA-1 beta-lactamase
0.009
Cys-Val-His-Ser-Pro-Asn-Arg-Glu-Cys
-
30°C, pH 8.0, uncompetitive
0.016
Cys-Val-His-Ser-Pro-Asn-Arg-Glu-Cys
-
30°C, pH 8.0, competitive
0.93
ethyl 3-(benzyloxycarbonyl)amino-2-oxo-1,1-difluoropropylphosphonate
-
-
0.95
ethyl 3-(benzyloxycarbonyl)amino-2-oxo-1,1-difluoropropylphosphonate
-
-
0.0014
JDB/ASR-II-292
-
pH and temperature not specified in the publication
0.0014
JDB/ASR-II-292
-
pH and temperature not specified in the publication, OXA-1 beta-lactamase
0.004
JDB/ASR-II-292
-
pH and temperature not specified in the publication, OXA-10 beta-lactamase
0.017
JDB/ASR-II-292
-
pH and temperature not specified in the publication, OXA-10 beta-lactamase
0.0007
JDB/LN-1-255
-
pH and temperature not specified in the publication, OXA-1 beta-lactamase
0.0014
JDB/LN-1-255
-
pH and temperature not specified in the publication, OXA-10 beta-lactamase
0.008
JDB/LN-1-255
-
pH and temperature not specified in the publication, OXA-10 beta-lactamase
0.00065
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.0061
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.007
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.015
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.00081
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.0018
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.00025
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.00035
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.0063
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.00086
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.0053
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.00082
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.0011
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.045
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.00033
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.0068
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.00034
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.00075
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.0056
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.0085
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.00023
N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.00043
N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.00051
N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.00038
N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.00039
N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.0012
N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.00025
N-phenyl-2-[[5-(pyridin-4-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.00042
N-phenyl-2-[[5-(pyridin-4-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.00054
N-phenyl-2-[[5-(pyridin-4-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.0013
N-phenyl-2-[[5-(pyridin-4-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.0043
N-phenyl-2-[[5-(pyridin-4-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.079
nitrocefin
pH 7.2, 25°C, recombinant enzyme
0.102
nitrocefin
pH 7.2, 25°C, recombinant enzyme
0.139
nitrocefin
pH 7.2, 25°C, recombinant enzyme
0.146
nitrocefin
pH 7.2, 25°C, recombinant enzyme
0.00003
penem 1
pH 7.2, temperature not specified in the publication, recombinant enzyme
0.00005
penem 1
pH 7.2, temperature not specified in the publication, recombinant enzyme
0.00015
penem 3
pH 7.2, temperature not specified in the publication, recombinant enzyme
0.00038
penem 3
pH 7.2, temperature not specified in the publication, recombinant enzyme
0.0045
pyridine-2,4-dicarboxylic acid
wild type enzyme, in 20 mM sodium cacodylate buffer, pH 6.5
0.028
pyridine-2,4-dicarboxylic acid
mutant enzyme N116H/N220G, in 20 mM sodium cacodylate buffer, pH 6.5
0.44
sodium benzyl (2-hydroxy-2-phenylethyl)phosphonate
pH 7.5, 25°C
1
sodium benzyl (2-hydroxy-2-phenylethyl)phosphonate
pH 7.5, 25°C
1.08
sodium benzyl (2-hydroxy-2-phenylethyl)phosphonate
pH 7.5, 25°C
0.15
sodium benzyl (2-oxo-2-phenylethyl)phosphonate
pH 7.5, 25°C
0.64
sodium benzyl (2-oxo-2-phenylethyl)phosphonate
pH 7.5, 25°C
1
sodium benzyl (2-oxo-2-phenylethyl)phosphonate
above, pH 7.5, 25°C
0.024
sodium benzyl 2-(1',3'-benzothiazol-2'-yl)-2-oxo-ethylphosphonate
pH 7.5, 25°C
0.17
sodium benzyl 2-(1',3'-benzothiazol-2'-yl)-2-oxo-ethylphosphonate
pH 7.5, 25°C
3600
sodium benzyl 2-(1',3'-benzothiazol-2'-yl)-2-oxo-ethylphosphonate
pH 7.5, 25°C
0.26
sodium benzyl [2-(biphenyl-4-yl)-2-hydroxyethyl]phosphonate
pH 7.5, 25°C
0.3
sodium benzyl [2-(biphenyl-4-yl)-2-hydroxyethyl]phosphonate
pH 7.5, 25°C
1
sodium benzyl [2-(biphenyl-4-yl)-2-hydroxyethyl]phosphonate
pH 7.5, 25°C
0.19
sodium benzyl [2-(biphenyl-4-yl)-2-oxoethyl]phosphonate
pH 7.5, 25°C
0.23
sodium benzyl [2-(biphenyl-4-yl)-2-oxoethyl]phosphonate
pH 7.5, 25°C
1
sodium benzyl [2-(biphenyl-4-yl)-2-oxoethyl]phosphonate
pH 7.5, 25°C
1
sodium benzyl [2-(biphenyl-4-yl)-2-oxoethyl]phosphonate
above, pH 7.5, 25°C
0.07
sodium benzyl [2-oxo-2-(2-oxo-2,3-dihydro-1,3-benzoxazol-6-yl)ethyl]phosphonate
pH 7.5, 25°C
0.27
sodium benzyl [2-oxo-2-(2-oxo-2,3-dihydro-1,3-benzoxazol-6-yl)ethyl]phosphonate
pH 7.5, 25°C
1.5
sodium benzyl [2-oxo-2-(2-oxo-2,3-dihydro-1,3-benzoxazol-6-yl)ethyl]phosphonate
pH 7.5, 25°C
0.43
sodium benzyl {2-[3-(2-chlorophenyl)-5-methyl-1,2-oxazol-4-yl]-2-oxoethyl}phosphonate
pH 7.5, 25°C
1
sodium benzyl {2-[3-(2-chlorophenyl)-5-methyl-1,2-oxazol-4-yl]-2-oxoethyl}phosphonate
pH 7.5, 25°C
1
sodium benzyl {2-[3-(2-chlorophenyl)-5-methyl-1,2-oxazol-4-yl]-2-oxoethyl}phosphonate
above, pH 7.5, 25°C
0.2
sodium biphenyl-4-ylmethyl (2-oxo-2-phenylethyl)phosphonate
pH 7.5, 25°C
1
sodium biphenyl-4-ylmethyl (2-oxo-2-phenylethyl)phosphonate
above, pH 7.5, 25°C
0.006
sodium biphenyl-4-ylmethyl [2-(biphenyl-4-yl)-2-oxoethyl]phosphonate
pH 7.5, 25°C
0.074
sodium biphenyl-4-ylmethyl [2-(biphenyl-4-yl)-2-oxoethyl]phosphonate
pH 7.5, 25°C
0.2
sodium biphenyl-4-ylmethyl [2-(biphenyl-4-yl)-2-oxoethyl]phosphonate
pH 7.5, 25°C
1
sodium phenyl (2-oxo-2-phenylethyl)phosphonate
above, pH 7.5, 25°C
1.05
sodium phenyl (2-oxo-2-phenylethyl)phosphonate
pH 7.5, 25°C
0.1
sodium phenyl [2-(biphenyl-4-yl)-2-oxoethyl]phosphonate
pH 7.5, 25°C
0.14
sodium phenyl [2-(biphenyl-4-yl)-2-oxoethyl]phosphonate
pH 7.5, 25°C
0.92
sodium phenyl [2-(biphenyl-4-yl)-2-oxoethyl]phosphonate
pH 7.5, 25°C
0.35
sodium phenyl [2-oxo-2-(pentafluorophenyl)ethyl]phosphonate
pH 7.5, 25°C
0.38
sodium phenyl [2-oxo-2-(pentafluorophenyl)ethyl]phosphonate
pH 7.5, 25°C
0.475
sodium phenyl [2-oxo-2-(pentafluorophenyl)ethyl]phosphonate
pH 7.5, 25°C
1
sodium phenyl [2-oxo-2-(pentafluorophenyl)ethyl]phosphonate
above, pH 7.5, 25°C
0.03
tazobactam
-
pH and temperature not specified in the publication, OXA-10 beta-lactamase
0.17
tazobactam
-
pH and temperature not specified in the publication, OXA-10 beta-lactamase
0.585
tazobactam
-
pH and temperature not specified in the publication, OXA-1 beta-lactamase
0.0109
vanadate/(3,4-dihydroxyphenyl)methanaminium complex
pH 7.0, 25°C
0.0042
vanadate/2-(3,4-dihydroxyphenyl)acetate complex
pH 7.0, 25°C
0.00043
vanadate/3-phenylcatechol complex
most effective, pH 7.0, 25°C
additional information
additional information
inhibition kinetics
-
additional information
additional information
-
Ki for diverse mutants of beta-lactamase inhibitor protein BLIP, overview
-
additional information
additional information
-
Ki for diverse mutants of beta-lactamase inhibitor protein BLIP, overview
-
additional information
additional information
Ki for diverse mutants of beta-lactamase inhibitor protein BLIP, overview
-
additional information
additional information
Ki for diverse mutants of beta-lactamase inhibitor protein BLIP, overview
-
additional information
additional information
-
Ki for (2R,3E)-2-([amino(phenyl)acetyl]amino)-3-[(1,2-dihydroxy-3-mercaptoprop-1-en-1-yl)imino]propanoic acid is less than 40 nM
-
additional information
additional information
-
inhibition kinetic analysis, overview
-
additional information
additional information
-
inhibition kinetics and mechanism, modeling, overview
-
additional information
additional information
kinetics of BlaMab inhibition by avibactam., overview
-
additional information
additional information
-
kinetics of BlaMab inhibition by avibactam., overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00175
3'-hydroxybiphenyl-2,3-dicarboxylic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.013
3-(3-hydroxypropyl)benzene-1,2-dicarboxylic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.16
3-methylbenzene-1,2-dicarboxylic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.00155
4'-hydroxybiphenyl-2,3-dicarboxylic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.00057
4,7-dichlorobenzothien-2-yl-sulfonylaminomethylboronic acid
Klebsiella pneumoniae
pH not specified in the publication, temperature not specified in the publication
0.016
4-butyl-3-methylbenzene-1,2-dicarboxylic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.243
4-butylbenzene-1,2-dicarboxylic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.207
biphenyl-2,2',3-tricarboxylic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0179
biphenyl-2,3,3'-tricarboxylic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.00225
biphenyl-2,3,4'-tricarboxylic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.000968
biphenyl-2,3-dicarboxylic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
2000
NaCl
Brachyspira pilosicoli
IC50 above 2000 mM, at 25°C in 100 mM sodium phosphate (pH 7.0)
0.00244
trisodium 2'-oxidobiphenyl-2,3-dicarboxylate
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0011
4,7-dichloro benzothien-2-yl sulfonylaminomethyl boronic acid
Pseudomonas aeruginosa
pH not specified in the publication, temperature not specified in the publication
0.0056
4,7-dichloro benzothien-2-yl sulfonylaminomethyl boronic acid
Acinetobacter baumannii
pH not specified in the publication, temperature not specified in the publication
0.000085
clavulanic acid
Alkalihalobacillus clausii
using cephalothin as a substrate, at 30°C
0.002
clavulanic acid
Brachyspira pilosicoli
at 25°C in 100 mM sodium phosphate (pH 7.0)
0.0063
N-[2-(7-chloro-quinolin-4-ylamino)-ethyl]-3-mercapto-propionamide
Pseudomonas aeruginosa
-
IC50: 0.0063 mM
0.0142
N-[2-(7-chloro-quinolin-4-ylamino)-ethyl]-3-mercapto-propionamide
Serratia marcescens
-
IC50: 0.0142 mM
0.0065
N-[3-(7-chloro-quinolin-4-ylamino)-propyl]-3-mercapto-propionamide
Pseudomonas aeruginosa
-
IC50: 0.0065 mM
0.0066
N-[3-(7-chloro-quinolin-4-ylamino)-propyl]-3-mercapto-propionamide
Serratia marcescens
-
IC50: 0.0066 mM
0.0024
N-[4-(7-chloro-quinolin-4-ylamino)-butyl]-3-mercapto-propionamide
Pseudomonas aeruginosa
-
IC50: 0.0024 mM
0.0025
N-[4-(7-chloro-quinolin-4-ylamino)-butyl]-3-mercapto-propionamide
Serratia marcescens
-
IC50: 0.0025 mM
0.0067
N-[5-(7-chloro-quinolin-4-ylamino)-pentyl]-3-mercapto-propionamide
Serratia marcescens
-
IC50: 0.0067 mM
0.0076
N-[5-(7-chloro-quinolin-4-ylamino)-pentyl]-3-mercapto-propionamide
Pseudomonas aeruginosa
-
IC50: 0.0076 mM
0.0034
N-[6-(7-cloro-quinolin-4-ylamino)-hexyl]-3-mercapto-propionamide
Serratia marcescens
-
IC50: 0.0034 mM
0.0049
N-[6-(7-cloro-quinolin-4-ylamino)-hexyl]-3-mercapto-propionamide
Pseudomonas aeruginosa
-
IC50: 0.0049 mM
0.00003
penem 1
Escherichia coli
pH 7.2, temperature not specified in the publication, recombinant enzyme
0.00015
penem 1
Acinetobacter baumannii
pH 7.2, temperature not specified in the publication, recombinant enzyme
0.00006
penem 3
Escherichia coli
pH 7.2, temperature not specified in the publication, recombinant enzyme
0.00016
penem 3
Acinetobacter baumannii
pH 7.2, temperature not specified in the publication, recombinant enzyme
0.000075
Sulbactam
Alkalihalobacillus clausii
using cephalothin as a substrate, at 30°C
0.012
Sulbactam
Brachyspira pilosicoli
IC50 above 2000 mM, at 25°C in 100 mM sodium phosphate (pH 7.0)
0.000004
tazobactam
Alkalihalobacillus clausii
using cephalothin as a substrate, at 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110
12.5
substrate benzylpenicillin, 30°C, pH not specified in the publication
46200
after a 6.3fold purification, the yield is 16.8% and the preparation have a purity above 99%
5667
additional information
additional information
The specific activity of purified BCL-1, measured with 0.1 mM of cephalothin as the substrate, was 35 units/mg of protein with a 26fold purification factor
additional information
-
The specific activity of purified BCL-1, measured with 0.1 mM of cephalothin as the substrate, was 35 units/mg of protein with a 26fold purification factor
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7
6.5
7.2
7.5
8.2
8.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 9
5 - 9
additional information
4 - 9
-
substrate phenoxymethylpenicillin: kcat 1/6 at pH 9 compared to pH 6.5
additional information
pH dependence of the kinetic parameters, revealing that the maximum velocity depends on the ionization state of two groups: a general base exhibiting a pK value of 4.5 and a general acid exhibiting a pK value of 7.8, overview
additional information
-
pH dependence of the kinetic parameters, revealing that the maximum velocity depends on the ionization state of two groups: a general base exhibiting a pK value of 4.5 and a general acid exhibiting a pK value of 7.8, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
25
30
35
37
40
45
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50 - 75
-
pH 7: stable up to 58, 62, 68°C for K234E, wild type and K234A respectively
additional information
temperature dependency at different NaCl concentrations, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.6 - 4.7
4.9
5.4
6 - 8
6.6
6.8
7.1
7.4
7.6
-
purified SFC-1 migrates as a single band, but isoelectric focusing reveals two forms of purified SFC-1, with pI values of 7.6 and 8.2
7.7
7.8
8
isoelectric focusing, beta-lactamases CTX-M-26, pH-range 3.5-9.5
8.2
8.6
8.7
5.4
isoelectric focusing, pH-range 3-10. Basic beta-lactamases (pI: 7.0) and the acid beta-lactamase with pI 5.4 are encoded by the same L2 gene, the active types of these L2 charge variants are dependent on the buffer pH. The L2 charge variants give Stenotrophomonas maltophilia a better chance of adapting and surviving in response to changes in the environment
6.6
isoelectric focusing, pH-range 3-10
6.8
the beta-lactamase Bla-B focuses at pH 6.8 and pH 7.1, isoelectric focusing, pH 3-10
6.8
isoelectric focusing, Bla-B shows multiple pI-values at 6.8 and 7.1
7
isoelectric focusing, pH-range 3-10. Basic beta-lactamases (pI: 7.0) and the acid beta-lactamase with pI 5.4 are encoded by the same L2 gene, the active types of these L2 charge variants are dependent on the buffer pH. The L2 charge variants give Stenotrophomonas maltophilia a better chance of adapting and surviving in response to changes in the environment
7.1
the beta-lactamase Bla-B focuses at pH 6.8 and pH 7.1, isoelectric focusing, pH 3-10
7.1
isoelectric focusing, Bla-B shows multiple pI-values at 6.8 and 7.1
7.4
isoelectric focusing, pH-range 3-10
7.8
isoelectric focusing, pH-range 3-10
8.2
-
purified SFC-1 migrates as a single band, but isoelectric focusing reveals two forms of purified SFC-1, with pI values of 7.6 and 8.2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain CIP69598, previously Alcaligenes xylosoxidans
UniProt
brenda
isolated from activated sludge in a penicillin G production wastewater treatment system
AB702957
GenBank
brenda
produces only one beta-lactamase belonging to molecular class C
UniProt
brenda
isolated from faecal samples of healthy humans of La Rioja region (Northern Spain), September to November 2010
UniProt
brenda
strain 254G9, strain 4952, strain 192c3, strain 2662, strain 3701, strain 3806 and strain 02C9
-
-
brenda
subsp. atroseptica DSM 30184 (also recently named Pectobacterium atrosepticum)
UniProt
brenda
plasmid pQE32Chl17
the chloramphenicol acetyltransferase gene replaces the blaTEM-1 gene as the selectable marker, allowing plasmid maintenance using 0.0125 mg/ml chloramphenicol. The blaTEM-1 gene is then subcloned under control of the IPTG-inducible promoter and mutated. The resulting constructs harbor a 6-histidine tag that is N-terminal to the native TEM-1 signal peptide. Upon processing of the signal peptide during expression and maturation in Escherichia coli, the histidine tag is also removed
-
-
brenda
gene blaIMP-1; blaIMP-cluster-producingstrains
UniProt
brenda
using the template blaSHV-1 gene in the phagemid vector pBC SK(-), degeneration of oligonucleotides at Ambler position 276 to make the full complement of amino acid substitutions. After PCR mutagenesis, electroporation of the resultant plasmids into Escherichia coli
-
-
brenda
from genetically distinct carbapenem-resistant strains from Argentina
SwissProt
brenda
IMP-1 producing strains A3035, A4861, A3880, A68, A4764, A4468, A129046, A695 and A696, and SIM-1 producing strain YMC 03/9/T104
-
-
brenda
-
209311, 209313, 209322, 209335, 209337, 209339, 209342, 209343, 209347, 209361, 209364, 654962, 663956, 664117
-
-
brenda
isolated from faecal samples of healthy humans of La Rioja region (Northern Spain), September to November 2010
UniProt
brenda
isolated from faecal samples of healthy humans of La Rioja region (Northern Spain), September to November 2010
UniProt
brenda
VIM-1 producing strains 75-10344, ECL3 and ECL4, and IMP-1 producing strain 199
-
-
brenda
-
-
-
brenda
a clinical strain isolated from a patient with a urinary tract infection in Spain, gene blaFOX-4
-
-
brenda
containing the TEM-1 beta-lactamase expression plasmid DNA
UniProt
brenda
isolated from chicken carcasses and human infection in a restrict area
UniProt
brenda
multidrug resistant extended-spectrum beta-lactamase-producing Escherichia coli among uropathogens of pediatrics in north of Iran
-
-
brenda
Fusobacterium nucleatum polymorphum strain NI61
SwissProt
brenda
gene blaCMY-2; 84 multidrug-resistant Klebsiella pneumoniae (MDR-KP) isolates from a chinese hospital from January to October 2012
UniProt
brenda
gene blaCTX-M-15; 84 multidrug-resistant Klebsiella pneumoniae (MDR-KP) isolates from a chinese hospital from January to October 2012
UniProt
brenda
gene blaIMP-4; 84 multidrug-resistant Klebsiella pneumoniae (MDR-KP) isolates from a chinese hospital from January to October 2012
UniProt
brenda
gene blaKPC-2; 84 multidrug-resistant Klebsiella pneumoniae (MDR-KP) isolates from a chinese hospital from January to October 2012
UniProt
brenda
gene blaNDM-1; 84 multidrug-resistant Klebsiella pneumoniae (MDR-KP) isolates from a chinese hospital from January to October 2012
UniProt
brenda
the recombinant plasmid pVT-1 is used as a source of the blaOXA-48 gene. The blaOXA-48 ORF is subcloned into expression vector pET-9a to yield recombinant plasmid pET-OXA-48. Escherichia coli MCT236(DE3) is used as the host for overproduction of the OXA-48 enzyme
UniProt
brenda
12 multidrug-resistant Pseudomonas aeruginosa, MDRPA, isolates isolated in the National Bone Marrow Transplant Centre of Tunisia, genes blaSHV-1 and blaOXA-18
-
-
brenda
19 strains isolated from seven immunocompromised patients, and 3 strains isolated from environmental swabs, genes blaOXA18 and blaSHV
-
-
brenda
an isolate from Turkey co-expressing extended-spectrum beta-lactamase PER-1 and metallo-beta-lactamase VIM-2, strain YUS, genes blaPER-1 and blaVIM-2
-
-
brenda
class A enzyme PSE-4, the active site structure involves Ser70, Lys73, Ser130, Glu166, Asn170, and Arg234 as catalytic residues
Uniprot
brenda
clinical human isolates from a Mexican tertiary-care hospital, strain 4677, gene blaVIM-1
-
-
brenda
clinical human isolates from Majorca, Spain, e.g. strain PA-SL2, and strain PAO1, genes blaVIM-1 and blaVIM-13
-
-
brenda
clinical human isolates of imipenem-resistant strains, genes blaIMP-1, blaVIM and blaVIM-2
-
-
brenda
clinical isolates from human patients, gene bla-VIM in MBl variant VIM-2
-
-
brenda
IMP-15; clinical human isolates from a Mexican tertiary-care hospital, strain 4677, gene blaIMP-15
UniProt
brenda
isolated from a clinical strain, gene blaVIM?2
SwissProt
brenda
isolates from Korean human individuals, genes blaOXA-10, blaVIM-2, blaPSE-I, blaOXA-4, blaOXA-17, blaOXA-30
-
-
brenda
metallo-beta-lactamase VIM-7; isolate from the USA, gene blaVIM-7
UniProt
brenda
MSC15369, IMP-1 is PCR amplified from plasmid DNA prepared from a carbapenems-resistant Pseudomonas aeruginosa MSC15369. The PCR product is cloned into pTrcHis2 TOPO vector (Invitrogen, Carlsbad, CA) and expressed in Escherichia coli DH5a after induction with 0.5 mM isopropyl-beta-D-(-)-thiogalactopyranoside for 3 h at room temperature
-
-
brenda
strain ATCC 27853, IMP-1 producing strains 131, 144, 137, 98, 128, 130, 143, 145, 183, PSA320, IMP-13 producing strain 86-10079, IMP-16 producing strain 101-4704, IMP-18 producing strains 3486 and 3489, GIM-1 producing strain 73-5671, VIM-1 producing strain 179, VIM-2 producing strain 225 and VIM-7 producing strain 07-406, SPM-1 producing strains 48-1997 A, 14, 44, 73, 75, 76, 83, 194, 196 and 197
-
-
brenda
strains P15 and P23, 2 imipenem-resistant isolates, gene oxa40 coding on a plasmid
-
-
brenda
serovar Typhimurium, transferable plasmid blaPER-2 in a ceftibuten-resistant strain
-
-
brenda
the blaSFC-1 gene is contained in the chromosome of Serratia fonticola UTAD54 and is absent from other Serratia fonticola strains
SwissProt
brenda
the blaSFC-1 gene is contained in the chromosome of Serratia fonticola UTAD54 and is absent from other Serratia fonticola strains
SwissProt
brenda
beta-lactamase domain, cf. EC 3.1.1.1; metagenome-derived family VIII carboxylesterase
UniProt
brenda
strain IP97. In the bla gene from strain IP97 a deletion of 51 bp results in a completely inactive beta-lactamase. In the ampC gene from strain Y56 the A751G mutation is responsible for the inactivation of beta-lactamase
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
screening and identification of MBLs from human clinical isolates, resistance phenotypes, overview
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the class A beta-lactamase BlaC is a cell surface expressed serine hydrolase
brenda
-
the class A beta-lactamase BlaC is a cell surface expressed serine hydrolase
-
brenda
-
the class A beta-lactamase BlaC is a cell surface expressed serine hydrolase
-
brenda
AB702957
the first 24 residues of MacQ are predicted to be a signal sequence
-
brenda
-
enzyme excreted during growth, synthesis intracellular
-
brenda
-
enzyme excreted during growth, synthesis intracellular
-
-
brenda
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
comparison of the structures of subclass B1 metallo-beta-lactamases IMP-1 and IMP-2, which have an 85% amino acid identity, suggests that the amino acid substitution at position 68 on a beta-strand (beta3) (Pro in IMP-1 versus Ser in IMP-2) may be a staple factor affecting the flexibility of loop 1 (comprising residues at positions 60-66, EVNGWGV). In the IMP-1 structure, loop 1 adopts an open, disordered conformation. Comparison of the active site structure between IMP-1 and IMP-2, loop 1 of IMP-2 forms a closed conformation in which the side chain of Trp64, involved in substrate binding, is oriented so as to cover the active site, even though there is an acetate ion in the active site of both IMP-1 and IMP-2. Loop 1 of IMP-2 has a more flexible structure in comparison to IMP-1 due to having a Ser residue instead of the Pro residue at position 68, indicating that this difference in sequence may be a trigger to induce a more flexible conformation in loop 1
evolution
metallo-beta-lactamases (MBLs) belong to the protein family of beta-lactamases, a group of enzymes that deactivate beta-lactam antibiotics by cleaving the amide bond in the beta-lactam ring, the enzyme belongs to the molecular class B, subclass B1. The Ambler class B beta-lactamase shares 39% and 29% amino acid identity with IMP-1 and VIM-2, from a Pseudomonas aeruginosa hospital isolate, respectively. Active-site residues that are coordinating zinc ions are conserved among all three subclasses
evolution
-
PER-2 belongs to a small group of extended-spectrum beta-lactamases. Enzyme PER-2 is defined by the presence of a singular trans bond between residues 166 to 167, which generates an inverted omega loop, an expanded fold of this domain that results in a wide active site cavity that allows for efficient hydrolysis of antibiotics like the oxyimino-cephalosporins, and a series of exclusive interactions between residues not frequently involved in the stabilization of the active site in other class A beta-lactamases. PER beta-lactamases might be included within a cluster of evolutionarily related enzymes harboring the conserved residues Asp136 and Asn179
evolution
the enzyme is a metallo-beta-lactamase of subgroup B3
evolution
the POM-1 metallo-beta-lactamase is a subclass B3 resident enzyme
evolution
EstSRT1 is a family VIII carboxylesterase. The enzyme contains a large alpha/beta domain and a small alpha-helical domain and harbors three catalytic residues, Ser71, Lys74, and Tyr160, in the cavity at the domain interface, similarly to other family VIII carboxylesterases. Comparison of the structures of EstSRT1 and EstU1, a family VIII carboxylesterase with no hydrolytic activity toward bulky oxyimino cephalosporins, reveals that EstSRT1 has a smaller active site, despite its extended substrate range. The B-factors of the active site segments that can potentially contact with the oxyimino groups and the R2 side chains of oxyimino cephalosporins are higher in EstSRT1 than in EstU1, thus suggesting the role of the active site's structural flexibility in the extension of EstSRT1's substrate spectrum
evolution
extended-spectrum beta-lactamases (ESBL)-producing Enterobacteriaceae from spring waters can be a thread to human health. ESBL-producing Enterobacteriaceae were found in four out of 50 sampled spring waters (4/50, 8.0%) and a total of 16 non-duplicate ESBL-producing Enterobacteriaceae are obtained, including 13 Escherichia coli and three Klebsiella pneumoniae strains. All 16 nonduplicate ESBL-producing Enterobacteriaceae isolates harbour genes encoding CTX-M ESBLs, among which six expressed CTX-M-15, five produced CTX-M-14, three produced CTX-M-55 and two expressed CTX-M-27. Four multilocus sequence types (ST) are found and ST131 is the dominant type (8/16, 50.0%). The contamination of ESBL-producing Enterobacteriaceae are present in spring waters of Mountain Tai
evolution
extended-spectrum beta-lactamases (ESBL)-producing Enterobacteriaceae from spring waters can be a thread to human health. ESBL-producing Enterobacteriaceae were found in four out of 50 sampled spring waters (4/50, 8.0%) and a total of 16 non-duplicate ESBL-producing Enterobacteriaceae are obtained, including 13 Escherichia coli and three Klebsiella pneumoniae strains. All 16 nonduplicate ESBL-producing Enterobacteriaceae isolates harbour genes encoding CTX-M ESBLs, among which six expressed CTX-M-15, five produced CTX-M-14, three produced CTX-M-55 and two expressed CTX-M-27. Four multilocus sequence types (ST) are found and ST131 is the dominant type (8/16, 50.0%). The contamination of ESBL-producing Enterobacteriaceae are present in spring waters of Mountain Tai
evolution
functionally classifying and characterising serine beta-lactamases: proposal of a grouping of serine beta-lactamases that more consistently captures and rationalizes the existing three classification schemes: classes (A, C and D, which vary in their implementation of the mechanism of action), types (that largely reflect evolutionary distance measured by sequence similarity), and variant groups (which largely correspond with the Bush-Jacoby clinical groups). Analysis of Class A enzymes, overview
evolution
-
genotyping and phenotyping of Escherichia coli strains with beta-lactamase activity in faeces from ducks, phylogenetic analysis. 5 (38.46%) Salmonella isolates are found to harbour gene blaCTX-M. Six Samonella isolates (46.15%) are detected as AmpC producers possessing gene blaAmpC. Significantly higher occurrence of beta-lactamase and biofilm producing Enterobacteriaceae isolates is detected in backyard ducks than organized farms
evolution
-
genotyping and phenotyping of Escherichia coli strains with beta-lactamase activity in faeces from ducks, phylogenetic analysis. Among the 87 phenotypically beta-lactamase producing Escherichia coli, 19 (17.43%), 6 (5.05%) and 15 (13.76%) isolates possess genes blaTEM, blaSHV, and blaCTX-M genes, respectively. Beta-lactamase producing Escherichia coli isolates belong to 14 different serogroups such as O1, O2, O3, O5, O7, O8, O35, O83, O84, O88, O119, O128, O145 and O157. 87 Escherichia coli isolates (79.82%) are detected as AmpC producers possessing gene blaAmpC. Significantly higher occurrence of beta-lactamase and biofilm producing Enterobacteriaceae isolates is detected in backyard ducks than organized farms
evolution
-
genotyping and phenotyping of Escherichia coli strains with beta-lactamase activity in faeces from ducks, phylogenetic analysis. In Klebsiella pneumoniae 10, 3, and 4 isolates possess blaTEM, blaSHV, and blaCTX-M genes, respectively. The sequences of selected PCR products are found 98% cognate with blaCTX-M-9, blaSHV-12 and blaTEM-1. 13 Klebsiella pneumoniae isolates (43.33%) are detected as AmpC producers possessing gene blaAmpC. Significantly higher occurrence of beta-lactamase and biofilm producing Enterobacteriaceae isolates is detected in backyard ducks than organized farms
evolution
genotyping of bla genes in pAmpC-producing Escherichia coli strains, and antimicrobial resistance profiles, overview. Bacteria overexpressing AmpC beta-lactamases are usually resistant to all beta-lactam antibiotics, except cefepime, cefpirome, and carbapenems, which is an important clinical concerns because the bacteria often express a multidrug-resistant phenotype, leaving limited therapeutic options
evolution
phenotype and genotype of the AmpC-positive strains. Beta-lactamases and other resistance mechanisms are characterized in Enterobacteriaceae isolates recovered from healthy human faecal samples, focusing on the ampC beta-lactamase genes. 50 human faecal samples are obtained, and 70 Enterobacteriaceae bacteria are isolated: 44 Escherichia coli, 4 Citrobacter braakii, 9 Citrobacter freundii, 8 Enterobacter cloacae, 1 Proteus mirabilis, 1 Proteus vulgaris, 1 Klebsiella oxytoca, 1 Serratia sp. and 1 Cronobacter sp. A high percentage of resistance to ampicillin is detected (57 %), observing the AmpC phenotype in 22 isolates (31 %) and the extended spectrum beta-lactamase (ESBL) phenotype in 3 isolates. AmpC molecular characterization shows high diversity into blaCMY and blaACT genes from Citrobacter and Enterobacter species, respectively, with low clonality among them. Clonal relationships among Citrobacter spp. and among Enterobacter spp. isolates, molecular typing and phylogenetic analysis, overview
evolution
phenotype and genotype of the AmpC-positive strains. Beta-lactamases and other resistance mechanisms are characterized in Enterobacteriaceae isolates recovered from healthy human faecal samples, focusing on the ampC beta-lactamase genes. 50 human faecal samples are obtained, and 70 Enterobacteriaceae bacteria are isolated: 44 Escherichia coli, 4 Citrobacter braakii, 9 Citrobacter freundii, 8 Enterobacter cloacae, 1 Proteus mirabilis, 1 Proteus vulgaris, 1 Klebsiella oxytoca, 1 Serratia sp. and 1 Cronobacter sp. A high percentage of resistance to ampicillin is detected (57 %), observing the AmpC phenotype in 22 isolates (31 %) and the extended spectrum beta-lactamase (ESBL) phenotype in 3 isolates. AmpC molecular characterization shows high diversity into blaCMY and blaACT genes from Citrobacter and Enterobacter species, respectively, with low clonality among them. Clonal relationships among Citrobacter spp. and among Enterobacter spp. isolates, molecular typing and phylogenetic analysis, overview
evolution
phenotype and genotype of the AmpC-positive strains. Beta-lactamases and other resistance mechanisms are characterized in Enterobacteriaceae isolates recovered from healthy human faecal samples, focusing on the ampC beta-lactamase genes. 50 human faecal samples are obtained, and 70 Enterobacteriaceae bacteria are isolated: 44 Escherichia coli, 4 Citrobacter braakii, 9 Citrobacter freundii, 8 Enterobacter cloacae, 1 Proteus mirabilis, 1 Proteus vulgaris, 1 Klebsiella oxytoca, 1 Serratia sp. and 1 Cronobacter sp. A high percentage of resistance to ampicillin is detected (57 %), observing the AmpC phenotype in 22 isolates (31 %) and the extended spectrum beta-lactamase (ESBL) phenotype in 3 isolates. AmpC molecular characterization shows high diversity into blaCMY and blaACT genes from Citrobacter and Enterobacter species, respectively, with low clonality among them. Clonal relationships among Citrobacter spp. and among Enterobacter spp. isolates, molecular typing and phylogenetic analysis, overview
evolution
the purified soluble form of recombinant MSMEG_4455 shows a beta-lactam hydrolysis pattern similar to group 2a penicillinase. The BlaA enzyme of H37Ra is identical to BlaC of H37Rv
evolution
The PWP triad is sequentially and structurally conserved in class a beta-lactamase family, the evolutionarily conserved allosteric site modulates beta-lactamase activity
evolution
-
the purified soluble form of recombinant MSMEG_4455 shows a beta-lactam hydrolysis pattern similar to group 2a penicillinase. The BlaA enzyme of H37Ra is identical to BlaC of H37Rv
-
evolution
-
the purified soluble form of recombinant MSMEG_4455 shows a beta-lactam hydrolysis pattern similar to group 2a penicillinase. The BlaA enzyme of H37Ra is identical to BlaC of H37Rv
-
malfunction
deletion of gene blaMab dramatically reduces the MIC values of penicillins and first-, second- and third generation cephalosporins (except ceftazidime)
malfunction
inactivation of the cell surface-expressed serine hydrolase and class A beta-lactamase BlaC in Mycobacterium tuberculosis (Mtb) causes increased susceptibility to beta-lactam antibiotics
malfunction
mutation at the glutamate residues in the omega-loop of SHV-14, i.e. E126, E164, and E167, can considerably modulate the beta-lactam sensitivity and reduce hydrolysis. The mutations in SHV-14 render beta-lactamase inhibitors more efficient. The mutations alter the active site configuration of SHV-14
malfunction
while point mutations in the PWP triad preserve the overall secondary structures around the allosteric site, they result in a more open and dynamic global structure with decreased chemical stability and increased aggregation propensity. These mutant enzymes with a less compact hydrophobic core around the allosteric site display significant activity loss
malfunction
-
deletion of gene blaMab dramatically reduces the MIC values of penicillins and first-, second- and third generation cephalosporins (except ceftazidime)
-
malfunction
-
inactivation of the cell surface-expressed serine hydrolase and class A beta-lactamase BlaC in Mycobacterium tuberculosis (Mtb) causes increased susceptibility to beta-lactam antibiotics
-
malfunction
-
inactivation of the cell surface-expressed serine hydrolase and class A beta-lactamase BlaC in Mycobacterium tuberculosis (Mtb) causes increased susceptibility to beta-lactam antibiotics
-
malfunction
Klebsiella pneumoniae MTCC 3384
-
mutation at the glutamate residues in the omega-loop of SHV-14, i.e. E126, E164, and E167, can considerably modulate the beta-lactam sensitivity and reduce hydrolysis. The mutations in SHV-14 render beta-lactamase inhibitors more efficient. The mutations alter the active site configuration of SHV-14
-
physiological function
-
plays a significant role in limiting susceptibility to penicillins and cephalosporins. The contribution of BlaB, a class C enzyme, is less profound and is limited primarily to cephalosporin susceptibility
physiological function
GES beta-lactamases are important contributors to carbapenem resistance in clinical bacterial pathogens
physiological function
New Delhi MBL (NDM)-1 is a clinically significant metallo beta-lactamase
physiological function
role of beta-lactamase BlaMab in beta-lactam resistance, overview
physiological function
-
subclass B3 metallo-beta-lactamase SMB-1 that confers carbapenem resistance
physiological function
the constitutively expressed, chromosomally-encoded beta-lactamase (BlaC) is the enzyme responsible for the intrinsic resistance to beta-lactam antibiotics in Mycobacterium tuberculosis
physiological function
the enzyme is involved in antibiotic resistance, catalyzing the hydrolysis of antibiotics such as benzylpenicillin and imipenem
physiological function
84 multidrug-resistant Klebsiella pneumoniae (MDR-KP) clinical isolates studied, 19 isolates exhibit high level resistance to amikacin mediated by the production of the 16S rRNA methylase. CTX-M genes were found in all of the isolates. Among these armA- or rmtB/CTX-M-producing Klebsiella pneumoniae isolates, 31.6% carry the carbapenemase genes (blaKPC-2 [26.3%], blaIMP-4 [10.5%], and blaNDM-1 [5.3%]), which made them resistant to imipenem
physiological function
chromosomal AmpC beta-lactamases are cephalosporinases, often inducible in the presence of certain beta-lactams such as cefoxitin or imipenem, but that confer a broad beta-lactam resistance profile when they are derepressed or hyperproduced or plasmid mediated. These AmpC enzymes, including plasmidmediated and derepressed or hyperproduced chromosomal AmpCs, suppose a huge repercussion in clinical treatments because they are active against all beta-lactams (including cephamycins), except fourth-generation cephalosporins and carbapenems
physiological function
chromosomal AmpC beta-lactamases are cephalosporinases, often inducible in the presence of certain beta-lactams such as cefoxitin or imipenem, but that confer a broad beta-lactam resistance profile when they are derepressed or hyperproduced or plasmid mediated. These AmpC enzymes, including plasmidmediated and derepressed or hyperproduced chromosomal AmpCs, suppose a huge repercussion in clinical treatments because they are active against all beta-lactams (including cephamycins), except fourth-generation cephalosporins and carbapenems
physiological function
chromosomal AmpC beta-lactamases are cephalosporinases, often inducible in the presence of certain beta-lactams such as cefoxitin or imipenem, but that confer a broad beta-lactam resistance profile when they are derepressed or hyperproduced or plasmid mediated. These AmpC enzymes, including plasmidmediated and derepressed or hyperproduced chromosomal AmpCs, suppose a huge repercussion in clinical treatments because they are active against all beta-lactams (including cephamycins), except fourth-generation cephalosporins and carbapenems
physiological function
extensive production of SHV-14 beta-lactamase makes Klebsiella pneumoniae resistant to beta-lactams. The presence of an omega-loop has been reported to influence the beta-lactamase activity, which is also present in SHV-14
physiological function
AB702957
MacQ is a bifunctional enzyme that confers both quorum quenching and antibiotic resistance on strain MRS7. The enzyme is capable of degrading not only various N-acylhomoserine lactones (AHLs) derivatives but also multiple beta-lactam antibiotics by deacylation activities. Recombinant MacQ confers multiple beta-lactam antibiotic resistance on an Escherichia coli host strain by hydrolyzing beta-lactam antibiotics. The N-acylhomoserine lactone acylase (AHL acylase) activity is responsible for disrupting cell-cell communication (quorum sensing) in bacteria
physiological function
metallo-beta-lactamase (MBL) is a class of enzyme that catalyzes the hydrolysis of a broad range of beta-lactam antibiotics leading to the development of drug resistance in bacteria
physiological function
-
role of beta-lactamase BlaMab in beta-lactam resistance, overview
-
physiological function
-
the constitutively expressed, chromosomally-encoded beta-lactamase (BlaC) is the enzyme responsible for the intrinsic resistance to beta-lactam antibiotics in Mycobacterium tuberculosis
-
physiological function
Klebsiella pneumoniae MTCC 3384
-
extensive production of SHV-14 beta-lactamase makes Klebsiella pneumoniae resistant to beta-lactams. The presence of an omega-loop has been reported to influence the beta-lactamase activity, which is also present in SHV-14
-
additional information
different genotypes of the New Delhi metallo beta-lactamase are identified: the substitutions do not affect the overall folds of the enzyme variants, within limits of detection. Differences in thermal stabilities are observed. kcat/KM values are similar for carbapenem and penicillin substrates for NDM variants, but differences in kinetics are observed for cephalosporin substrates. Apparent substrate inhibition is observed with nitrocefin for variants containing the M154L substitution. In all cases, cefoxitin and ceftazidime are poorly hydrolysed. Clinically observed substitutions can make substantial differences in thermodynamic stability, suggesting that this may be a factor in metallo beta-lactamase evolution. Comparative analysis of the beta-lactam susceptibility of the NDM variants in Escherichia coli, overview
additional information
different genotypes of the New Delhi metallo beta-lactamase are identified: the substitutions do not affect the overall folds of the enzyme variants, within limits of detection. Differences in thermal stabilities are observed. kcat/KM values are similar for carbapenem and penicillin substrates for NDM variants, but differences in kinetics are observed for cephalosporin substrates. Apparent substrate inhibition is observed with nitrocefin for variants containing the M154L substitution. In all cases, cefoxitin and ceftazidime are poorly hydrolysed. Clinically observed substitutions can make substantial differences in thermodynamic stability, suggesting that this may be a factor in metallo beta-lactamase evolution. Comparative analysis of the beta-lactam susceptibility of the NDM variants in Escherichia coli, overview
additional information
different genotypes of the New Delhi metallo beta-lactamase are identified: the substitutions do not affect the overall folds of the enzyme variants, within limits of detection. Differences in thermal stabilities are observed. kcat/KM values are similar for carbapenem and penicillin substrates for NDM variants, but differences in kinetics are observed for cephalosporin substrates. Apparent substrate inhibition is observed with nitrocefin for variants containing the M154L substitution. In all cases, cefoxitin and ceftazidime are poorly hydrolysed. Clinically observed substitutions can make substantial differences in thermodynamic stability, suggesting that this may be a factor in metallo beta-lactamase evolution. Comparative analysis of the beta-lactam susceptibility of the NDM variants in Escherichia coli, overview
additional information
different genotypes of the New Delhi metallo beta-lactamase are identified: the substitutions do not affect the overall folds of the enzyme variants, within limits of detection. Differences in thermal stabilities are observed. kcat/KM values are similar for carbapenem and penicillin substrates for NDM variants, but differences in kinetics are observed for cephalosporin substrates. Apparent substrate inhibition is observed with nitrocefin for variants containing the M154L substitution. In all cases, cefoxitin and ceftazidime are poorly hydrolysed. Clinically observed substitutions can make substantial differences in thermodynamic stability, suggesting that this may be a factor in metallo beta-lactamase evolution. Comparative analysis of the beta-lactam susceptibility of the NDM variants in Escherichia coli, overview
additional information
different genotypes of the New Delhi metallo beta-lactamase are identified: the substitutions do not affect the overall folds of the enzyme variants, within limits of detection. Differences in thermal stabilities are observed. kcat/KM values are similar for carbapenem and penicillin substrates for NDM variants, but differences in kinetics are observed for cephalosporin substrates. Apparent substrate inhibition is observed with nitrocefin for variants containing the M154L substitution. In all cases, cefoxitin and ceftazidime are poorly hydrolysed. Clinically observed substitutions can make substantial differences in thermodynamic stability, suggesting that this may be a factor in metallo beta-lactamase evolution. Comparative analysis of the beta-lactam susceptibility of the NDM variants in Escherichia coli, overview
additional information
different genotypes of the New Delhi metallo beta-lactamase are identified: the substitutions do not affect the overall folds of the enzyme variants, within limits of detection. Differences in thermal stabilities are observed. kcat/KM values are similar for carbapenem and penicillin substrates for NDM variants, but differences in kinetics are observed for cephalosporin substrates. Apparent substrate inhibition is observed with nitrocefin for variants containing the M154L substitution. In all cases, cefoxitin and ceftazidime are poorly hydrolysed. Clinically observed substitutions can make substantial differences in thermodynamic stability, suggesting that this may be a factor in metallo beta-lactamase evolution. Comparative analysis of the beta-lactam susceptibility of the NDM variants in Escherichia coli, overview
additional information
different genotypes of the New Delhi metallo beta-lactamase are identified: the substitutions do not affect the overall folds of the enzyme variants, within limits of detection. Differences in thermal stabilities are observed. kcat/KM values are similar for carbapenem and penicillin substrates for NDM variants, but differences in kinetics are observed for cephalosporin substrates. Apparent substrate inhibition is observed with nitrocefin for variants containing the M154L substitution. In all cases, cefoxitin and ceftazidime are poorly hydrolysed. Clinically observed substitutions can make substantial differences in thermodynamic stability, suggesting that this may be a factor in metallo beta-lactamase evolution. Comparative analysis of the beta-lactam susceptibility of the NDM variants in Escherichia coli, overview
additional information
different genotypes of the New Delhi metallo beta-lactamase are identified: the substitutions do not affect the overall folds of the enzyme variants, within limits of detection. Differences in thermal stabilities are observed. kcat/KM values are similar for carbapenem and penicillin substrates for NDM variants, but differences in kinetics are observed for cephalosporin substrates. Apparent substrate inhibition is observed with nitrocefin for variants containing the M154L substitution. In all cases, cefoxitin and ceftazidime are poorly hydrolysed. Clinically observed substitutions can make substantial differences in thermodynamic stability, suggesting that this may be a factor in metallo beta-lactamase evolution. Comparative analysis of the beta-lactam susceptibility of the NDM variants in Escherichia coli, overview
additional information
different genotypes of the New Delhi metallo beta-lactamase are identified: the substitutions do not affect the overall folds of the enzyme variants, within limits of detection. Differences in thermal stabilities are observed. kcat/KM values are similar for carbapenem and penicillin substrates for NDM variants, but differences in kinetics are observed for cephalosporin substrates. Apparent substrate inhibition is observed with nitrocefin for variants containing the M154L substitution. In all cases, cefoxitin and ceftazidime are poorly hydrolysed. Clinically observed substitutions can make substantial differences in thermodynamic stability, suggesting that this may be a factor in metallo beta-lactamase evolution. Comparative analysis of the beta-lactam susceptibility of the NDM variants in Escherichia coli, overview
additional information
different genotypes of the New Delhi metallo beta-lactamase are identified: the substitutions do not affect the overall folds of the enzyme variants, within limits of detection. Differences in thermal stabilities are observed. kcat/KM values are similar for carbapenem and penicillin substrates for NDM variants, but differences in kinetics are observed for cephalosporin substrates. Apparent substrate inhibition is observed with nitrocefin for variants containing the M154L substitution. In all cases, cefoxitin and ceftazidime are poorly hydrolysed. Clinically observed substitutions can make substantial differences in thermodynamic stability, suggesting that this may be a factor in metallo beta-lactamase evolution. Comparative analysis of the beta-lactam susceptibility of the NDM variants in Escherichia coli, overview
additional information
different genotypes of the New Delhi metallo beta-lactamase are identified: the substitutions do not affect the overall folds of the enzyme variants, within limits of detection. Differences in thermal stabilities are observed. kcat/KM values are similar for carbapenem and penicillin substrates for NDM variants, but differences in kinetics are observed for cephalosporin substrates. Apparent substrate inhibition is observed with nitrocefin for variants containing the M154L substitution. In all cases, cefoxitin and ceftazidime are poorly hydrolysed. Clinically observed substitutions can make substantial differences in thermodynamic stability, suggesting that this may be a factor in metallo beta-lactamase evolution. Comparative analysis of the beta-lactam susceptibility of the NDM variants in Escherichia coli, overview
additional information
different genotypes of the New Delhi metallo beta-lactamase are identified: the substitutions do not affect the overall folds of the enzyme variants, within limits of detection. Differences in thermal stabilities are observed. kcat/KM values are similar for carbapenem and penicillin substrates for NDM variants, but differences in kinetics are observed for cephalosporin substrates. Apparent substrate inhibition is observed with nitrocefin for variants containing the M154L substitution. In all cases, cefoxitin and ceftazidime are poorly hydrolysed. Clinically observed substitutions can make substantial differences in thermodynamic stability, suggesting that this may be a factor in metallo beta-lactamase evolution.Comparative analysis of the beta-lactam susceptibility of the NDM variants in Escherichia coli, overview
additional information
different genotypes of the New Delhi metallo beta-lactamase are identified: the substitutions do not affect the overall folds of the enzyme variants, within limits of detection. Differences in thermal stabilities are observed. kcat/KM values are similar for carbapenem and penicillin substrates for NDM variants, but differences in kinetics are observed for cephalosporin substrates. Apparent substrate inhibition is observed with nitrocefin for variants containing the M154L substitution. In all cases, cefoxitin and ceftazidime are poorly hydrolysed. Clinically observed substitutions can make substantial differences in thermodynamic stability, suggesting that this may be a factor in metallo beta-lactamase evolution.Comparative analysis of the beta-lactam susceptibility of the NDM variants in Escherichia coli, overview
additional information
different genotypes of the New Delhi metallo beta-lactamase are identified: the substitutions do not affect the overall folds of the enzyme variants, within limits of detection. Differences in thermal stabilities are observed. kcat/KM values are similar for carbapenem and penicillin substrates for NDM variants, but differences in kinetics are observed for cephalosporin substrates. Apparent substrate inhibition is observed with nitrocefin for variants containing the M154L substitution. In all cases, cefoxitin and ceftazidime are poorly hydrolysed. Clinically observed substitutions can make substantial differences in thermodynamic stability, suggesting that this may be a factor in metallo beta-lactamase evolution.Comparative analysis of the beta-lactam susceptibility of the NDM variants in Escherichia coli, overview
additional information
different genotypes of the New Delhi metallo beta-lactamase are identified: the substitutions do not affect the overall folds of the enzyme variants, within limits of detection. Differences in thermal stabilities are observed. kcat/KM values are similar for carbapenem and penicillin substrates for NDM variants, but differences in kinetics are observed for cephalosporin substrates. Apparent substrate inhibition is observed with nitrocefin for variants containing the M154L substitution. In all cases, cefoxitin and ceftazidime are poorly hydrolysed. Clinically observed substitutions can make substantial differences in thermodynamic stability, suggesting that this may be a factor in metallo beta-lactamase evolution.Comparative analysis of the beta-lactam susceptibility of the NDM variants in Escherichia coli, overview
additional information
different genotypes of the New Delhi metallo beta-lactamase are identified: the substitutions do not affect the overall folds of the enzyme variants, within limits of detection. Differences in thermal stabilities are observed. kcat/KM values are similar for carbapenem and penicillin substrates for NDM variants, but differences in kinetics are observed for cephalosporin substrates. Apparent substrate inhibition is observed with nitrocefin for variants containing the M154L substitution. In all cases, cefoxitin and ceftazidime are poorly hydrolysed. Clinically observed substitutions can make substantial differences in thermodynamic stability, suggesting that this may be a factor in metallo beta-lactamase evolution.Comparative analysis of the beta-lactam susceptibility of the NDM variants in Escherichia coli, overview
additional information
different genotypes of the New Delhi metallo beta-lactamase are identified: the substitutions do not affect the overall folds of the enzyme variants, within limits of detection. Differences in thermal stabilities are observed. kcat/KM values are similar for carbapenem and penicillin substrates for NDM variants, but differences in kinetics are observed for cephalosporin substrates. Apparent substrate inhibition is observed with nitrocefin for variants containing the M154L substitution. In all cases, cefoxitin and ceftazidime are poorly hydrolysed. Clinically observed substitutions can make substantial differences in thermodynamic stability, suggesting that this may be a factor in metallo beta-lactamase evolution.Comparative analysis of the beta-lactam susceptibility of the NDM variants in Escherichia coli, overview
additional information
different genotypes of the New Delhi metallo beta-lactamase are identified: the substitutions do not affect the overall folds of the enzyme variants, within limits of detection. Differences in thermal stabilities are observed. kcat/KM values are similar for carbapenem and penicillin substrates for NDM variants, but differences in kinetics are observed for cephalosporin substrates. Apparent substrate inhibition is observed with nitrocefin for variants containing the M154L substitution. In all cases, cefoxitin and ceftazidime are poorly hydrolysed. Clinically observed substitutions can make substantial differences in thermodynamic stability, suggesting that this may be a factor in metallo beta-lactamase evolution.Comparative analysis of the beta-lactam susceptibility of the NDM variants in Escherichia coli, overview
additional information
in GES-2 an extensive hydrogen-bonding network between the acyl-enzyme complex and the active site water attenuates activation of this water molecule, which results in poor deacylation by this enzyme
additional information
in GES-2 an extensive hydrogen-bonding network between the acyl-enzyme complex and the active site water attenuates activation of this water molecule, which results in poor deacylation by this enzyme
additional information
in GES-2 an extensive hydrogen-bonding network between the acyl-enzyme complex and the active site water attenuates activation of this water molecule, which results in poor deacylation by this enzyme
additional information
Mox-1 is a unique plasmid-mediated class C beta-lactamase. Structure comparison with other beta-lactamases shows that two region in Mox 1, amino acid residues 214 to 216 positioned in the omega loop and the other in the N-terminus of the B3 beta-strand corresponding to amino acid residues 303 to 306, having significant structural flexibility of these regions, may impact the recognition and binding of substrates in Mox-1 leading to the unique substrate profile of the enzyme, overview. A substrate-induced conformational change underlies the basis of the hydrolytic profile of Mox-1 beta-lactamase, active site structure of enzyme Mox-1, overview
additional information
-
secondary structures and conserved motifs of PER-2 and other class A beta-lactamases, presence of a hydrogen-bond network connecting Ser70-Gln69-water-Thr237-Arg220 that might be important for the proper activity and inhibition of the enzyme, strcture comparisson, simulation and modeling, overview
additional information
the catalytic mechanism of BlaC relies on three highly conserved active site residues, Lys73 and Glu166, which are involved in the activation of the acylating nucleophile Ser70 and the activation of the active site water molecule for deacylation, respectively. Lys73 is essential for the acylation step
additional information
-
the catalytic mechanism of BlaC relies on three highly conserved active site residues, Lys73 and Glu166, which are involved in the activation of the acylating nucleophile Ser70 and the activation of the active site water molecule for deacylation, respectively. Lys73 is essential for the acylation step
additional information
the marine enzyme is highly salt tolerant and cold active
additional information
-
structural basis of the hydrolytic activity of EstSRT1 toward bulky oxyimino antibiotics. Structural comparison between EstSRT1 and the EstU1/cephalothin complex
additional information
structural basis of the hydrolytic activity of EstSRT1 toward bulky oxyimino antibiotics. Structural comparison between EstSRT1 and the EstU1/cephalothin complex
additional information
-
structural basis of the hydrolytic activity of EstSRT1 toward bulky oxyimino antibiotics. The three catalytic residues are Ser71, Lys74, and Tyr160. Structural comparison between EstSRT1 and the EstU1/cephalothin complex
additional information
structural basis of the hydrolytic activity of EstSRT1 toward bulky oxyimino antibiotics. The three catalytic residues are Ser71, Lys74, and Tyr160. Structural comparison between EstSRT1 and the EstU1/cephalothin complex
additional information
characterization of pAmpC-producing Escherichia coli strains isolated from chicken carcasses and human infection in a restrict area and to determine their antimicrobial resistance profiles, and molecular type by multilocus sequence typing (MLST) and pulsed-field gel electrophoresis. The blaCMY-2 gene is identified in all pAmpC-producing Escherichia coli strains
additional information
-
characterization of pAmpC-producing Escherichia coli strains isolated from chicken carcasses and human infection in a restrict area and to determine their antimicrobial resistance profiles, and molecular type by multilocus sequence typing (MLST) and pulsed-field gel electrophoresis. The blaCMY-2 gene is identified in all pAmpC-producing Escherichia coli strains
additional information
close to 80% of blaTEM-1 and blaSHV-12 are linked to IS26 while 90% or more of blaCTX-Ms and blaCMYs are linked to ISEcp1. ISAba125 is located upstream of blaNDM-1 and some blaCMY-2 genes. In addition, seven transconjugants are available for further analysis, and armA, qnrS1, acc(6')-Ib-cr, blaCTX-M-15, blaTEM-1, and blaNDM-1 are cotransferred. The dissemination of 16S rRNA methylase genes and the prevalence of selected elements implicated in evolution of antibiotics resistance determinants in collection of clinical Klebsiella pneumoniae in China, overview
additional information
close to 80% of blaTEM-1 and blaSHV-12 are linked to IS26 while 90% or more of blaCTX-Ms and blaCMYs are linked to ISEcp1. ISAba125 is located upstream of blaNDM-1 and some blaCMY-2 genes. In addition, seven transconjugants are available for further analysis, and armA, qnrS1, acc(6')-Ib-cr, blaCTX-M-15, blaTEM-1, and blaNDM-1 are cotransferred. The dissemination of 16S rRNA methylase genes and the prevalence of selected elements implicated in evolution of antibiotics resistance determinants in collection of clinical Klebsiella pneumoniae in China, overview
additional information
close to 80% of blaTEM-1 and blaSHV-12 are linked to IS26 while 90% or more of blaCTX-Ms and blaCMYs are linked to ISEcp1. ISAba125 is located upstream of blaNDM-1 and some blaCMY-2 genes. In addition, seven transconjugants are available for further analysis, and armA, qnrS1, acc(6')-Ib-cr, blaCTX-M-15, blaTEM-1, and blaNDM-1 are cotransferred. The dissemination of 16S rRNA methylase genes and the prevalence of selected elements implicated in evolution of antibiotics resistance determinants in collection of clinical Klebsiella pneumoniae in China, overview
additional information
close to 80% of blaTEM-1 and blaSHV-12 are linked to IS26 while 90% or more of blaCTX-Ms and blaCMYs are linked to ISEcp1. ISAba125 is located upstream of blaNDM-1 and some blaCMY-2 genes. In addition, seven transconjugants are available for further analysis, and armA, qnrS1, acc(6')-Ib-cr, blaCTX-M-15, blaTEM-1, and blaNDM-1 are cotransferred. The dissemination of 16S rRNA methylase genes and the prevalence of selected elements implicated in evolution of antibiotics resistance determinants in collection of clinical Klebsiella pneumoniae in China, overview
additional information
close to 80% of blaTEM-1 and blaSHV-12 are linked to IS26 while 90% or more of blaCTX-Ms and blaCMYs are linked to ISEcp1. ISAba125 is located upstream of blaNDM-1 and some blaCMY-2 genes. In addition, seven transconjugants are available for further analysis, and armA, qnrS1, acc(6')-Ib-cr, blaCTX-M-15, blaTEM-1, and blaNDM-1 are cotransferred. The dissemination of 16S rRNA methylase genes and the prevalence of selected elements implicated in evolution of antibiotics resistance determinants in collection of clinical Klebsiella pneumoniae in China, overview
additional information
-
close to 80% of blaTEM-1 and blaSHV-12 are linked to IS26 while 90% or more of blaCTX-Ms and blaCMYs are linked to ISEcp1. ISAba125 is located upstream of blaNDM-1 and some blaCMY-2 genes. In addition, seven transconjugants are available for further analysis, and armA, qnrS1, acc(6')-Ib-cr, blaCTX-M-15, blaTEM-1, and blaNDM-1 are cotransferred. The dissemination of 16S rRNA methylase genes and the prevalence of selected elements implicated in evolution of antibiotics resistance determinants in collection of clinical Klebsiella pneumoniae in China, overview
additional information
-
consumption of antibiotic through feed or during therapy is considered as potential reason for generation of antimicrobial resistant bacteria in birds
additional information
-
consumption of antibiotic through feed or during therapy is considered as potential reason for generation of antimicrobial resistant bacteria in birds
additional information
-
consumption of antibiotic through feed or during therapy is considered as potential reason for generation of antimicrobial resistant bacteria in birds
additional information
enzyme structure-function relationship in silico analysis, overview. Residues E193 and Y194 of the omega-like loop might have importance in strengthening hydrogen bond network around the active site, though involvement of tyrosine is rare for beta-lactamase activity. Y194 is the key for beta-lactamase activity of MSMEG_4455
additional information
-
enzyme structure-function relationship in silico analysis, overview. Residues E193 and Y194 of the omega-like loop might have importance in strengthening hydrogen bond network around the active site, though involvement of tyrosine is rare for beta-lactamase activity. Y194 is the key for beta-lactamase activity of MSMEG_4455
additional information
-
Escherichia coli remains as one of the most important bacteria causing infections in pediatrics and producing extended-spectrum beta-lactamases (ESBLs) making them resistant to beta-lactam antibiotics. Multidrug resistant extended-spectrum beta-lactamase-producing Escherichia coli strains among uropathogens of pediatrics in north of Iran are isolated and tested by PCR for the presence or absence of CTX, TEM, SHV, GES, and VEB beta-lactamase genes. Genotyping reveals that the TEM gene is the most prevalent (49%) followed by SHV (44%), CTX (28%), VEB (8%), and GES (0%) genes. The ESBL-producing Escherichia coli isolates are susceptible to carbapenems (66%) and amikacin (58%) and show high resistance to cefixime (99%), colistin (82%), and ciprofloxacin (76%). Carbapenems are the most effective antibiotics against ESBl-producing Escherichia coli in urinary tract infection in north of Iran
additional information
Glu152 and Ser191 are the key residues required for the metallo-beta-lactamase activity of strain NDM-7. Three-dimensional structure homology modelling of wild-type BlaNDM-7 and mutant enzymes
additional information
mechanism of antibiotics resistance, overview
additional information
mechanism of antibiotics resistance, overview
additional information
mechanism of antibiotics resistance, overview
additional information
mechanism of antibiotics resistance, overview
additional information
mechanism of antibiotics resistance, overview
additional information
mechanism of antibiotics resistance, overview
additional information
mechanism of antibiotics resistance, overview
additional information
mechanism of antibiotics resistance, overview
additional information
mechanism of antibiotics resistance, overview
additional information
mechanism of antibiotics resistance, overview
additional information
mechanism of antibiotics resistance, overview
additional information
mechanism of antibiotics resistance, overview
additional information
mechanism of antibiotics resistance, overview
additional information
mechanism of antibiotics resistance, overview
additional information
mechanism of antibiotics resistance, overview
additional information
mechanism of antibiotics resistance, overview
additional information
structure-based classification of beta-lactamases, functional determinants between the Class A, C, D beta-lactamases and of sites in the active sites of class A serine beta-lactamases likely to be affecting phenotype
additional information
structure-based classification of beta-lactamases, functional determinants between the Class A, C, D beta-lactamases and of sites in the active sites of class A serine beta-lactamases likely to be affecting phenotype
additional information
structure-based classification of beta-lactamases, identification functional determinants between the Class A, C, D beta-lactamases and of sites in the active sites of class A serine beta-lactamases likely to be affecting phenotype. Isozyme TEM-1 is a class A type 1 enzyme
additional information
structure-based classification of beta-lactamases, identification functional determinants between the Class A, C, D beta-lactamases and of sites in the active sites of class A serine beta-lactamases likely to be affecting phenotype. Isozyme TEM-1 is a class A type 1 enzyme
additional information
structure-function analysis, molecular dynamics simulation and modeling, overview
additional information
substrate binding to active site residues of SHV-14 wild-type and mutant enzyme proteins, structures, overview
additional information
-
substrate binding to active site residues of SHV-14 wild-type and mutant enzyme proteins, structures, overview
additional information
the evolutionarily conserved PWP triad located at the N-terminus of the H10 helix directly interacts with the allosteric site in TEM-1 beta-lactamase and regulates its activity. The PWP triad is an evolutionarily conserved motif unique to class A beta-lactamases aligning its allosteric site. The H10 helix C-terminus forms part of the active site, specifically K243 participating in catalysis and substrate binding, while P226-W229-P252 (PWP triad) residues at the N-terminus participate in aromatic ring stacking that stabilize the helix. Together with the T-shaped aromatic interaction between W229 and W290, this extensive interaction network modulates the flexibility of H10 and its interactions with other secondary structural elements in the hydrophobic inhibitor binding pocket, suggesting the contribution of these residues to allostery. Structure comparisons, overview
additional information
Klebsiella pneumoniae NDM-7
-
Glu152 and Ser191 are the key residues required for the metallo-beta-lactamase activity of strain NDM-7. Three-dimensional structure homology modelling of wild-type BlaNDM-7 and mutant enzymes
-
additional information
-
enzyme structure-function relationship in silico analysis, overview. Residues E193 and Y194 of the omega-like loop might have importance in strengthening hydrogen bond network around the active site, though involvement of tyrosine is rare for beta-lactamase activity. Y194 is the key for beta-lactamase activity of MSMEG_4455
-
additional information
-
the catalytic mechanism of BlaC relies on three highly conserved active site residues, Lys73 and Glu166, which are involved in the activation of the acylating nucleophile Ser70 and the activation of the active site water molecule for deacylation, respectively. Lys73 is essential for the acylation step
-
additional information
-
enzyme structure-function relationship in silico analysis, overview. Residues E193 and Y194 of the omega-like loop might have importance in strengthening hydrogen bond network around the active site, though involvement of tyrosine is rare for beta-lactamase activity. Y194 is the key for beta-lactamase activity of MSMEG_4455
-
additional information
Klebsiella pneumoniae MTCC 3384
-
substrate binding to active site residues of SHV-14 wild-type and mutant enzyme proteins, structures, overview
-
additional information
-
Mox-1 is a unique plasmid-mediated class C beta-lactamase. Structure comparison with other beta-lactamases shows that two region in Mox 1, amino acid residues 214 to 216 positioned in the omega loop and the other in the N-terminus of the B3 beta-strand corresponding to amino acid residues 303 to 306, having significant structural flexibility of these regions, may impact the recognition and binding of substrates in Mox-1 leading to the unique substrate profile of the enzyme, overview. A substrate-induced conformational change underlies the basis of the hydrolytic profile of Mox-1 beta-lactamase, active site structure of enzyme Mox-1, overview
-
Show AA Sequence and Transmembrane Helices (45503 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
115000
22000
25000
25120
25130
25150
25160
25180
25190
25200
25220
25250
26000
28000
28100
28200
28370
28400
28500
28636
4 * 28636, recombinant enzyme, mass spectrometry, 4 * 28639, sequence calculation
28639
4 * 28636, recombinant enzyme, mass spectrometry, 4 * 28639, sequence calculation
28910
electrospray mass spectrometry, corresponding to the cleavage of the N-terminal extremity after residue Phe6
29000
29050
electrospray mass spectrometry, corresponding to the cleavage of the N-terminal extremity after residue Met5
30000
30630
-
truncated protein, matrix-assisted laser desorption ionization
31500
32000
34000
35000
35060
theoretical and determined by electrospray mass spectrometry
37000
38000
38720
40000
41000
53000
in presence of Cd2+, Cu2+ or Zn2+, gel filtration and analytical ultracentrifugation
28370
determined by mass spectrometry using a MALDI-TOF-MS instrument
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
AB702957
1 * 20000, alpha-subunit, + 1 * 62000, beta-subunit, SDS-PAGE, recombinant enzyme
homodimer
monomer
tetramer
additional information
?
x * 30000, about, recombinant wild-type and mutant enzymes, SDS-PAGE and MALDI-ToF MS analysis
?
Klebsiella pneumoniae MTCC 3384
-
x * 30000, about, recombinant wild-type and mutant enzymes, SDS-PAGE and MALDI-ToF MS analysis
-
?
x * 43000, about, recombinant His-tagged wild-type and mutant enzymes, SDS-PAGE
?
-
x * 43000, about, recombinant His-tagged wild-type and mutant enzymes, SDS-PAGE
-
?
-
x * 43000, about, recombinant His-tagged wild-type and mutant enzymes, SDS-PAGE
-
tetramer
4 * 28636, recombinant enzyme, mass spectrometry, 4 * 28639, sequence calculation
additional information
His118 and His196 participate in the catalytic mechanism of the subclass B2 CphA metallo-beta-lactamase, for which an intact Asp120/Cys221/His263 site is essential
additional information
-
His118 and His196 participate in the catalytic mechanism of the subclass B2 CphA metallo-beta-lactamase, for which an intact Asp120/Cys221/His263 site is essential
additional information
-
the enzyme shows a typical alphabeta/betaalpha metallo-beta-lactamase fold
additional information
-
enzyme belongs to a subclass containing an enlarged OMEGA loop near the beta-lactam binding site, which projects into solvent and cannot interact directly with the substrate
additional information
three-dimensional analysis using crystal structures PDB IDs 1FQG and 1BTL, modeling
additional information
three-dimensional analysis using crystal structures PDB IDs 1FQG and 1BTL, modeling
additional information
cation mediated formation of a homodimer, but NaCl leads to dissociation of the dimer, overview
additional information
-
cation mediated formation of a homodimer, but NaCl leads to dissociation of the dimer, overview
additional information
enzyme consists of an alpha/beta domain and a predominantly alpha-helical domain
additional information
-
enzyme consists of an alpha/beta domain and a predominantly alpha-helical domain
additional information
VIM-2 secondary structure, structure comparison to other VIMs, overview
additional information
-
VIM-2 secondary structure, structure comparison to other VIMs, overview
additional information
folding of alphabeta/betaalpha sandwich, consisting of a core of beta-sheet surrounded by alpha-helices
additional information
-
folding of alphabeta/betaalpha sandwich, consisting of a core of beta-sheet surrounded by alpha-helices
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospholipoprotein
phosphoprotein
proteolytic modification
mature enzyme is generated by cleavage of a 26-amino acid signal peptide
phosphoprotein
phosphorylated Ser70 in BlaC following inactivation by dibenzoyl phosphate
phosphoprotein
-
phosphorylated Ser70 in BlaC following inactivation by dibenzoyl phosphate
-
phosphoprotein
-
phosphorylated Ser70 in BlaC following inactivation by dibenzoyl phosphate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme IMP-2 MBL, hanging drop vapour diffusion metod, mixxing of 0.003 ml of 5 mg/ml protein in 20 mM HEPES-NaOH, pH 7.5, with 0.003 ml of reservoir solution containing 30% w/v PEG 4000, 0.1 M citric acid/sodium citrate, and 0.2 M sodium acetate, pH 6.0, equilibration against 0.35 ml reservori solution, 20°C, X-ray diffraction structure determination and analysis at 2.3 A resolution, modeling and structure comparisons
purified recombinant enzyme, hanging drop vapor diffusion method, mixing of 6 mg/ml protein in 10 mM HEPES, pH 7.5, with crystallization solution containing 0.1 M HEPES, pH 7.5, 0.1 M sodium acetate, and 28% PEG 2000, X-ray diffraction structure determination and analysis
structure of the class D beta-lactamase OXA-1 as an acyl complex with doripenem, determined to 1.4 A resolution
-
crystal structure of wild-type enzyme mutant enzyme N220G, and of the complex of wild-type enzyme with biapenem
hanging drop vapour diffusion method with 30% (w/v) polyethylene glycol 8000, 0.6 M ammonium sulfate, and 100 mM Na-citrate, pH 6.5
hanging-drop vapor-diffusion method, crystals exhibit orthorhombic symmetry P2(1)2(1)2(1), with unit-cell parameters a = 40.75, b = 42.05, c = 128.88 A. There is one monomer in the asymmetric unit
-
purified recombinant enzyme, complexed with cefoxitin in an acyl-enzyme-adduct, for monoclinic crystals: 0.005 ml protein solution, 10 mg/ml, + equal volume of reservoir solution containing 25% PEG 6000, 0.1 M sodium acetate, pH 5.0, against 1 ml of reservoir solution at 20°C, for very big prismatic crystals: 40 mg/ml protein with lowered PEG 6000 concentration, pH 3.4, complexing by diffusion of cefoxitin for 24 h, X-ray diffraction structure determination and analysis at 1.7 A resolution
hanging drop vapor diffusion, crystals are soaked with a solution of 6-beta-iodopenicillanic acid and the structure solved at 1.65 A
-
using the microbatch crystallization method, X-ray intensity data are collected to 1.49 A resolution using synchrotron radiation
-
enzyme BlaB in complex with the inhibitor D-captopril, hanging drop method, 0.002 ml of 5 mg/ml protein in 10 mM sodium cacodylate, 0.1 mM zinc acetate, 0.1 mM DTT, pH 6.5, is mixed with 0.001 ml of reservoir solution containing 28% PEG 4000, 0.2 M sodium acetate, 0.1 M Tris-HCl, pH 8.4, at 8°C, 3 weeks, complexing by soaking of the crystals in a solution containing 2 mM D-captopril for 5 weeks, cryoprotection by 15% glycerol, X-ray diffraction structure determination and analysis at 1.5 A resolution
-
hanging drop vapour diffusion method with 20% poly(ethylene)glycol 6 K in 0.1 M Tris (pH 8.0)
0.98 mg/ml purified mutant N152A in complex with inhibitor moxalactam in 1.7 M potassium phosphate, pH 8.7, 23°C, after microseeding with the wild-type enzyme in 1 M potassium phosphate, pH 8.7, vapor diffusion hanging drop method, serial dilutions, 5-7 days, X-ray diffraction structure determination and analysis at 1.83 A resolution
2.5-3 mg/ml purified recombinant enzyme in 10% PEG 8000, 0.05 M HEPES, pH 7.5, vapour diffusion sitting drop method, equilibration of 0.01 ml protein solution over a reservoir solution containing 20% PEG 8000, macro-seeding at 1.2-1.5 mg/ml, growth of prismatic crystals, X-ray diffraction structure determination and analysis at 1.5 A resolution, modeling
-
crystal quality of Toho-1 is improved by using surface modification to remove a sulfate ion involved in crystal packing
in complex with ([(benzylsulfonyl)amino]methyl)boronic acid, 4-([[(dihydroxyboranyl)methyl]sulfamoyl]methyl)benzoic acid, and 3-[(2R)-2-[(benzylsulfonyl)amino]-2-(dihydroxyboranyl)ethyl]benzoic acid, to 1.6, 1.8 and 1.6 A resolution, respectively. The sulfonamides have a highly distinct structure-activity relationship from the carboxamides, with high ligand efficiencies, and Ki values down to 25 nM and up to 23 times better for smaller analogs. Conversely, Ki values are 10 to 20 times worse for larger molecules than in the carboxamide congener series. X-ray crystal structures suggest that this altered structure-activity relationship results from the different geometry and polarity of the sulfonamide versus the carboxamide
microseeding, enzyme/beta-lactamase inhibitory protein(BLIP) complexes: BLIP/TEM-1, BLIP(W150A)/TEM-1 and BLIP(Y51A)/TEM-1
purified recombinant enzyme, hanging drop vapor diffusion method, mixing of 9 mg/ml protein solution with crystallization solution containing 0.05 M HEPES, pH 7.5, and 15% PEG 8000, X-ray diffraction structure determination and analysis
three-dimensional analysis using crystal structure PDB ID 1IYO, modeling
hanging-drop vapour-diffusion. Two crystal forms are obtained from the same growth conditions. One is orthorhombic, with crystals that diffracted to better than 1.9 A, the other is tetragonal, with crystals that only diffracted to about 3.0 A. The orthorhombic crystal belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 46.54 A, b = 73.43 A, c = 84.56 A, while the tetragonal crystal has unit-cell parameters a = b = 73.72, c = 96.81 A
-
crystal structure of the complex of SHV-1 mutant D104E with beta-lactamse inhibitor protein BLIP, to 1.6 A resolution. Mutation D104E results in a 1000fold enhancement in binding affinity to BLIP, as it restores a salt bridge to BLIP. Mutation of a neighboring residue, BLIP E73M, results in salt bridge formation between SHV-1 D104 and BLIP K74 and a 400fold increase in binding affinity. BLIP F142 cooperatively stabilizes both interactions
purified recombinant enzyme, hanging-drop or sitting-drop vapor diffusion, mixing of 10 mg/ml protein in 10 mM Tris-HCl, pH 7.0, with reservoir solution containing of 20% PEG 8000, 100 mM sodium cacodylate, pH 6.5, and 0.2 M zinc acetate, to a finaal volume of 0.01 ml, equilibration against 0.5 ml reservoir solution, 1 month, 16°C, X-ray diffraction structure determination and analysis at 1.54 A resolution, modeling and molecular replacement
sitting-drop method, crystal structure of the OXA-48 carbapenemase is determined at pH 7.5 and at a resolution of 1.9 A. The enzyme shows a noncrystallographic pseudo 2-fold axis
vapour diffusion method, 1.5 A resolution, space group 2(1), a = 49.7 A, b = 59.5 A, c = 63.75 A, beta = 102.57°
-
vapour diffusion method, 2.5 A resolution, space group 2(1), a = 49.73 A, b = 59.54 A, c = 63.78 A, beta = 102.52°
-
BLaC is crystallized in the hanging drop vapor diffusion configuration over well conditions that include 0.1 M HEPES (pH 7.5) and 2 M NH4H2PO4. The final pH of the well solution is 4.1
enzyme in complex with inhibitor NXL104, hanging drop vapor diffusion, mixing of 12 mg/ml protein solution in a 1:1 ratio with well solution containing 0.1 M HEPES and 2 M NH4H2PO4, pH 4.1, 10°C, 4-5 days, microseeding, X-ray diffraction structure determination and analysis at 2.3 A resolution
-
hanging drop vapour diffusion method with 0.1 M Tris-HCl, pH 8.0, 2.0 M NH4H2PO4
-
purified recombinant detagged wild-type and mutant enzymes in complex with inhibitor tebipenem, hanging drop vapor diffusion, mixing of 12 mg/ml protein with 0.1 M HEPES and 2 M NH4H2PO4, pH 4.1, in a 1:1 ratio, 10°C, microseeding for the mutant enzyme, X-ray diffraction structure determination and analysis at 1.90 A and 1.75 A resolution
hanging drop vapour diffusion method in 0.1 M Tris HCl buffer, pH 7.3, with 27% polyethylene glycol 10000
hanging-drop vapor diffusion method, 2.13 A resolution, P2(1)2(1)2(1), a = 35.66 A, b = 73.42 A, c = 91.32 A, one molecule per asymmetric unit
sitting drop vapour diffusion method, crystallographic structure of the KPC-2/BLIP complex is solved to 1.9 A resolution
-
hanging drop vapor diffusion method, mutant enzyme W154A, mutant enzyme W154G, mutant enzyme W154H
plasmid pGEM-T-easy
-
0.003 ml 10 mg/ml purified recombinant wild-type enzyme or mutant R234K, mixed with 0.001 ml of well solution containing 2 M ammonium sulfate, 50 mM MOPS pH 6.4, and 0.1 M acetate pH 4.5, respectively, 100 mM MgCl2, 1-2 weeks at room temperature, X-ray diffraction structure determination and analysis at 1.75 A resolution
as the native enzyme, with Cys221 oxidized, and with a sulfur atom bridging the two active-site zinc ions, to 1.9, 1.8 and 2.5 A resolution, respectively. Comparison with VIM-2 and VIM-4 structures suggests an explanation for the reduced catalytic efficiency of VIM-7 against cephalosporins with a positively charged cyclic substituent at the C3 position. Kinetic variations are attributed to substitutions in residues 6066, that form a loop adjacent to the active site previously implicated in substrate binding, and to the disruption of two hydrogen-bonding clusters through substitutions at positions 218 and 224
in complex with rac-2-omega-phenylpropyl-3-mercaptopropionic acid, in 30% PEG MME5000, 0.1 M MES-NaOH, and 0.2 M ammonium sulfate (pH 6.5)
-
purified recombinant enzyme, sitting drop vapor diffusion method, mixxing of 0001 ml of 10 mg/mL VIM-2 protein with 0.001 ml of reservoir solution containing 0.2 M ammonium acetate, 0.1 mM zinc chloride, 0.1 M HEPES, pH 7.5, and 25% PEG 3350, X-ray diffraction tructure determination and analysis, molecular replacement
purified recombinant native and chloride-treated enzyme, from 1.8 M ammonium sulfate, 0.1 M MES, pH 6.5, 10 mM CoCl2, vapour diffusion method, X-ray diffraction structure determination and analysis at 2.0 A resolution, modeling
purified recombinant native and oxidized VIM-2, hanging drop vapour diffusion method, mixing 0.001 ml of 5.5 mg/ml of protein in 10 mM HEPES, pH 7.5, 0.2 M NaCl, and 1 mM DTT, with 0.001 ml of precipitant solution containing 30% PEG 8000, 0.2 M Na acetate, 0.1 M Na cacodylate/cacodylic acid, pH 6.5, and 0.01 mM ZnCl2, 20°C, 3-4 days, X-ray diffraction structure determination and analysis at 1.9-2.2 A resolution
substrate ertapenem-isozyme GES-2 crystal structure determination and analysis
X-ray data collection and structure refinement of the reduced and oxidised VIM-2
hanging drop vapour diffusion method with 20% poly(ethylene)glycol 6 K in 0.1 M Tris (pH 8.0)
purified recombinant enzyme, hanging drop vapor diffusion method, mixing of 0.0025 ml of 3.5mg/ml protein in , with 0.001 ml of crystallization solution containing 0.1 M HEPES in 1.5 M sodium citrate, pH 7.5, equilibration against 1.0 ml crystallization solution, 20°C, X-ray diffraction structure determination and analyysis at 2.2 A resolution, modeling
-
hanging drop vapour diffusion method with 20% poly(ethylene)glycol 6 K in 0.1 M Tris (pH 8.0)
-
hanging-drop vapour diffusion method. Three-dimensional structures of D120A mutant and D120E mutant determined at 2.0 A and 3.0 A resolution, respectively
purified recombinant His-tagged enzyme, method screening, sitting drop vapour diffusion method, mixing of 0.001 ml protein solution with 0.001 ml reservoir solution containing 0.2 M ammonium sulfate, 0.1 M sodium acetate trihydrate, pH 5.3, 28% w/v PEG MME 2000, or 1.0 M lithium chloride, 0.1 M MES, pH 5.8, and 26% w/v PEG 6000, 1 week, 20°C, resulting in two different types of crystals: SMB-1a and SMB-1b, X-ray diffraction structure determination and analysis at 1.60-1.63 A resolution, molecular replacement and modeling
-
hanging drop vapour diffusion method with 100 mM HEPES (pH 7.75), 1.8 M (NH4)2SO4, 1.5% (v/v) PEG400
to 1.8 A resolution. The overall structure of ST1585 contains thirteen beta-strands and nine alpha-helices. The asymmetric unit of the crystal contains two monomers, and one cis peptide bond is observed between Pro181 and Val182. The overall structure is made up of an alpha-beta-beta-alpha structure. The two-metal ion-binding center is located at the external edge of the beta-beta sandwich, and two zinc ions are coordinated with conserved amino acid residues located in segments 2 to 5
recombinant His-tagged selenomethionyl-labeled EstSTR1 free and with bound PMSF, vapor batch crystallization method, mixing of 9 mg/ml protein and 1 mM PMSF with reservoir solution containing 25% w/v polyethylene glycol 3350, 100-mM 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES) (pH 7.5), and 200-mM NaCl, 22°C, X-ray diffraction structure determination and analysis at 2.0 A resolution
hanging drop vapour diffusion method with 20% poly(ethylene)glycol 6 K in 0.1 M Tris (pH 8.0)
hanging drop vapour diffusion method with 20% poly(ethylene)glycol 6 K in 0.1 M Tris (pH 8.0)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
P28A
naturally occuring genetic variation, the P28A substitution occurs in the predicted N-terminal periplasmic signal peptide
H118A
site-directed mutant of CphA, generated and characterized, H118A and H196A mutations lead to a decrease of at least 1000fold in activity against carbapenems compared with the wild-type enzyme
H196A
site-directed mutant of CphA, generated and characterized, H118A and H196A mutations lead to a decrease of at least 1000fold in activity against carbapenems compared with the wild-type enzyme
N116H/N220G
N116H/N220G/K224Q
site-directed mutant of CphA, generated and characterized
N220G
kinetic parameters of the wild-type and N220G mutant enzymes are not significantly different
V67LFKHV
site-directed mutant of CphA, generated and characterized
E152C
ImiS mutant (ImiS[E152C]) is generated by mutating the imiS gene in pET26bimiS. Mutant exhibits very similar kinetic behavior to wild type
C221S
mutant catalytic activity on the burst phase is similar to that of the wild type BcII
D104A
-
km for benzylpenicillin and methicillin increased 2 fold, no change in catalytic activity
DELTA1-17
-
mutant lacking the first 17 residues, first alpha helix, reduced activity, no hydrolysis of cloxacillin
C221S
-
mutant catalytic activity on the burst phase is similar to that of the wild type BcII
-
D104A
-
km for benzylpenicillin and methicillin increased 2 fold, no change in catalytic activity
-
DELTA1-17
-
mutant lacking the first 17 residues, first alpha helix, reduced activity, no hydrolysis of cloxacillin
-
E166C
mutant constructed to obtain an engineered beta-lactamase that contains an environment-sensitive fluorophore conjugated near its active site to probe the structural dynamics of the omega-loop and to detect the binding of substrates. Mutant enzyme carrying a 6-bromoacetyl-2-dimethylaminonaphthalene label shows improved binding kinetics and positive fluorescence signal toward oxyimino-cephalosporins, but shows little such effect to non-oxyimino-cephalosporins. The omega-loop adopts a less stabilized structure, and readily undergoes conformational change to accommodate the binding of bulky oxyimino-cephalosporins while no such change is observed for non-oxyimino-cephalosporins
K234A
-
no significant structural change, mutant with decreased Km 1-2 orders of magnitude and kcat 2-3 orders of magnitude
K234E
-
no significant structural change, mutant with decreased Km 1-2 orders of magnitude and kcat 2-3 orders of magnitude
D170N
-
increase in Ki-value for clavulanic acid, little difference in the hydrolytic profile of beta-lactams compared to wild-type,no ceftazidime hydrolysis
K232N
-
increase in Ki-value for clavulanic acid, little difference in the hydrolytic profile of beta-lactams compared to wild-type
L316I
A233V
naturally occuring genetic variant
D130G/M154L
naturally occuring genetic variation
D130N/M154L
naturally occuring genetic variation
D66A
site-saturation mutagenesis at position 66, 8fold increase in minimum inhibitory concentration for ceftazidime compared with the wild type (0.25 to 2 microg/ml). Mutation results in only minor changes in steady-state protein levels
D66C
site-saturation mutagenesis at position 66. Expression of this variant is diminished relative to that of the other proteins
D66L
site-saturation mutagenesis at position 66, rise in resistance against ceftazidime compared with the wild type
D66M
site-saturation mutagenesis at position 66, rise in resistance against ceftazidime compared with the wild type. Mutation results in only minor changes in steady-state protein levels
D66N
site-saturation mutagenesis at position 66, mutation leads to a moderate enhancement of extended-spectrum cephalosporin resistance and an increase in cefepime and cefotaxime resistance. Mutation results in only minor changes in steady-state protein levels
D66W
site-saturation mutagenesis at position 66, mutation results in only minor changes in steady-state protein levels
D66Y
site-saturation mutagenesis at position 66, mutation results in only minor changes in steady-state protein levels
D95N
naturally occuring genetic variation
M154L
naturally occuring genetic variation
M154L/G222D
naturally occuring genetic variation
M182T/T195S/A224V
-
mutant selected by a directed evolution strategy. It is allosterically downregulated by Zn2+, Ni2+ and Co2+ with binding affinities around 300 microM
N152A
site-directed mutagenesis, 6300fold reduced kinetic efficiency compared to the wild-type enzyme
P226A
site-directed mutagenesis, the mutant has 92% reduced activity compared to wild-type
P252A
site-directed mutagenesis, the mutant has 85% reduced activity compared to wild-type
R274N/R276N
sitting-drop vapour-diffusion technique, surface-modified Toho-1 variant does not form merohedrally twinned crystals. Crystals diffract to a significantly higher resolution (0.97 A) than the wild-type crystals (1.65 A)
R276C
site-directed mutagenesis, the MICs of cefotaxime are clearly lower, clearly reduced catalytic efficiency towards cefotaxime. Investigation of the role of Arg276 in cefotaxime hydrolysis
R276G
site-directed mutagenesis, the MICs of cefotaxime are clearly lower, clearly reduced catalytic efficiency towards cefotaxime. Investigation of the role of Arg276 in cefotaxime hydrolysis
R276H
site-directed mutagenesis, investigation of the role of Arg276 in cefotaxime hydrolysis
R276N
site-directed mutagenesis, investigation of the role of Arg276 in cefotaxime hydrolysis
R276S
site-directed mutagenesis, the MICs of cefotaxime are clearly lower, clearly reduced catalytic efficiency towards cefotaxime. Investigation of the role of Arg276 in cefotaxime hydrolysis
R276W
site-directed mutagenesis, the MICs of cefotaxime are clearly lower, clearly reduced catalytic efficiency towards cefotaxime. Investigation of the role of Arg276 in cefotaxime hydrolysis
R61H/E64H/43H
-
circularly permuted enzyme, created by rational design. Mutant shows little regulation upon metal ion binding except for a weak activation with Zn2+
S287N
the AmpC variants AmpC-A and AmpC-B2 harboring the S287N substitution are obtained by mutagenesis from cephalosporinases representative of the phylogenetic groups A and B2 of Escherichia coli. Their biochemical characterization reveals that the S287N replacement leads to an important increase in the catalytic efficiency toward extended-spectrum cephalosporins in the AmpC beta-lactamase of group A only
V88L/M154L
naturally occuring genetic variation
W229A
site-directed mutagenesis, the mutant has 98% reduced activity compared to wild-type
W229F
site-directed mutagenesis, the mutant has 84% reduced activity compared to wild-type
W229Y
site-directed mutagenesis, the mutant has 82% reduced activity compared to wild-type
W290F
-
activity and spectroscopic properties of the mutant enzyme does not differ significantly from those of the wild type, indicating that the mutation has only a very limited effect on the structure of the protein. The stability of the folded protein is reduced, however, by 5-10 kJ mol-1 relative to that of the molten globule intermediate (H), but the values of the folding rate constants are unchanged, suggesting that Trp290 becomes organized in its native like environment only after the rate-limiting step, i.e., the C-terminal region of the enzyme folds very late
N152A
-
site-directed mutagenesis, 6300fold reduced kinetic efficiency compared to the wild-type enzyme
-
W290F
-
activity and spectroscopic properties of the mutant enzyme does not differ significantly from those of the wild type, indicating that the mutation has only a very limited effect on the structure of the protein. The stability of the folded protein is reduced, however, by 5-10 kJ mol-1 relative to that of the molten globule intermediate (H), but the values of the folding rate constants are unchanged, suggesting that Trp290 becomes organized in its native like environment only after the rate-limiting step, i.e., the C-terminal region of the enzyme folds very late
-
E240V
E240V
D104E
mutation results in a 1000fold enhancement in binding affinity to beta-lactamase inhibitor protein BLIP, as it restores a salt bridge to BLIP. Mutation of a neighboring residue, BLIP E73M, results in salt bridge formation between SHV-1 D104 and BLIP K74 and a 400fold increase in binding affinity. BLIP F142 cooperatively stabilizes both interactions
D223A
site-directed mutagenesis, the mutation does not signifcantly affect resistance of the cells against antibiotics
E152A
site-directed mutagenesis, the mutant shows highly declined resistance to antibiotics compared to wild-type NDM-7
E152A/S191A
site-directed mutagenesis, the double mutant shows 2fold reduced antibiotic resistance compared to single mutants, but substantially declined resistance compared to wild-type NDM-7
E162A
site-directed mutagenesis, mutation of the an omega loop glutamate, the mutant shows reduced activity against penicilin and cepahlosporin antibiotics in recombinant Escherichia coli cells and reduces the resistance level of the cells
E164A
site-directed mutagenesis, mutation of the an omega loop glutamate, the mutant shows highly reduced activity against penicilin and cepahlosporin antibiotics in recombinant Escherichia coli cells and potently reduces the resistance level of the cells
E167A
site-directed mutagenesis, mutation of the an omega loop glutamate, the mutant shows reduced activity against penicilin and cepahlosporin antibiotics in recombinant Escherichia coli cells and reduces the resistance level of the cells
G69S/A74T/G200R
naturally occuring genetic variation
K216A
site-directed mutagenesis, the mutation does not signifcantly affect resistance of the cells against antibiotics
S130G
S191A
site-directed mutagenesis, mutant shows highly declined resistance to antibiotics compared to wild-type NDM-7
S213A
site-directed mutagenesis, the mutation does not signifcantly affect resistance of the cells against antibiotics
E162A
Klebsiella pneumoniae MTCC 3384
-
site-directed mutagenesis, mutation of the an omega loop glutamate, the mutant shows reduced activity against penicilin and cepahlosporin antibiotics in recombinant Escherichia coli cells and reduces the resistance level of the cells
-
E164A
Klebsiella pneumoniae MTCC 3384
-
site-directed mutagenesis, mutation of the an omega loop glutamate, the mutant shows highly reduced activity against penicilin and cepahlosporin antibiotics in recombinant Escherichia coli cells and potently reduces the resistance level of the cells
-
E167A
Klebsiella pneumoniae MTCC 3384
-
site-directed mutagenesis, mutation of the an omega loop glutamate, the mutant shows reduced activity against penicilin and cepahlosporin antibiotics in recombinant Escherichia coli cells and reduces the resistance level of the cells
-
D223A
Klebsiella pneumoniae NDM-7
-
site-directed mutagenesis, the mutation does not signifcantly affect resistance of the cells against antibiotics
-
E152A
Klebsiella pneumoniae NDM-7
-
site-directed mutagenesis, the mutant shows highly declined resistance to antibiotics compared to wild-type NDM-7
-
K216A
Klebsiella pneumoniae NDM-7
-
site-directed mutagenesis, the mutation does not signifcantly affect resistance of the cells against antibiotics
-
S191A
Klebsiella pneumoniae NDM-7
-
site-directed mutagenesis, mutant shows highly declined resistance to antibiotics compared to wild-type NDM-7
-
S213A
Klebsiella pneumoniae NDM-7
-
site-directed mutagenesis, the mutation does not signifcantly affect resistance of the cells against antibiotics
-
E166A
site-directed mutagenesis, inactive mutant. The Glu166Ala mutant form of BlaC has no hydrolytic activity and forms a stable acyl-enzyme complex that can be structurally characterized, suggesting that Glu166 is required for deacylation and product release
K73A
E166A
-
site-directed mutagenesis, inactive mutant. The Glu166Ala mutant form of BlaC has no hydrolytic activity and forms a stable acyl-enzyme complex that can be structurally characterized, suggesting that Glu166 is required for deacylation and product release
-
K73A
E193A
site-directed mutagenesis, the mutant shows 30% reduced activity compared to the wild-type enzyme. In vivo expression of 4455E193A reduces the beta-lactam resistance for penicillin and ampicillin by twofold as compared to the expression of wild-type MSMEG_4455
Y194F
site-directed mutagenesis, the mutant shows 62% reduced activity compared to the wild-type enzyme
E193A
-
site-directed mutagenesis, the mutant shows 30% reduced activity compared to the wild-type enzyme. In vivo expression of 4455E193A reduces the beta-lactam resistance for penicillin and ampicillin by twofold as compared to the expression of wild-type MSMEG_4455
-
Y194F
-
site-directed mutagenesis, the mutant shows 62% reduced activity compared to the wild-type enzyme
-
E193A
-
site-directed mutagenesis, the mutant shows 30% reduced activity compared to the wild-type enzyme. In vivo expression of 4455E193A reduces the beta-lactam resistance for penicillin and ampicillin by twofold as compared to the expression of wild-type MSMEG_4455
-
Y194F
-
site-directed mutagenesis, the mutant shows 62% reduced activity compared to the wild-type enzyme
-
T237A
plasmid pBC
-
the mutant enzyme exhibits elevated MICs for ampicillin, piperacillin, and the beta-lactambeta-lactamase inhibitor combinations. The T237A mutant enzyme demonstrates a lower kcat/Km for imipenem, cephalothin, and cefotaxime. The T237A mutant enzyme shows increased Kis for clavulanic acid, sulbactam, and tazobactam
T237S
plasmid pBC
-
the mutant enzyme maintains MICs equivalent to those of the wild type against all of the beta-lactams tested, including carbapenems. The mutant enzyme displays substrate kinetics similar to those of the wild-type KPC-2 enzyme. The T237S mutant enzyme displays Kis similar to wilde-type enzyme
N166A/170G
plasmid pBG66
-
kcat/KM for ampicillin is 725fold lower than wild-type value, kcat/KM for penicillin G is 850fold lower than wild-type value
N170A
plasmid pBG66
-
kcat/KM for ampicillin is 17fold lower than wild-type value, kcat/KM for penicillin G is 6fold lower than wild-type value, kcat/KM for cephalexin is 10fold lower than wild-type value, kcat/KM for cephalothin is 5fold lower than wild-type value
N170G
plasmid pBG66
-
very efficient at hydrolyzing substrates that contain a primary amine in the antibiotic R-group that would be close to the Asn170 side chain in the acyl-intermediate. The X-ray structure of the N170G enzyme indicates that the position of an active site water important for deacylation is altered compared with the wild-type enzyme. N170G TEM-1 hydrolyzes ampicillin efficiently because of substrate-assisted catalysis where the primary amine of the ampicillin R-group positions the hydrolytic water and allows for efficient deacylation. kcat/KM for ampicillin is 3.5fold lower than wild-type value, kcat/KM for penicillin G is 1.6fold lower than wild-type value, kcat/KM for cephalexin is 1.7fold lower than wild-type value, kcat/KM for cephalothin is 40fold lower than wild-type value
W154F
plasmid pGEM-T-easy
-
noncarboxylated enzymes which displays poor catalytic efficiencies and reduced stability when compared to the wild-type OXA-10
W154G
plasmid pGEM-T-easy
-
noncarboxylated enzymes which displays poor catalytic efficiencies and reduced stability when compared to the wild-type OXA-10
W154H
plasmid pGEM-T-easy
-
noncarboxylated enzymes which displays poor catalytic efficiencies and reduced stability when compared to the wild-type OXA-10
G240H
plasmid pQE32Chl17
-
kcat/Km for cefotaxime is 5fold higher than wild-type value, kcat/Km for cephalothin is 6.4fold higher than wild-type value, kcat/Km for cefazolin is 2.3fold higher than wild-type value, kcat/Km for benzylpenicillin is 3.9fold lower than wild-type value
K104E
-
thermal stability is increased, mutant enzyme loses activity against oxyimino-cephgalosporins, aztreonam, and ampicillin
P51L
-
thermal stability is greatly decreased, mutant enzyme loses activity against cefotaxime and exhibits a reduced catalytic efficiency with penicillins and aztreonam, no inhibition by beta-odopenicillanate
S164E
-
thermal stability is increased, mutant enzyme loses activity against ceftazidime
R234K
site-directed replacement mutagenesis, about 4fold reduced catalytic efficiency compared to the wild-type enzyme
Y218F
substitution may be responsible for the reduced catalytic efficiency against certain cephalosporins, including ceftazidime and cefepime
D120A
kcat/KM is up to 425000fold lower than the wild-type enzyme. Ki-value for phosphate is 450fold lower than wild-type value
D120E
kcat/KM is up to 136000fold lower than the wild-type enzyme. the Zn-Zn distance is increased by 0.3 A compared with wild-type enzyme
D120C
site-directed mutagenesis, reduced activity and metal binding compared to the wild-type enzyme
D120N
site-directed mutagenesis, reduced activity and metal binding compared to the wild-type enzyme
D120S
site-directed mutagenesis, reduced activity and metal binding compared to the wild-type enzyme
H116C
site-directed mutagenesis. Mutant binds 0.33 equiv of Zn2+
H121C
site-directed mutagenesis. Mutant binds 0.11 equiv of Zn2+
N276D
-
reduced susceptibility to ampicillin/clavulanate while maintaining high-level resistance to ampicillin. Slightly diminished kcat/Km for all substrates tested. 5-fold increase in Ki for clavulanate and a 40% reduction in kinact/KI
A751G
G984A
A751G
additional information
N116H/N220G
mutant enzyme with a broader specificity than wild type CphA
N116H/N220G
site-directed mutant of CphA, generated and characterized
L316I
-
substitution is located within the R2 loop that is considered the hotspot region responsible for the extended substrate spectrum in class C beta-lactamases
L316I
-
substitution is located within the R2 loop that is considered the hotspot region responsible for the extended substrate spectrum in class C beta-lactamases
-
E240V
substitution increases catalytic efficiency toward ceftazidime
S130G
-
site-directed mutagenesis, resistant to inhibition by taxobactam in contrast to the wild-type enzyme
S130G
-
mutant resistant to tazobactam, sulbactam, clavulanic acid, and 2'-glutaroxy penem sulfone
K73A
site-directed mutagenesis, inactive mutant, substrate/inhibitor binding structure
K73A
site-directed mutagenesis, inactive mutant. The Lys73Ala mutant form of BlaC permits the structural identification of the Michaelis complex, but has no catalytic activity, indicating Lys73 is essential for the acylation step
K73A
-
site-directed mutagenesis, inactive mutant. The Lys73Ala mutant form of BlaC permits the structural identification of the Michaelis complex, but has no catalytic activity, indicating Lys73 is essential for the acylation step
-
K73A
-
site-directed mutagenesis, inactive mutant, substrate/inhibitor binding structure
-
A751G
in the ampC gene from strain Y56 the A751G mutation is responsible for the inactivation of beta-lactamase
A751G
-
in the ampC gene from strain Y56 the A751G mutation is responsible for the inactivation of beta-lactamase
-
additional information
-
construction of diverse mutants of the beta-lactamase inhibitor protein BLIP by alanine scanning mutation
additional information
replacement, separately or simultaneously, three of the ESBL alpha helices with prototype amphiphatic helices from a catalog of secondary structure elements. Although the substitutes bear no sequence similarity to the originals and pertain to unrelated protein families, all the engineered ESBL variants fold in native like structures with in vitro and in vivo enzymic activity. The triple substituted variant resembles a primitive protein, with folding defects such as a strong tendency to oligomerization and very low stability. It mimics a non homologous recombinant abandoning the family sequence space while preserving fold
additional information
-
replacement, separately or simultaneously, three of the ESBL alpha helices with prototype amphiphatic helices from a catalog of secondary structure elements. Although the substitutes bear no sequence similarity to the originals and pertain to unrelated protein families, all the engineered ESBL variants fold in native like structures with in vitro and in vivo enzymic activity. The triple substituted variant resembles a primitive protein, with folding defects such as a strong tendency to oligomerization and very low stability. It mimics a non homologous recombinant abandoning the family sequence space while preserving fold
additional information
-
analysis of 516 mutated enzymes that acquired the ceftazidime-hydrolyzing activity, and identification of twelve positions with single amino acid substitutions, co-localized at the active-site pocket area. single amino acid substitutions are found at positions C89, N136, L162, R164, E166, L169, N170, T171, A172, P174, D176, D179. All substitutions cause a congruent effect, expanding the space in a conserved structure called the omega loop, which in turn increased flexibility at the active site
additional information
-
large scale mutant screening, construction of four deletion mutations in a class A beta-lactamase PenA, each conferring an extended substrate spectrum. Single-amino-acid deletions T171del, I173del, and P174del and a two-amino-acid deletion, R165_T167delinsP, occurr in the omega loop, increasing the flexibility of the binding cavity. The four additional deletion mutations in PenA extend the substrate spectrum, in addition to the characterized E168del mutation. The mutations are potential future mutations conferring high-level ceftazidime resistance on isolates from clinical settings, compared with amino acid substitution mutations. MIC values of mutant enzymes for antibiotics ceftazidime, amoxicillin, amoxicillin-clavulanic acid, cefotaxime, ceftriaxone, cefepime, and meropenem, overview. None of the deletion mutations confer resistance to cefepime, a fourth-generation cephalosporin, or to meropenem, a carbapenem subgroup member, but the deletion mutations exhibit various profiles of resistance to expanded-spectrum cephalosporins
additional information
construction of diverse mutants of the beta-lactamase inhibitor protein BLIP by alanine scanning mutation
additional information
-
lactamase CoCo-L1, enzyme containing transition metal ions other than Zn(2+), prepared and characterized by kinetic and spectroscopic studies
additional information
-
lactamase Cu-L1, Cu-containing analog of metallo-beta-lactamase L1. Enzyme containing transition metal ions other than Zn(2+), prepared and characterized by kinetic and spectroscopic studies
additional information
-
lactamase Ni-L1, Ni-containing analog of metallo-beta-lactamase L1. Enzyme containing transition metal ions other than Zn(2+), prepared and characterized by kinetic and spectroscopic studies
additional information
-
lactamase NiZn-L1, enzyme containing transition metal ions other than Zn(2+), prepared and characterized by kinetic and spectroscopic studies
additional information
-
lactamase ZnCo-L1, enzyme containing transition metal ions other than Zn(2+), prepared and characterized by kinetic and spectroscopic studies
additional information
-
lactamase ZnFe-L1, enzyme containing transition metal ions other than Zn(2+), prepared and characterized by kinetic and spectroscopic studies
additional information
-
lactamase ZnNi-L1, enzyme containing transition metal ions other than Zn(2+), prepared and characterized by kinetic and spectroscopic studies
additional information
-
lactamase ZnZn-L1, enzyme containing transition metal ions other than Zn(2+), prepared and characterized by kinetic and spectroscopic studies
additional information
identification of two variants that confer elevated resistance to cefotaxime but decreased resistance to other antibiotics. These variants are circularly permuted in the omega-loop proximal to the active site. One variant is circularly permuted such that the key catalytic residue Glu166 is located at the N-terminus of the mature protein
additional information
insertion of a circularly permuted TEM-1 beta-lactamase gene into the maltose binding protein leads to protein RG13, which exhibits allostery. RG13 is positively regulated by maltose yet is inhibited by Zn2+ at low millimolar concentration. The structure reveals that the maltose binding protein and TEM-1 domains are in close proximity connected via two linkers and a zinc ion bridging both domains. By bridging both TEM-1 and MBP, Zn2+ acts to twist tie the linkers thereby partially dislodging a linker between the two domains from its original catalytically productive position in TEM-1. This linker 1 contains residues normally part of the TEM-1 active site including the critical beta3 and beta4 strands important for activity. Mutagenesis of residues comprising the crystallographically observed Zn2+ site only slightly affect Zn2+ inhibition 2- to 4fold. Structural analysis indicates that the linker attachment sites on maltose binding protein are at a site that, upon maltose binding, harbors both the largest local Calpha distance changes and displays surface curvature changes. Maltose activation and zinc inhibition of RG13 are hypothesized to have opposite effects on productive relaxation of the TEM-1 beta3 linker region via steric and/or linker juxtapositioning mechanisms
additional information
no significant loss in thermal stability for the point mutants compared to the wild-type enzyme
additional information
construction of diverse mutant of the beta-lactamase inhibitor protein BLIP by alanine scanning mutation
additional information
TEM-107 extended-spectrum beta-lactamase detected in a Klebsiella pneumoniae clinical isolate has a Gly238Ser substitution compared to the TEM-43 beta-lactamase
additional information
-
TEM-107 extended-spectrum beta-lactamase detected in a Klebsiella pneumoniae clinical isolate has a Gly238Ser substitution compared to the TEM-43 beta-lactamase
additional information
-
the amino acid substitutions N132G, R164A, R244A, and R276E explain the broad specificity of the enzyme, relatively low penicillinase activity, and resistance to clavulanic acid
additional information
generation of an enzyme-deletion mutant of strain CIP104536
additional information
-
generation of an enzyme-deletion mutant of strain CIP104536
additional information
-
generation of an enzyme-deletion mutant of strain CIP104536
-
additional information
plasmid pQE32Chl17
-
investigation of the potential for increased recognition of an extended-spectrum cephalosporin by targeted sequence variation in TEM-1
additional information
-
a VIM-2 enzyme inserted in integron In58, in an isolate from a female cystic fibrosis patient, is resistant to all antimicrobial agents tested except colistin, this isolate presented a unique random amplified polymorphic DNA, RAPD, type, overview
additional information
-
identification of blaSHV gene mutants SHV-2a, SHV5 et SHV1, that do not seem to be ESBLs, overview
additional information
overproduction of a metallo-beta-lactamase by a strong promoter causes high-level imipenem resistance in a strain KG2505, PAO1 derivative without an AmpC beta-lactamase and a Mex-AB-OprM efflux pump, derived from a clinical human isolate of Pseudomonas aeruginosa, overview
additional information
-
overproduction of a metallo-beta-lactamase by a strong promoter causes high-level imipenem resistance in a strain KG2505, PAO1 derivative without an AmpC beta-lactamase and a Mex-AB-OprM efflux pump, derived from a clinical human isolate of Pseudomonas aeruginosa, overview
additional information
-
construction of diverse mutants of the beta-lactamase inhibitor protein BLIP by alanine scanning mutation
additional information
gene knockout mutant, KJDELTAL1. Induction of the L1 and L2 genes is differentially regulated
additional information
gene knockout mutant, KJDELTAL1. Induction of the L1 and L2 genes is differentially regulated
additional information
gene knockout mutant, KJDELTAL2. Induction of the L1 and L2 genes is differentially regulated
additional information
gene knockout mutant, KJDELTAL2. Induction of the L1 and L2 genes is differentially regulated
additional information
-
gene knockout mutant, KJDELTAL1. Induction of the L1 and L2 genes is differentially regulated
-
additional information
-
gene knockout mutant, KJDELTAL2. Induction of the L1 and L2 genes is differentially regulated
-
additional information
-
mutagenesis is performed to better understand the basis of the inhibitor-resistant phenotype in SHV, examination of the role of a second-shell residue, Asn276
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 10
7.2 - 8
-
at pH values higher than 7.2 a decrease of the enzyme activity is observed, having lost 50% at pH 8.0
690020
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 55
thermal stability of TEM-149 wild-type and TEM-149T182M mutant is determined by measuring the residual activity after incubation of the enzymes at three different temperatures: 25°C, 40°C, and 55°C. TEM-149 wild-type exhibits half-lives of 90 min at 25°C, 70 min at 40°C, and 30 min at 55°C, whereas TEM-149T182M mutant shows half-lives greater than 120 min at 25°C and 40°C and 45 min at 55°C. Compared to the thermal stability of TEM-149, the thermal stability of the TEM-149T182M mutant is substantially increased
37 - 55
-
residual activity of 82% after 25 min at 37°C and complete loss of activity after 1 min at 60°C or 5 min at 55°C
39.9
plasmid pGEM-T-easy
-
t1/2 for mutant enzyme W154A, in presence of 1.1 mM sodium bicarbonate
40 - 55
the enzyme exhibits a half-life of 90 min at 40°C, 25 min at 45°C, and less than 1 min at 55°C
41.9
plasmid pGEM-T-easy
-
t1/2 for mutant enzyme W154G, in presence of 1.1 mM sodium bicarbonate
42
-
30 min, mutant enzyme R146S is stable, mutant enzyme K104E loses 50% of maximal activity, mutant enzyme P51L loses 95% of maximal activity, wild-type enzyme loses 80% of maximal activity
48
the wild-type Tm is around 48°C occurring over a temperature range of about 23°C (35-58°C) for both the wild-type and the three W229 mutants
48.8
plasmid pGEM-T-easy
-
t1/2 for mutant enzyme W154F, in presence of 1.1 mM sodium bicarbonate
50
50.7
plasmid pGEM-T-easy
-
t1/2 for mutant enzyme W154G, in presence of 50 mM sodium bicarbonate
53.5
plasmid pGEM-T-easy
-
t1/2 for mutant enzyme W154F, in presence of 50 mM sodium bicarbonate
55.1
melting temperature of the purified NDM-1 variant
55.9
plasmid pGEM-T-easy
-
t1/2 for wild-type enzyme, in presence of 1.1 mM sodium bicarbonate
56.7
plasmid pGEM-T-easy
-
t1/2 for mutant enzyme W154A, in presence of 50 mM sodium bicarbonate
59.5
melting temperature of the purified NDM-1 variant
60
61.4
melting temperature of the purified NDM-1 variant
63.4
melting temperature of the purified NDM-1 variant
64.6
melting temperature of the purified NDM-1 variant
72.1
melting temperature of the purified NDM-1 variant
60
-
total loss of activity, immobilized enzyme bound to aminoethyl cellulose still active at 62°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50 mM sodium phosphate buffer, pH 6.8, 50% glycerol
20C, 1 year, no loss of activity
crude extract, HCl buffer, 0.05 M triethanolamine, 4 days, 50% loss of activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Sephadex G75 gel filtration, and DEAE-cellulose column chromatography
-
CTX-M-1 wild-type and six derived mutants are purified by affinity chromatography
gene macQ, recombinant His-tagged enzyme from Escherichia coli strain Origami 2(DE3) by nickel affinity chromatography
AB702957
High Load Q Sepharose column chromatography, MonoP HR5/20 column chromatography, and Superdex 75 gel filtration
ion-exchange chromatography
Ni-NTA agarose column chromatography and Superdex 200 Hi-Load gel filtration
-
Ni-NTA column chromatography
Ni2+-loaded HiTrap chelating column chromatography and Superdex 200 gel filtration
-
Q Sepharose column chromatography, SP-Sepharose column chromatography, and gel filtration
Q-Sepharose column chromatography and S-Sepharose column chromatography
recombinant active N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography to homogeneity
recombinant cobalt-cobtaining enzyme from Escherichia coli strain BL21(DE3) by cobalt affinity chromatography
recombinant enzyme from Escherichia coli strain BL21(DE3) by ultrafiltration and anion exchange chromatography
recombinant enzyme from Escherichia coli, 31.3fold by ammonium sulfate precipitation and Zn2+-affinity chromatography
-
recombinant enzyme IMP-2 from Escherichia coli strain HB101 harboring pBC SK(+) by cation exchange chromatography, ultrafiltration and gel filtration, to over 95% purity
recombinant His-tagged enzyme from Escherichia coli BL21(DE3)/pLysS by nickel affinity chhromatography and gel filtration
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography and two different steps of gel filtration, followed by diafiltration
-
recombinant His-tagged selenomethionyl-EstSTR1 from Escherichia coli strain B834 (DE3) by affinity chromatography and gel filtration
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage by thrombin, and gel filtration
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, cleavage of the N-terminal His6-tag using recombinant human Rhinovirus 3C protease, and further purification of the untagged protein by affinity chromatography, followed by ultrafiltration
recombinant N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
recombinant wild-type and mutant enzymes from Escherichia coli
recombinant wild-type and mutant R234K from Escherichia coli BL21(DE3)
S-Sepharose column chromatography and Q-Sepharose column chromatography
Sephadex G-100 column chromatography, CM-Sepharose column chromatography
VIM-6 enzyme is purified from the culture supernatant of 800 ml of stationary-phase culture grown with anion exchange chromatography and gel filtration.
wild type OXA-1 purified by CM-cellulose chromatography and His6-tagged wild type OXA-1 purified by nickel-affinity chromatography
-
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, cleavage of the N-terminal His6-tag using recombinant human Rhinovirus 3C protease, and further purification of the untagged protein by affinity chromatography, followed by ultrafiltration
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, cleavage of the N-terminal His6-tag using recombinant human Rhinovirus 3C protease, and further purification of the untagged protein by affinity chromatography, followed by ultrafiltration
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, cleavage of the N-terminal His6-tag using recombinant human Rhinovirus 3C protease, and further purification of the untagged protein by affinity chromatography, followed by ultrafiltration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
beta-lactamase genes, DNA and amino acid sequence determination and analysis
-
carbapenemase activity of MBL results from acquisition of carbapenemase-encoding determinants via horizontal gene transfer, overview
chromosome-encoded metallo-beta-lactamase, genotyping in Aliivibrio isolates, recombinant enzyme overexpression in Escherichia coli
cloned into a multicopy plasmid and expressed in Escherichia coli and Pseudomonas aeruginosa
construction of the expression system for overproduction of VIM-6 in Escherichia coli
diverse multidrug resistant extended-spectrum beta-lactamase-producing Escherichia coli strains among uropathogens of pediatrics in north of Iran are isolated and tested by PCR for the presence or absence of CTX, TEM, SHV, GES, and VEB beta-lactamase genes, genotyping
-
DNA and amino acid sequence determination and analysis, expression in Escherichia coli
-
DNA and amino acid sequence determination and analysis, PCR screening for MBL variants in cystic fibrosis patient isolates of Pseudomonas aeruginosa in Portugal, overview
-
Escherichia coli strain HB101 is used as the host for the recombinant plasmids
-
expressed in Bacillus subtilis
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli TG1
expressed in Escherichia coli Top10 cells
expressed in Escherichia coli, Bacillus subtilis, Bacillus stearothermophilus
-
expression in Escherichia coli
expression of wild-type and mutant enzymes in Escherichia coli
expression of wild-type and mutant R234K in Escherichia coli BL21(DE3)
gene blaACT-12, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene blaACT-14, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene blaACT-15, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene blaACT-17, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene blaACT-18, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene blaACT-19, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene blaACT-22, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene blaC, DNA and amino acid sequence determination and analysis, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene blaCMY-2, DNA and amino acid sequence determination and analysis, genotyping of the bla gene in 14 pAmpC-producing Escherichia coli strains, 11 sequence types are found, genomic relationships analysis
gene blaCMY-65, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene blaCMY-67, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene blaCMY-68, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene blaCMY-70, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene blaCMY-71, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene blaCMY-74, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene blaCMY-83, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene blaCMY-93, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene blaCTX-M-14, extended-spectrum beta-lactamases (ESBL), genotyping
gene blaCTX-M-15, extended-spectrum beta-lactamases (ESBL), genotyping
gene blaCTX-M-27, extended-spectrum beta-lactamases (ESBL), genotyping
gene blaCTX-M-55, extended-spectrum beta-lactamases (ESBL), genotyping
gene blaFOX-4, recombinant expression in Escherichia coli strain BL21(DE3)
-
gene blaIMP-1, quantitative expression analysis in 124 different strains, among metallo-beta-lactamase-producing Gram-negative rods in Japan, 84.45% are blaIMP-1 or blaIMP-2
gene blaIMP-10, DNA and amino acid sequence determination and analysis, promoter analysis, overexpression of metallo-beta-lactamase IMP-10 by the strong promoter of gene blaIMP-10 in Pseudomonas aeruginosa strain KG2505, overview. Genetic structure of the class 1 integron carrying the blaIMP-10 cassette, overview
gene blaIMP-15, the blaIMP-15 gene cassette is inserted in a plasmid-borne integron with a unique array of gene cassettes and named In95, genotyping for beta-lactamase genes in human isolates from a hospital in Mexico, overview. Genetic structure in strain 4677, overview, transformations of plasmid preparations of strains 4677 and 4663 by electroporation into Escherichia coli strain DH10B and Pseudomonas aeruginosa strain PU21
gene blaIMP-2, recombinant expression in Escherichia coli strain HB101 harboring pBC SK(+)
gene blaKPC-2, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene blaNDM-1, genotyping, recombinant N-terminally His6-tagged enzyme expression in Escherichia coli strain BL21(DE3)
gene blaNDM-10, genotyping, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene blaNDM-12, genotyping, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene blaNDM-2, genotyping, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene blaNDM-3, genotyping, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene blaNDM-4, genotyping, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene blaNDM-5, genotyping, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene blaNDM-6, genotyping, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene blaNDM-7, genotyping, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene blaNDM-7, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strains BL21(DE3) and CS109, subcloning in Escherichia coli strain XL-1 Blue. Host Escherichia coli strain CS109 harbouring cloned blaNDM-7 displays a resistant status with over 60fold increased resistance compared to control strain CS109 for all penicillins, cephalosporin and carbapenems tested
gene blaNDM-8, genotyping, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene blaNDM-9, genotyping, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene blaOXA-1, recombinant expression in Escerichia coli strain BL21(DE3)
gene blaSHV-14, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strains BL21(DE3) and CS109. On expression, the clone of wild-type SHV-14 aggravates the resistance of host by 60-500 folds against penicillin and cephalosporin groups of antibiotics, while the expression of mutated enzymes (especially E164A) substantially reduces the resistance level as compared to the wild-type, and the results are in synchrony with the estimated enzymatic efficiencies of wild-type and mutated proteins
gene blaTEM-1, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene blaVIM, genotyping for beta-lactamase genes in human isolates from a hospital in Mexico, overview. Genetic structure in strain 4677, overview, transformations of plasmid preparations of strains 4677 and 4663 by electroporation into Escherichia coli strain DH10B and Pseudomonas aeruginosa strain PU21
gene blaVIM-2, recombinant Co2+-enzyme expression in Escherichia coli strain BL21(DE3) in in minimal medium
gene blaVIM-7, located on a plasmid (p07-406), DNA and amino acid sequence determination and analysis
gene estSRT1, recombinant expression of His-tagged enzyme in Escherichia coli strain B834 (DE3) as selenomethionyl-EstSTR1
gene macQ, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, recombinant expression of His-tagged enzyme in Escherichia coli strain Origami 2(DE3). Recombinant plasmid (pMQ28) confers 2 to 16fold higher MIC values toward all six beta-lactam antibiotics in Escherichia coli Origami 2(DE3) than the strain with a control vector. This indicates that MacQ confers multiple beta-lactam antibiotic resistance on a host strain by hydrolyzing beta-lactam antibiotics
AB702957
gene MSMEG_4455, DNA and amino acid sequence determination and analysis, recombinant ectopic expression of wild-type and mutant enzymes in beta-lactamase-deficient Escherichia coli mutant strain AM1OC-1, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene OXA24, recombinant expression in Escerichia coli strain BL21(DE3)
gene oxa40, DNA and amino acid sequence determination and analysis, the gene is encoded on a plasmid
-
gene SMB-1, recombinant expression of Hhis-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
-
genes blaOXA-10, blaVIM-2, blaPSE-I, blaOXA-4, blaOXA-17, blaOXA-30, DNA and amino acid sequence determination and analysis, genotyping in human isolates and correlation of amikain resistance, overview
-
genes blaPER-1 and blaVIM-2, DNA and amino acid sequence determination and analysis
-
genes blaVIM and blaIMP, DNA and amino acid sequence determination and analysis, overview
-
genes blaVIM1 and blaVIM-13, genetic structure and genotyping, VIM-13 is harbored in a class 1 integron, along with an A108T variant of the aminoglycoside-modifying enzyme encoding gene aacA4, which confers resistance to gentamicin and tobramycin
genotyping and identification of beta-lactamase by PCR amplification followed by sequencing of bla genes
-
genotyping and phenotyping of Escherichia coli strains with beta-lactamase activity in faeces from ducks
-
genotyping and phenotyping of Klebsiella strains with beta-lactamase activity in faeces from ducks
-
genotyping and phenotyping of Salmonella strains with beta-lactamase activity in faeces from ducks
-
genotyping and screening of clinical isolates from human patients, sequencing of gene bla-VIM in MBl variant VIM-2, random amplified polymorphic DNA, RAPD, types, overview
-
genotyping of IMP-9 MBL variants in Pseudomonas aeruginosa patient isolates with multi-drug resistance phenotype, overview
identification of SHV-type extended spectrum beta-lactamase genes in Pseudomonas aeruginosa by PCR-restriction fragment length polymorphism and insertion site restriction-PCR, genotyping, overview
-
macrorestriction profiling of chromosomal DNA from 30 isolates and identification of two different clonal lineages, named cluster A, serotype O11, and cluster B, serotype O12, that produce VIM-1 and VIM-2 MBLs, respectively. The VIM-2-producing isolates from Italy carried identical, or very similar, allelic forms of the oprD gene, harbour a common class 1 integron, belong to the same multilocus sequence type, and show macrorestriction profiles that are related to those of the MBL-negative French strains, overview
Mox-1 is a unique plasmid-mediated class C beta-lactamase, recombinant expression of His-tagged enzyme in Escherichia coli BL21(DE3)/pLysS
pMB19-2 plasmid, expression in Escherichia coli
screening for genes blaIMP-1, blaVIM and blaVIM-2 in clinical human isolates from a university hospital in Sichuan, China, genotyping and antimicrobial susceptibility, overview
-
the ECA2849 ORF is cloned and expressed in recombinant Escherichia coli strain
gene blaCTX-M-14, extended-spectrum beta-lactamases (ESBL), genotyping
gene blaCTX-M-14, extended-spectrum beta-lactamases (ESBL), genotyping
gene blaCTX-M-15, extended-spectrum beta-lactamases (ESBL), genotyping
gene blaCTX-M-15, extended-spectrum beta-lactamases (ESBL), genotyping
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
refolding of recombinant enzyme from periplasmic protein pellets by resuspension in 5 mL 50 mM Tris buffer, pH 7.8, with addition pf 10 ml 8 M urea
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
-
diagnostic utility of the combination of Syn 2190 and cefotetan in a disk test for the detection of clinical isolates of Klebsiella sp. producing plasmid-mediated AmpC beta-lactamases. The sensitivity of this test is 91%, the specificity is 100%, and the reproducibility is 100%
drug development
medicine
pharmacology
synthesis
drug development
the enzyme is a target for treatment of Mycobacterium abscessus infections
drug development
ZINC01807204 might be useful as a lead molecule for further optimization and development of more potent non beta-lactam inhibitors against KPC-2
drug development
enzyme BlaC is a rational enzyme target for therapeutic agents in treatment of tuberculosis caused by Mycobacterium tuberculosis
drug development
the PWP triad is an evolutionarily conserved motif unique to class A beta-lactamases aligning its allosteric site and hence is an effective potential target for enzyme regulation and selective drug design
drug development
-
ZINC01807204 might be useful as a lead molecule for further optimization and development of more potent non beta-lactam inhibitors against KPC-2
-
drug development
-
the enzyme is a target for treatment of Mycobacterium abscessus infections
-
drug development
-
enzyme BlaC is a rational enzyme target for therapeutic agents in treatment of tuberculosis caused by Mycobacterium tuberculosis
-
drug development
-
enzyme BlaC is a rational enzyme target for therapeutic agents in treatment of tuberculosis caused by Mycobacterium tuberculosis
-
medicine
-
putative development of a screening of MBL producing strains by routine clinical microbiology laboratories. The detection of the MBL phenotype of resistance is of crucial importance for selecting the most appropriate therapy and applying infection control measures
medicine
-
putative development of a screening of MBL producing strains by routine clinical microbiology laboratories. The detection of the MBL phenotype of resistance is of crucial importance for selecting the most appropriate therapy and applying infection control measures
medicine
-
putative development of a screening of MBL producing strains by routine clinical microbiology laboratories. The detection of the MBL phenotype of resistance is of crucial importance for selecting the most appropriate therapy and applying infection control measures
medicine
-
putative development of a screening of MBL producing strains by routine clinical microbiology laboratories. The detection of the MBL phenotype of resistance is of crucial importance for selecting the most appropriate therapy and applying infection control measures
medicine
-
putative development of a screening of MBL producing strains by routine clinical microbiology laboratories. The detection of the MBL phenotype of resistance is of crucial importance for selecting the most appropriate therapy and applying infection control measures.
medicine
-
putative development of a screening of MBL producing strains by routine clinical microbiology laborities. The detection of the MBL phenotype of resistance is of crucial importance for selecting the most appropriate therapy and applying infection control measures
medicine
-
beta-lactamases, which catalyze the inactivation of beta-lactam antibiotics such as penicillins and cephalosporins are of great interest because of their high incidence in pathogenic bacteria
pharmacology
-
enzyme is a target for design of non-beta-lactam, broad-spectrum peptidomimetic enzyme inhibitors
pharmacology
-
enzyme is a target for design of non-beta-lactam, broad-spectrum peptidomimetic enzyme inhibitors
pharmacology
-
enzyme is a target for design of non-beta-lactam, broad-spectrum peptidomimetic enzyme inhibitors
synthesis
-
production of (-)2-azabicyclo[2.2.1]hept-5-en-3-one, which can be converted into carbovir, carbovir is a potent and selective inhibitor of HIV-1
synthesis
-
production of 4-amino-cyclopent-2-enecarboxylic acid, which is used as building block in the synthesis of carbocyclic nucleosides of the natural configuration
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 3.5.2.6)
Transporter Classification Database (TCDB): 9.B.29.2.7
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
