3.5.2.6: beta-lactamase
This is an abbreviated version!
For detailed information about beta-lactamase, go to the full flat file.
Word Map on EC 3.5.2.6
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3.5.2.6
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pneumonia
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klebsiella
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enterobacteriaceae
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esbls
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carbapenems
-
aeruginosa
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carbapenem-resistant
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ampicillin
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esbl-producing
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multidrug-resistant
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enterobacter
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cefotaxime
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ceftazidime
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aureus
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acinetobacter
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surveillance
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meropenem
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nosocomial
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clavulanic
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microbiological
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haemophilus
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aminoglycosides
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ciprofloxacin
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baumannii
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cloacae
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tetracycline
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pulsed-field
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outbreak
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disk
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gentamicin
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integrons
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plasmid-mediated
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colistin
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amikacin
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ceftriaxone
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fluoroquinolones
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microdilution
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quinolone
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citrobacter
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proteus
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multilocus
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carriage
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mirabilis
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gonorrhoeae
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staphylococci
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community-acquired
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third-generation
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methicillin
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penicillin-binding
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enterococci
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drug development
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synthesis
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diagnostics
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medicine
-
pharmacology
- 3.5.2.6
- pneumonia
- klebsiella
- enterobacteriaceae
-
esbls
- carbapenems
- aeruginosa
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carbapenem-resistant
- ampicillin
-
esbl-producing
-
multidrug-resistant
- enterobacter
- cefotaxime
- ceftazidime
- aureus
- acinetobacter
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surveillance
- meropenem
-
nosocomial
-
clavulanic
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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
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third-generation
- methicillin
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penicillin-binding
-
enterococci
- drug development
- synthesis
- diagnostics
- medicine
- pharmacology
Reaction
Synonyms
ACT-3, ALI-1, Ambler class A beta-lactamase, AmpC, AmpC beta-lactamase, AmpC beta-lactamases M19, AmpC beta-lactamases M29, AmpC beta-lactamases M37, AmpC M19, AmpC M29, AmpC M37, AmpC-A, AmpC-B2, AmpC-type beta-lactamase, apo Bacillus cereus 569/H/9 enzyme, apo-BcII, B1 metallo-beta-lactamase, B3 MBL, BcII, BCL-1, BEL-1, Beta lactamase OXA-10, beta-lactamase, beta-lactamase A-C, beta-lactamase ACT-1, beta-lactamase AME I, beta-lactamase Bla-A, beta-lactamase Bla-B, beta-lactamase CMY-1, beta-lactamase CMY-2, beta-lactamase I-III, beta-lactamase II, beta-lactamase MIR-1, beta-lactamase OXA-1, beta-lactamase OXA-10, beta-lactamase P99, beta-lactamase PSE-1, beta-lactamase YRC-1, beta-lactamase, class C, beta-lactamases CTX-M-25, beta-lactamases CTX-M-26, beta-lactamse A-D, BLA, Bla-A, Bla-B, Bla1, Bla2, BlaA, blaACT-12, blaACT-14, blaACT-15, blaACT-17, blaACT-18, blaACT-19, blaACT-22, BlaB, BlaC, blaCMY-126, blaCMY-2, blaCMY-65, blaCMY-66, blaCMY-67, blaCMY-68, blaCMY-70, blaCMY-71, blaCMY-74, blaCMY-83, blaCMY-93, blaCTX-M-14, blaCTX-M-15, blaCTX-M-27, blaCTX-M-55, BLAIMP, blaIMP-4, blaKPC-2, blaLUT-1, BlaMab, blaNDM-1, blaNDM-7, blaoxa-1, blaSHV-1, blaSHV-14, blaTEM-1, blaToho-11, blaVIM-2, BS3, CAR-1 enzyme, CARB-3, carbapenem-hydrolysing MBL, carbapenem-hydrolyzing ambler class D beta-lactamase, carbapenem-hydrolyzing class A beta-lactamase, carbapenemase, carbapenemase CphA, Carbenicillinase, CcrA, cefotaximase, ceftazidimase, cefurooximase, Cefuroximase, Cephalosporinase, cephamycinase, CIA-1, CKO, class A beta-lactamase, class A beta-lactamase CKO-1, class A beta-lactamase CKO-2, class A beta-lactamase CKO-3, class A beta-lactamase CKO-4, class A TEM-2 beta-lactamase, class A TEM-2 enzyme, class B beta-lactamase SFB-1, class B beta-lactamase SLB-1, class B carbapenemase, class B metallo-beta-lactamase, class B metallo-beta-lactamase L-1, class C beta-lactamase, class C cephalosporinase, class C P99 beta-lactamase, class D beta lactamase, class D beta-lactamase, class D OXA-1 beta-lactamase, class D oxacillinase, CMY-1, CMY-10, CMY-2-type beta-lactamase, CMY-37, CphA, CTX-M beta-lactamase, CTX-M-1, CTX-M-14, CTX-M-64, CTX-M-64 beta-lactamase, EC 3.5.2.8, ESBL, Est-Y29, EstSRT1, exo-small beta-lactamase, extended spectrum beta-lactamase, extended-spectrum beta-lactamase, extended-spectrum beta-lactamase TEM-60, extended-spectrum-beta-lactamase, FEZ-1 metallo-beta-lactamase, FOX-4, FUS-1, GC1 beta-lactamase, GES-1, GES-2, GES-5, GES-type beta-lactamase, GIM-1, Imipenem-cefoxitin hydrolyzing enzyme, imipenemase, ImiS, IMP-1, IMP-10, IMP-12, IMP-13, IMP-15, IMP-16, IMP-18, IMP-2, IMP-2 MBL, IMP-9-type metallo-beta-lactamase, IMP-like metallo-beta-lactamase, IMP-type beta-lactamase, IMP-type metallo-beta-lactamase, IND-5, KHM-1, KLUA-9, KPC beta-lactamase, KPC-2, KPC-2 beta-lactamase, KPC-3, L1, L1 beta-lactamase, L1 metallo-beta-lactamase, L2 beta-lactamase, LHK-5, LUT-1 beta-lactamase, M19, M29, M37, MacQ, MbetaL, mbetal L1, MBL, metagenome-derived family VIII carboxylesterase, metallo-beta -lactamase, metallo-beta-L-lactamase, metallo-beta-lactamase, metallo-beta-lactamase BceII, metallo-beta-lactamase BcII, metallo-beta-lactamase ImiS, metallo-beta-lactamase IMP-1, metallo-beta-lactamase L1, metallo-beta-lactamase type 2, metallo-beta-lactamase VIM-1, metallo-beta-lactamase VIM-2, metallo-beta-lactamase VIM-6, MFO, MIR-4 beta-lactamase, More, Mox-1, Mox-1 beta-lactamase, MSMEG_4455, NDM, NDM-1, NDM-10, NDM-12, NDM-2, NDM-3, NDM-4, NDM-5, NDM-6, NDM-7, NDM-8, NDM-9, neutrapen, New Delhi MbetaL-1, New Delhi MBL, New Delhi metallo-beta-lactamase, New Delhi metallo-beta-lactamase-1, OXA group I, OXA group II, OXA-1, oxa-1 beta-lactamase, OXA-10, OXA-10 beta-lactamase, OXA-10 enzyme, OXA-17, OXA-18, OXA-2, OXA-229, OXA-24, OXA-24 beta-lactamase, OXA-40, OXA-48 carbapenemase, Oxa-50, OXA-55, OXA-57, OXA-63, OXA-69, OXA-85, OXA-type metallo-beta-lactamase, OXA114, Oxacillinase, oxycillinase, P99, P99 beta-lactamase, PenA, PenB1 beta-lactamase, PenB2, PenB3, PenB4, penicillinase, penicillinase I, II, PenP, PER-1, PER-2, plasmidic class C beta-lactamase, POM-1, poxB, PSE-1, PSE-4, serine beta-lactamase, SFC-1, Sfh-I, SHV, SHV beta-lactamase, SHV-1, SHV-1 beta-lactamase, SHV-1 penicillinase, SHV-14 beta-lactamase, SHV-2A, SHV-4, SHV-5, SHV-55, SHV-type beta-lactamase, SHV-type extended spectrum beta-lactamase, SIM-1, SMB-1, SME-1, SPM-1, ST1585, subclass B1 metallo-?-lactamase, subclass B3 metallo-beta-lactamase, TEM, TEM extended-spectrum beta-lactamase, TEM-1, TEM-1 beta-lactamase, TEM-107, TEM-116, TEM-149, TEM-21, TEM-8, TEM-type beta-lactamase, TEM1, THIN-B metallo-beta-lactamase, TMB-1, Toho-1, TRU-1, Verona integron-encoded MBL, Verona integron-encoded MBL-2, VIM, VIM-1, VIM-1 metallo-beta-lactamase, VIM-11, VIM-12, VIM-13, VIM-2, VIM-2 metallo-beta-lactamase, VIM-3, VIM-4, VIM-5, VIM-6, VIM-6 enzyme, VIM-7, VIM-metallo beta-lactamase, VIM-type MBL, VIM-type metallo-beta-lactamase, zinc beta-lactamase, Zn-beta-lactamase
ECTree
3.5.2.6 beta-lactamaseAdvanced search results
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results (Inhibitors
Inhibitors on EC 3.5.2.6 - beta-lactamase
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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
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competitive
(2Z)-2-(((E)-2-carboxy-2-[(2-thienylacetyl)amino]vinyl)imino)-3-mercaptobut-3-enoic acid
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-
(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
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o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
3-hydroxy-5-(hydroxycarbamoyl)benzoic acid
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92% residual activity at 0.1 mM
3-hydroxy-5-[(4-hydroxyphenyl)carbonyl]benzoic acid
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67% residual activity at 0.1 mM
3-[(2R)-2-(dihydroxyboranyl)-2-[[(thiophen-2-ylmethyl)sulfonyl]amino]ethyl]benzoic acid
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3-[(2R)-2-[(benzylsulfonyl)amino]-2-(dihydroxyboranyl)ethyl]benzoic acid
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4-chloro-7-(4-methoxyphenyl)-5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidine
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-
4-chloro-7-(4-methylphenyl)-5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidine
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-
7-(4-methylphenyl)-8,9-diphenyl-7H-pyrrolo[3,2-e][1,2,4]triazolo[4,3-c]pyrimidine-3-thione
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-
AAGHYY
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synthetic peptide, derived from screenings using phage display and peptide arrays
amoxicillin
susceptible to amoxicillin in combination with clavulanic acid
benzyl (4-chlorophenoxy)carbonyloxycarbamate
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o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
benzyl (4-methoxyphenoxy)carbonyloxycarbamate
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o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
benzyl (4-nitrophenoxy)carbonyloxycarbamate
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o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
benzyl (naphthalen-2-yloxy)carbonyloxycarbamate
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o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
benzyl carbonylbis(oxy)dicarbamate
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o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
benzyl methoxycarbonyloxycarbamate
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o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
benzyl methyl(phenoxycarbonyloxy)carbamate
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o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits slightly, 20fold less effectiv than benzyl phenoxycarbonyloxycarbamate
benzyl phenoxycarbonothioyloxycarbamate
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o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits slightly
benzyl phenoxycarbonyloxycarbamate
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o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
benzyl phenylcarbamoyloxycarbamate
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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
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biphenyl-4-ylmethyl phenoxycarbonyloxycarbamate
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completely inactivated, 2 micro M concentration, o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
carbapenem antibiotics
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EDTA combined with carbapenems produces a significant PLIE on VIM-MBL-positive Pseudomonas aeruginosa strains
D-captopril
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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
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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
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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
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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
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64% residual activity at 0.1 mM
N,3-dihydroxy-5-[(4-hydroxyphenyl)carbonyl]benzamide
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15% residual activity at 0.1 mM
N,5-dihydroxy-N'-methylbenzene-1,3-dicarboxamide
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47% residual activity at 0.1 mM
N,5-dihydroxy-N'-phenylbenzene-1,3-dicarboxamide
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42% residual activity at 0.1 mM
N,N-diethyl-N',5-dihydroxybenzene-1,3-dicarboxamide
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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
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N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
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N-(phenoxycarbonyloxy)benzenesulfonamide
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o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
N-benzyl-N',5-dihydroxybenzene-1,3-dicarboxamide
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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
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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
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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
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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
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2-[[5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-yl]sulfanyl]-N-phenylacetamide
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2-[[5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-yl]sulfanyl]-N-phenylacetamide
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2-[[5-(2-hydroxyphenyl)-1,3,4-thiadiazol-2-yl]sulfanyl]-N-phenylacetamide
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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
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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
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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
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BLIP, competitive inhibitor of a number of class A beta-lactamases
-
beta-lactamase inhibitor protein
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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
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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
-
