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BRENDA support

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

Reaction

A beta-lactam
+
H2O
=
a substituted beta-amino acid

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 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.2 In cyclic amides
                3.5.2.6 beta-lactamase

Organism

Organism on EC 3.5.2.6 - beta-lactamase

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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain CIP69598, previously Alcaligenes xylosoxidans
UniProt
Manually annotated by BRENDA team
isolated from activated sludge in a penicillin G production wastewater treatment system
AB702957
GenBank
Manually annotated by BRENDA team
clinical strain of genomic species 3
SwissProt
Manually annotated by BRENDA team
produces only one beta-lactamase belonging to molecular class C
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
Bacillus sp. (in: Bacteria) No. 170
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Manually annotated by BRENDA team
pathogenic bacteria
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Manually annotated by BRENDA team
isolated from faecal samples of healthy humans of La Rioja region (Northern Spain), September to November 2010
UniProt
Manually annotated by BRENDA team
previously known as Levinea malonatica
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Manually annotated by BRENDA team
basonym Alcaligenes eutrophus
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Manually annotated by BRENDA team
stain NOR-1
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Manually annotated by BRENDA team
strain 254G9, strain 4952, strain 192c3, strain 2662, strain 3701, strain 3806 and strain 02C9
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain DH5alpha
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Manually annotated by BRENDA team
E384
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
class C enzyme AmpC
UniProt
Manually annotated by BRENDA team
-
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-
Manually annotated by BRENDA team
class A enzyme SHV-1
SwissProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
mox1, plasmid-encoded
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
R or S derivative, gene MAB_2875
UniProt
Manually annotated by BRENDA team
R or S derivative, gene MAB_2875
UniProt
Manually annotated by BRENDA team
i.e. Mycobacterium smegmatis
UniProt
Manually annotated by BRENDA team
i.e. Mycobacterium smegmatis
UniProt
Manually annotated by BRENDA team
i.e. Mycobacterium smegmatis
UniProt
Manually annotated by BRENDA team
no activity in Enterobacter agglomerans
no extended-spectrum beta-lactamase
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-
Manually annotated by BRENDA team
no activity in Enterobacter asburiae
no extended-spectrum beta-lactamase
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-
Manually annotated by BRENDA team
no activity in Enterobacter cloacae
no extended-spectrum beta-lactamase
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Manually annotated by BRENDA team
no activity in Enterobacter gergoviae
no extended-spectrum beta-lactamase
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-
Manually annotated by BRENDA team
no activity in Enterobacter sakazakii
no extended-spectrum beta-lactamase
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Manually annotated by BRENDA team
producing blaKPC-2
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-
Manually annotated by BRENDA team
subsp. atroseptica DSM 30184 (also recently named Pectobacterium atrosepticum)
UniProt
Manually annotated by BRENDA team
plasmid pBC
vector SK(+)-blaKPC-2
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-
Manually annotated by BRENDA team
plasmid pBG66
contains the wild-type blaTEM-1 gene, expressed in Escherichia coli
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Manually annotated by BRENDA team
plasmid pGEM-T-easy
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Manually annotated by BRENDA team
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
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
gene blaIMP-1; blaIMP-cluster-producingstrains
UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
isolated from faeces (cloacal swabs) of healthy ducks
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Manually annotated by BRENDA team
clinical isolate KB-1
SwissProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
strain antibioticus Tü1718, beta-lactamase AME 1
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Manually annotated by BRENDA team
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
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
precursor
UniProt
Manually annotated by BRENDA team