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Information on EC 3.5.2.6 - beta-lactamase and Organism(s) Staphylococcus aureus PC1

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EC Tree
     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
IUBMB 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.
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This record set is specific for:
Staphylococcus aureus PC1
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Word Map
The enzyme appears in selected 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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Beta lactamase OXA-10
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beta-lactamase
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beta-lactamase AME I
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beta-lactamase II
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beta-lactamse A-D
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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
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BLAIMP
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carbapenemase
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Carbenicillinase
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cefotaximase
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ceftazidimase
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cefurooximase
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Cefuroximase
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Cephalosporinase
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Imipenem-cefoxitin hydrolyzing enzyme
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imipenemase
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metallo-beta-lactamase
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neutrapen
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Oxacillinase
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penicillinase
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SHV-2A
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amide hydrolysis
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
9073-60-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
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-
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?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
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?
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
show the reaction diagram
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?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
show the reaction diagram
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?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
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?
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
show the reaction diagram
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?
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
show the reaction diagram
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Guo, F.; Huynh, J.; Dmitrienko, G.I.; Viswanatha, T.; Clarke, A.J.
The role of the non-conserved residue at position 104 of class A beta-lactamases in susceptibility to mechanism-based inhibitors
Biochim. Biophys. Acta
1431
132-147
1999
Bacillus cereus, Staphylococcus aureus, Bacillus cereus 569/H/9, Staphylococcus aureus PC1
Manually annotated by BRENDA team
Zygmunt, D.J.; Stratton, C.W.; Kernodle, D.S.
Characterization of four beta-lactamases produced by Straphylococcus aureus
Antimicrob. Agents Chemother.
36
440-445
1992
Staphylococcus aureus, Staphylococcus aureus PC1
Manually annotated by BRENDA team