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Information on EC 3.5.2.6 - beta-lactamase and Organism(s) Enterobacter cloacae and UniProt Accession Q59401
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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.
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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 taxonomic range for the selected organisms is: Enterobacter cloacae
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Beta lactamase OXA-10
-
-
-
-
beta-lactamase
-
-
-
-
beta-lactamase AME I
-
-
-
-
beta-lactamase II
-
-
-
-
BLAIMP
-
-
-
-
carbapenemase
-
-
-
-
Carbenicillinase
-
-
-
-
cefotaximase
-
-
-
-
ceftazidimase
-
-
-
-
cefurooximase
-
-
-
-
Cefuroximase
-
-
-
-
Cephalosporinase
-
-
-
-
class C beta-lactamase
Imipenem-cefoxitin hydrolyzing enzyme
-
-
-
-
imipenemase
-
-
-
-
metallo-beta-lactamase
neutrapen
-
-
-
-
Oxacillinase
-
-
-
-
P99 beta-lactamase
penicillinase
-
-
-
-
serine beta-lactamase
SHV-2A
-
-
-
-
metallo-beta-lactamase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylic acid amide hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
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
9073-60-3
-
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
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
-
-
-
?
(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,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
-
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
-
-
?
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
-
-
?
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
-
-
-
-
?
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
-
-
?
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
-
-
-
-
?
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-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
-
-
-
?
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
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
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
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
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
-
-
-
?
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
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
-
-
-
-
?
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-oxazole-4-carbonyl)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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
-
?
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
-
-
?
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
-
-
?
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
-
-
-
?
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
-
-
-
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
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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-[3-(2-chlorophenyl)-5-methyl-1,2-oxazol-4-yl]-2-oxoethyl}phosphonate
-
sodium biphenyl-4-ylmethyl [2-(biphenyl-4-yl)-2-oxoethyl]phosphonate
-
3-((benzyloxycarbonylaminooxy)carbonyloxy)benzoic acid
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
AAGHYY
-
synthetic peptide, derived from screenings using phage display and peptide arrays
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
biphenyl-4-ylmethyl phenoxycarbonyloxycarbamate
-
completely inactivated, 2 micro M concentration, o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
ethyl 3-(benzyloxycarbonyl)amino-2-oxo-1,1-difluoropropylphosphonate
-
-
HSAYSDTRRGDYG
-
synthetic peptide, derived from screenings using phage display and peptide arrays
N-(phenoxycarbonyloxy)benzenesulfonamide
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
RRGHYY
-
synthetic peptide, derived from screenings using phage display and peptide arrays, inhibition mechanism
thiono derivative of N-(phenylacetyl)thioglycylglycolic acid
-
weak reversible inhibition
-
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-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-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-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/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/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
-
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/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
[(phenoxycarbonyl)oxy][(phenylacetyl)oxy]amine
-
0.01 mM, irreversible inhibition
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 by vanadate-catechol complex. 0.1 mM vanadate, varied catechol
-
additional information
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
(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
0.0154
(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
0.366
(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
0.032
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
0.34
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
0.0085
cephalexin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
0.0000005
Cloxacillin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
0.023
nitrocefin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
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
0.004
ampicillin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
0.0005
benzylpenicillin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
additional information
additional information
-
combination of detailed post- and pre-steady state kinetics
-
additional information
additional information
-
enzyme-ligand interaction kinetics and energies
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
0.49
(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
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
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
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
0.004
carbenicillin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
0.004
Cloxacillin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
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
18
benzylpenicillin
at 30°C in 50mM sodium phosphate buffer (pH 7.0)
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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
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
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
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.08
sodium benzyl (2-hydroxy-2-phenylethyl)phosphonate
pH 7.5, 25°C
0.024
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
0.19
sodium benzyl [2-(biphenyl-4-yl)-2-oxoethyl]phosphonate
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
1
sodium benzyl {2-[3-(2-chlorophenyl)-5-methyl-1,2-oxazol-4-yl]-2-oxoethyl}phosphonate
above, pH 7.5, 25°C
0.074
sodium biphenyl-4-ylmethyl [2-(biphenyl-4-yl)-2-oxoethyl]phosphonate
pH 7.5, 25°C
0.1
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
0.95
ethyl 3-(benzyloxycarbonyl)amino-2-oxo-1,1-difluoropropylphosphonate
-
-
5.5
thiono derivative of N-(phenylacetyl)thioglycylglycolic acid
-
pH 7.5, 25°C
-
0.0109
vanadate/(3,4-dihydroxyphenyl)methanaminium complex
pH 7.0, 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
0.0042
vanadate/2-(3,4-dihydroxyphenyl)acetate complex
pH 7.0, 25°C
0.0019
vanadate/3,4,5,6-tetrafluorobenzene-1,2-diol complex
pH 7.0, 25°C
0.00043
vanadate/3-phenylcatechol complex
most effective, 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
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
additional information
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method with 20% poly(ethylene)glycol 6 K in 0.1 M Tris (pH 8.0)
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
pharmacology
-
enzyme is a target for design of non-beta-lactam, broad-spectrum peptidomimetic enzyme inhibitors
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ross, G.W.
beta-Lactamase (Enterobacter species)
Methods Enzymol.
43
678-687
1975
Enterobacter cloacae, Enterobacter sp., Enterobacter cloacae P99
Ross, G.W.; Boulton, M.G.
Purification of beta-lactamases on QAE-sephadex
Biochim. Biophys. Acta
309
430-439
1973
Klebsiella aerogenes, Enterobacter cloacae, Enterobacter cloacae P99, Klebsiella aerogenes 1082E
Citri, N.
Penicillinase and other beta-lactamases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
4
23-46
1971
Enterobacter cloacae, Bacillus cereus, Bacillus licheniformis, Escherichia coli, Staphylococcus aureus
-
Mariotte-Boyer, S.; Nicolas-Chanoine, M.H.; Labia, R.
A kinetic study of NMC-A beta-lactamase, an Ambler class A carbapenemase also hydrolysing cephamycins
FEMS Microbiol. Lett.
143
29-33
1996
Enterobacter cloacae, Enterobacter cloacae NOR-1
Bell, J.H.; Pratt, R.F.
Mechanism of inhibition of the beta-lactamase of Enterobacter cloacae P99 by 1:1 complexes of vanadate with hydroxamic acids
Biochemistry
41
4329-4338
2002
Enterobacter cloacae (P05364), Enterobacter cloacae P99 (P05364), Enterobacter cloacae P99
Kumar, S.; Adediran, S.A.; Nukaga, M.; Pratt, R.F.
Kinetics of turnover of cefotaxime by the Enterobacter cloacae P99 and GCl beta-lactamases: two free enzyme forms of the P99 beta-lactamase detected by a combination of pre- and post-steady state kinetics
Biochemistry
43
2664-2672
2004
Enterobacter cloacae, Enterobacter cloacae P99, Enterobacter cloacae GC1
Curley, K.; Pratt, R.F.
The oxyanion hole in serine beta-lactamase catalysis: interactions of thiono substrates with the active site
Bioorg. Chem.
28
338-356
2000
Enterobacter cloacae, Enterobacter cloacae P99
Huang, W.; Beharry, Z.; Zhang, Z.; Palzkill, T.
A broad-spectrum peptide inhibitor of beta-lactamase identified using phage display and peptide arrays
Protein Eng.
16
853-860
2003
Enterobacter cloacae, Bacillus anthracis, Escherichia coli
Gacar, G.G.; Midilli, K.; Kolayli, F.; Ergen, K.; Gundes, S.; Hosoglu, S.; Karadenizli, A.; Vahaboglu, H.
Genetic and enzymatic properties of metallo-beta-lactamase VIM-5 from a clinical isolate of Enterobacter cloacae
Antimicrob. Agents Chemother.
49
4400-4403
2005
Enterobacter cloacae (Q4ZE97), Enterobacter cloacae
Bonnefoy, A.; Dupuis-Hamelin, C.; Steier, V.; Delachaume, C.; Seys, C.; Stachyra, T.; Fairley, M.; Guitton, M.; Lampilas, M.
In vitro activity of AVE1330A, an innovative broad-spectrum non-beta-lactam beta-lactamase inhibitor
J. Antimicrob. Chemother.
54
410-417
2004
Enterobacter cloacae, Escherichia coli, Enterobacter cloacae 293HT6
Perumal, S.K.; Pratt, R.F.
Synthesis and evaluation of ketophosph(on)ates as beta-lactamase inhibitors
J. Org. Chem.
71
4778-4785
2006
Enterobacter cloacae, Escherichia coli, Enterobacter cloacae P99
Michaux, C.; Massant, J.; Kerff, F.; Frere, J.M.; Docquier, J.D.; Vandenberghe, I.; Samyn, B.; Pierrard, A.; Feller, G.; Charlier, P.; Van Beeumen, J.; Wouters, J.
Crystal structure of a cold-adapted class C beta-lactamase
FEBS J.
275
1687-1697
2008
Psychrobacter immobilis, Serratia marcescens, Enterobacter cloacae (P05364), Pseudomonas fluorescens (P85302), Pseudomonas fluorescens, Pseudomonas fluorescens TAE4 (P85302), Enterobacter cloacae 908R (P05364)
Wyrembak, P.N.; Babaoglu, K.; Pelto, R.B.; Shoichet, B.K.; Pratt, R.F.
O-aryloxycarbonyl hydroxamates: New beta-lactamase inhibitors that cross-link the active Site
J. Am. Chem. Soc.
129
9548-9549
2007
Enterobacter cloacae, Enterobacter cloacae P99
Picao, R.C.; Andrade, S.S.; Nicoletti, A.G.; Campana, E.H.; Moraes, G.C.; Mendes, R.E.; Gales, A.C.
Metallo-beta-Lactamase detection: comparative evaluation of double-disk synergy versus combined disk tests for IMP, GIM, SIM, SPM or VIM-producing isolates
J. Clin. Microbiol.
46
2028-2037
2008
Acinetobacter sp., Enterobacter cloacae, Klebsiella pneumoniae, Pseudomonas aeruginosa, Pseudomonas putida, Serratia marcescens
Pelto, R.B.; Pratt, R.F.
Kinetics and mechanism of inhibition of a serine beta -lactamase by O-aryloxycarbonyl hydroxamates
Biochemistry
47
12037-12046
2008
Enterobacter cloacae, Enterobacter cloacae P99
Adediran, S.A.; Pratt, R.F.
Inhibition of serine beta -lactamases by vanadate-catechol complexes
Biochemistry
47
9467-9474
2008
Escherichia coli, Enterobacter cloacae (P05364), Enterobacter cloacae P99 (P05364)
Perumal, S.K.; Adediran, S.A.; Pratt, R.F.
beta -Ketophosphonates as beta -lactamase inhibitors: Intramolecular cooperativity between the hydrophobic subsites of a class D beta -lactamase
Bioorg. Med. Chem.
16
6987-6994
2008
Escherichia coli, Escherichia coli (P13661), Escherichia coli (P62593), Enterobacter cloacae (Q59401), Enterobacter cloacae P99 (Q59401), Enterobacter cloacae P99
Fenollar-Ferrer, C.; Frau, J.; Donoso, J.; Munoz, F.
Evolution of class C beta -lactamases: factors influencing their hydrolysis and recognition mechanisms
Theor. Chem. Acc.
121
209-218
2008
Enterobacter cloacae, Enterobacter cloacae P99
-
Ganta, S.R.; Perumal, S.; Pagadala, S.R.; Samuelsen, O.; Spencer, J.; Pratt, R.F.; Buynak, J.D.
Approaches to the simultaneous inactivation of metallo- and serine-beta-lactamases
Bioorg. Med. Chem. Lett.
19
1618-1622
2009
Enterobacter cloacae, Escherichia coli
Pelto, R.B.; Pratt, R.F.
Serendipitous discovery of alpha-hydroxyalkyl esters as beta-lactamase substrates
Biochemistry
49
10496-10506
2010
Enterobacter cloacae (P05364)
Adediran, S.; Cabaret, D.; Lohier, J.; Wakselman, M.; Pratt, R.
Substituted aryl malonamates as new serine beta-lactamase substrates: structure-activity studies
Bioorg. Med. Chem.
18
282-291
2010
Enterobacter cloacae (P05364)
Porres-Osante, N.; Saenz, Y.; Somalo, S.; Torres, C.
Characterization of beta-lactamases in faecal Enterobacteriaceae recovered from healthy humans in Spain focusing on AmpC polymorphisms
Microb. Ecol.
70
132-140
2015
Citrobacter freundii (A3RLA9), Citrobacter freundii (H6UZZ2), Citrobacter freundii (H6UZZ8), Citrobacter freundii (I3QHT4), Citrobacter freundii (I3QHT7), Citrobacter freundii (X2EXH4), Citrobacter freundii, Citrobacter braakii (K0GES5), Citrobacter braakii (K0GET7), Citrobacter braakii (K0GG60), Citrobacter braakii, Enterobacter cloacae (K0GEV1), Enterobacter cloacae (K0GEV3), Enterobacter cloacae (K0GG70), Enterobacter cloacae (Q8KP20), Enterobacter cloacae (X2EXI0), Enterobacter cloacae (X2EXI1), Enterobacter cloacae (X2EXI6), Enterobacter cloacae
EXTERNAL LINKS (specific for EC-Number 3.5.2.6)
Transporter Classification Database (TCDB): 9.B.29.2.7
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