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Information on EC 3.5.2.6 - beta-lactamase and Organism(s) Pseudomonas aeruginosa and UniProt Accession P16897
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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: Pseudomonas aeruginosa
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
GIM-1
Imipenem-cefoxitin hydrolyzing enzyme
-
-
-
-
imipenemase
-
-
-
-
IMP-1
IMP-13
IMP-18
MbetaL
MBL
metallo-beta-lactamase
neutrapen
-
-
-
-
OXA-10
Oxacillinase
penicillinase
PSE-1
SHV-2A
VIM-1
VIM-2
VIM-7
additional information
beta-lactamase
-
-
-
-
carbapenemase
-
-
-
-
Cephalosporinase
-
-
-
-
metallo-beta-lactamase
-
-
-
-
metallo-beta-lactamase
-
-
Oxacillinase
-
-
-
-
penicillinase
-
-
-
-
SHV-2A
-
-
-
-
additional information
-
no metallo-beta-lactamase, MBL, in Pseudomonas aeruginosa
additional information
VIM-2 belongs to the B1 subfamily ofMBLs
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a beta-lactam + H2O = a substituted beta-amino acid
Arg234 is involved in catalysis
a beta-lactam + H2O = a substituted beta-amino acid
catalytic mechanism of enzyme class D, unique in comparison with classes A and C, active site structure with elements S-X-X-K, S-X-N, and K-T/S-G
a beta-lactam + H2O = a substituted beta-amino acid
VIM-2 catalytic Cys221, located in the Cys site, shows a high tendency to be strongly oxidized becoming a cysteinesulfonic residue, active site structure, overview
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
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)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
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
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
azlocillin + H2O
(2R,4S)-2-[(R)-carboxy({(2R)-2-[(2-oxoimidazolidine-1-carbonyl)amino]-2-phenylacetyl}amino)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
biapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[(6,7-dihydro-5H-pyrazolo[1,2-a][1,2,4]triazol-4-ium-6-yl)sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylate
carbapenem + H2O
[(2R)-2,3-dihydro-1H-pyrrol-2-yl]acetic acid
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
cefamandole + H2O
(2R)-2-[(R)-carboxy{[(2R)-2-hydroxy-2-phenylacetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
cefoperazone + H2O
(2R)-2-[(R)-carboxy{[(2S)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-(4-hydroxyphenyl)acetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cefotiam + H2O
(2R)-2-[(R)-[2-(2-amino-1,3-thiazol-4-yl)acetamido](carboxy)methyl]-5-[({1-[2-(dimethylamino)ethyl]-1H-tetrazol-5-yl}sulfanyl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cefpirome + H2O
(2S)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino}(carboxy)methyl]-5-[(6,7-dihydro-5H-cyclopenta[b]pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cefsulodin + H2O
(2R)-5-[(4-carbamoylpyridin-1-ium-1-yl)methyl]-2-[(R)-carboxy{[(2R)-2-phenyl-2-sulfoacetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefsulodine + H2O
(2R)-5-[(4-carbamoylpyridin-1-ium-1-yl)methyl]-2-[(R)-carboxy{[(2R)-2-phenyl-2-sulfoacetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino](carboxy)methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
ceftriaxone + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[[(6-hydroxy-2-methyl-5-oxo-2,5-dihydro-1,2,4-triazin-3-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
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
-
poor substrate
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
cephalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
chromacef + H2O
(2S)-2-[(S)-carboxy(2-phenylacetamido)methyl]-5-[(E)-2-(4-nitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
doripenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4-methyl-3-([(3S,5S)-5-[(sulfamoylamino)methyl]pyrrolidin-3-yl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
ertapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl]sulfanyl)-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
ertapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl}sulfanyl)-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([2-[(iminomethyl)amino]ethyl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
methicillin + H2O
(2R,4S)-2-[(R)-carboxy(2,6-dimethoxybenzamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
poor substrate
-
-
?
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
nitrocefin + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
nitrocefin + H2O
(2R)-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
oxacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(5-methyl-3-phenyl-1,2-oxazol-4-yl)carbonyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
penicillin N + H2O
N6-{(R)-carboxy[(2R,4S)-4-carboxy-5,5-dimethyl-1,3-thiazolidin-2-yl]methyl}-6-oxo-D-lysine
-
-
-
-
?
phenoxyethylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(3-phenoxypropanamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
phenoxymethylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenoxyacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
phenoxypropylpenicillin + H2O
(2R,4S)-2-[carboxy(4-phenoxybutanamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
biapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[(6,7-dihydro-5H-pyrazolo[1,2-a][1,2,4]triazol-4-ium-6-yl)sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylate
-
-
-
-
?
biapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[(6,7-dihydro-5H-pyrazolo[1,2-a][1,2,4]triazol-4-ium-6-yl)sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylate
-
-
-
?
biapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[(6,7-dihydro-5H-pyrazolo[1,2-a][1,2,4]triazol-4-ium-6-yl)sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylate
-
activity in resistant strains
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino](carboxy)methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino](carboxy)methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
cephalosporin antibiotic
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
poor substrate
-
-
?
cephalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
poor substrate
-
-
?
ertapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl]sulfanyl)-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
ertapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl]sulfanyl)-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
ertapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl]sulfanyl)-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
activity in resistant strains
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
the enzyme shows carbapenemase activity, e.g. against the carbapenem antibiotics meropenem and imipenem used in treatment of Pseudomonas aeruginosa infection, and contributes to resistance to anti-pseudomonal agents, overview
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
beta-lactam antibiotic
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
high activity of IMP-10
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
activity in resistant strains
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
the enzyme shows carbapenemase activity, e.g. against the carbapenem antibiotics meropenem and imipenem used in treatment of Pseudomonas aeruginosa infection, and contributes to resistance to anti-pseudomonal agents, overview
-
-
?
moxalactam + H2O
(2R)-2-{(R)-carboxy[2-carboxy(4-hydroxyphenyl)acetamido]methoxymethyl}-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-oxazine-4-carboxylic acid
-
-
-
?
moxalactam + H2O
(2R)-2-{(R)-carboxy[2-carboxy(4-hydroxyphenyl)acetamido]methoxymethyl}-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-oxazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
additional information
?
-
-
a VIM-2 enzyme inserted in integron In58, in an isolate from a female cystic fibrosis patient, is resistant to all antimicrobial agents tested except colistin, overview
-
-
?
additional information
?
-
-
antibiotic resistance rates and mechanisms of beta-lactam and aminoglycoside resistance, e.g. against ticarcillin, among human isolates of Pseudomonas aeruginosa isolated in the extra-hospital setting, MIC values of diverse beta-lactam antibiotics, resistance mechanisms, overview
-
-
?
additional information
?
-
-
carbapenem resistance screening of diverse clinical strains by a 2-mercaptopropionic acid inhibition test method, determination of MIC values, overview
-
-
?
additional information
?
-
-
determination of MIC values of SHV-1 for several antibiotics, overview
-
-
?
additional information
?
-
-
genetic variants of beta-lactamases cause resistance to antibiotics cefepime and/or ceftazidime, overview
-
-
?
additional information
?
-
-
occurrence and mechanisms of amikacin resistance and its association with beta-lactamases in Pseudomonas aeruginosa, a Korean nationwide study, gene blaOXA-10 is involved in amikain resistance, overview
-
-
?
additional information
?
-
-
production of beta-lactamases is the main mechanism of resistance to beta-lactams in Gram-negative bacteria, the phenomenon of continuing suppression of bacterial growth after removal of beta-lactamase inhibitors is termed post-beta-lactamase inhibitor effect, PLIE. EDTA combined with carbapenems produces a significant PLIE on VIM-MBL-positive Pseudomonas aeruginosa strains
-
-
?
additional information
?
-
-
screening for beta-lactamase genes in clincal isolates using Etest MBL screening test, The blaVIM-13-producing isolate shows resistance to all beta-lactams, except aztreonam, gentamicin, tobramycin, and ciprofloxacin, VIM-13 confers slightly higher levels of resistance to piperacillin and lower levels of resistance to ceftazidime and cefepime than VIM-1, MIC values, overview
-
-
?
additional information
?
-
screening for beta-lactamase genes in clincal isolates using Etest MBL screening test, The blaVIM-13-producing isolate shows resistance to all beta-lactams, except aztreonam, gentamicin, tobramycin, and ciprofloxacin, VIM-13 confers slightly higher levels of resistance to piperacillin and lower levels of resistance to ceftazidime and cefepime than VIM-1, MIC values, overview
-
-
?
additional information
?
-
screening for beta-lactamase genes in clincal isolates using Etest MBL screening test, The blaVIM-13-producing isolate shows resistance to all beta-lactams, except aztreonam, gentamicin, tobramycin, and ciprofloxacin, VIM-13 confers slightly higher levels of resistance to piperacillin and lower levels of resistance to ceftazidime and cefepime than VIM-1, MIC values, overview
-
-
?
additional information
?
-
-
screening for strains expressing IMP-15 beta-lactamases in clinical human isolates from a Mexican tertiary-care hospital, overview
-
-
?
additional information
?
-
screening for strains expressing IMP-15 beta-lactamases in clinical human isolates from a Mexican tertiary-care hospital, overview
-
-
?
additional information
?
-
screening for strains expressing IMP-15 beta-lactamases in clinical human isolates from a Mexican tertiary-care hospital, overview
-
-
?
additional information
?
-
-
screening for strains expressing VIM-1, and other beta-lactamases in clinical human isolates from a Mexican tertiary-care hospital, overview
-
-
?
additional information
?
-
screening for strains expressing VIM-1, and other beta-lactamases in clinical human isolates from a Mexican tertiary-care hospital, overview
-
-
?
additional information
?
-
screening for strains expressing VIM-1, and other beta-lactamases in clinical human isolates from a Mexican tertiary-care hospital, overview
-
-
?
additional information
?
-
susceptibility and enzymatic activity of metallo-beta-lactamases in Pseudomonas aeruginosa-producing metallo-beta-lactamases, overview
-
-
?
additional information
?
-
-
susceptibility and enzymatic activity of metallo-beta-lactamases in Pseudomonas aeruginosa-producing metallo-beta-lactamases, overview
-
-
?
additional information
?
-
the IMP-9 variant of metallo-beta-lactamases show a broad spectrum antibiotic resistance resulting in an out break in 2005-2007 in China, multidrug-resistant profile of IMP-9 MBL variants, overview
-
-
?
additional information
?
-
-
the IMP-9 variant of metallo-beta-lactamases show a broad spectrum antibiotic resistance resulting in an out break in 2005-2007 in China, multidrug-resistant profile of IMP-9 MBL variants, overview
-
-
?
additional information
?
-
the Pseudomonas aeruginosa strain that contains the mobile metallo-beta-lactamase gene, designated blaVIM-7, located on a plasmid (p07-406), is resistant to all tested antimicrobials except polymyxin B causing an outbreak of infections in Houston, USA, overview
-
-
?
additional information
?
-
-
the Pseudomonas aeruginosa strain that contains the mobile metallo-beta-lactamase gene, designated blaVIM-7, located on a plasmid (p07-406), is resistant to all tested antimicrobials except polymyxin B causing an outbreak of infections in Houston, USA, overview
-
-
?
additional information
?
-
-
screening for MBL and ESBL variants using different test methods, overview
-
-
?
additional information
?
-
VIM-2 has a broad substrate hydrolysis range, which includes penicillins, cephalosporins, cephamycins, oxacephamycins and carbapenems but not monobactams. Amongst the carbapenems, VIM-2 better hydrolyses meropenem than imipenem
-
-
?
additional information
?
-
-
VIM-2 has a broad substrate hydrolysis range, which includes penicillins, cephalosporins, cephamycins, oxacephamycins and carbapenems but not monobactams. Amongst the carbapenems, VIM-2 better hydrolyses meropenem than imipenem
-
-
?
additional information
?
-
a single amino acid difference at position 170 of the GES-1, GES-2, and GES-5 enzymes is responsible for the expansion of their substrate profile to include carbapenem antibiotics. The catalytic efficiency of the enzymes with carbapenems meropenem, ertapenem, and doripenem progressively increases 100fold from GES-1 to -5, mainly due to an increase in the rate of acylation. While acylation is rate limiting for GES-1 and GES-2 for all three carbapenems, acylation and deacylation are indistinguishable for GES-5. Only the core structure of the antibiotic interacts with the active site of the GES-2 beta-lactamase. The identical core structures of ertapenem, doripenem, and meropenem are likely responsible for the observed similarities in the kinetics with these carbapenems. The lack of a methyl group in the core structure of imipenem may provide a structural rationale for the increase in turnover of this carbapenem by the GES beta-lactamases
-
-
?
additional information
?
-
a single amino acid difference at position 170 of the GES-1, GES-2, and GES-5 enzymes is responsible for the expansion of their substrate profile to include carbapenem antibiotics. The catalytic efficiency of the enzymes with carbapenems meropenem, ertapenem, and doripenem progressively increases 100fold from GES-1 to -5, mainly due to an increase in the rate of acylation. While acylation is rate limiting for GES-1 and GES-2 for all three carbapenems, acylation and deacylation are indistinguishable for GES-5. Only the core structure of the antibiotic interacts with the active site of the GES-2 beta-lactamase. The identical core structures of ertapenem, doripenem, and meropenem are likely responsible for the observed similarities in the kinetics with these carbapenems. The lack of a methyl group in the core structure of imipenem may provide a structural rationale for the increase in turnover of this carbapenem by the GES beta-lactamases
-
-
?
additional information
?
-
a single amino acid difference at position 170 of the GES-1, GES-2, and GES-5 enzymes is responsible for the expansion of their substrate profile to include carbapenem antibiotics. The catalytic efficiency of the enzymes with carbapenems meropenem, ertapenem, and doripenem progressively increases 100fold from GES-1 to -5, mainly due to an increase in the rate of acylation. While acylation is rate limiting for GES-1 and GES-2 for all three carbapenems, acylation and deacylation are indistinguishable for GES-5. Only the core structure of the antibiotic interacts with the active site of the GES-2 beta-lactamase. The identical core structures of ertapenem, doripenem, and meropenem are likely responsible for the observed similarities in the kinetics with these carbapenems. The lack of a methyl group in the core structure of imipenem may provide a structural rationale for the increase in turnover of this carbapenem by the GES beta-lactamases
-
-
?
additional information
?
-
a single amino acid difference at position 170 of the GES-1, GES-2, and GES-5 enzymes is responsible for the expansion of their substrate profile to include carbapenem antibiotics. The catalytic efficiency of the enzymes with carbapenems meropenem, ertapenem, and doripenem progressively increases 100fold from GES-1 to -5, mainly due to an increase in the rate of acylation. While acylation is rate limiting for GES-1 and GES-2 for all three carbapenems, acylation and deacylation are indistinguishable for GES-5. The identical core structures of ertapenem, doripenem, and meropenem are likely responsible for the observed similarities in the kinetics with these carbapenems. The lack of a methyl group in the core structure of imipenem may provide a structural rationale for the increase in turnover of this carbapenem by the GES beta-lactamases
-
-
?
additional information
?
-
a single amino acid difference at position 170 of the GES-1, GES-2, and GES-5 enzymes is responsible for the expansion of their substrate profile to include carbapenem antibiotics. The catalytic efficiency of the enzymes with carbapenems meropenem, ertapenem, and doripenem progressively increases 100fold from GES-1 to -5, mainly due to an increase in the rate of acylation. While acylation is rate limiting for GES-1 and GES-2 for all three carbapenems, acylation and deacylation are indistinguishable for GES-5. The identical core structures of ertapenem, doripenem, and meropenem are likely responsible for the observed similarities in the kinetics with these carbapenems. The lack of a methyl group in the core structure of imipenem may provide a structural rationale for the increase in turnover of this carbapenem by the GES beta-lactamases
-
-
?
additional information
?
-
a single amino acid difference at position 170 of the GES-1, GES-2, and GES-5 enzymes is responsible for the expansion of their substrate profile to include carbapenem antibiotics. The catalytic efficiency of the enzymes with carbapenems meropenem, ertapenem, and doripenem progressively increases 100fold from GES-1 to -5, mainly due to an increase in the rate of acylation. While acylation is rate limiting for GES-1 and GES-2 for all three carbapenems, acylation and deacylation are indistinguishable for GES-5. The identical core structures of ertapenem, doripenem, and meropenem are likely responsible for the observed similarities in the kinetics with these carbapenems. The lack of a methyl group in the core structure of imipenem may provide a structural rationale for the increase in turnover of this carbapenem by the GES beta-lactamases
-
-
?
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
biapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[(6,7-dihydro-5H-pyrazolo[1,2-a][1,2,4]triazol-4-ium-6-yl)sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylate
-
activity in resistant strains
-
-
?
carbapenem + H2O
[(2R)-2,3-dihydro-1H-pyrrol-2-yl]acetic 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
-
-
-
-
?
cefoperazone + H2O
(2R)-2-[(R)-carboxy{[(2S)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-(4-hydroxyphenyl)acetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
doripenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4-methyl-3-([(3S,5S)-5-[(sulfamoylamino)methyl]pyrrolidin-3-yl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
ertapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl]sulfanyl)-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
activity in resistant strains
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
the enzyme shows carbapenemase activity, e.g. against the carbapenem antibiotics meropenem and imipenem used in treatment of Pseudomonas aeruginosa infection, and contributes to resistance to anti-pseudomonal agents, overview
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
activity in resistant strains
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
the enzyme shows carbapenemase activity, e.g. against the carbapenem antibiotics meropenem and imipenem used in treatment of Pseudomonas aeruginosa infection, and contributes to resistance to anti-pseudomonal agents, overview
-
-
?
additional information
?
-
-
a VIM-2 enzyme inserted in integron In58, in an isolate from a female cystic fibrosis patient, is resistant to all antimicrobial agents tested except colistin, overview
-
-
?
additional information
?
-
-
antibiotic resistance rates and mechanisms of beta-lactam and aminoglycoside resistance, e.g. against ticarcillin, among human isolates of Pseudomonas aeruginosa isolated in the extra-hospital setting, MIC values of diverse beta-lactam antibiotics, resistance mechanisms, overview
-
-
?
additional information
?
-
-
carbapenem resistance screening of diverse clinical strains by a 2-mercaptopropionic acid inhibition test method, determination of MIC values, overview
-
-
?
additional information
?
-
-
determination of MIC values of SHV-1 for several antibiotics, overview
-
-
?
additional information
?
-
-
genetic variants of beta-lactamases cause resistance to antibiotics cefepime and/or ceftazidime, overview
-
-
?
additional information
?
-
-
occurrence and mechanisms of amikacin resistance and its association with beta-lactamases in Pseudomonas aeruginosa, a Korean nationwide study, gene blaOXA-10 is involved in amikain resistance, overview
-
-
?
additional information
?
-
-
production of beta-lactamases is the main mechanism of resistance to beta-lactams in Gram-negative bacteria, the phenomenon of continuing suppression of bacterial growth after removal of beta-lactamase inhibitors is termed post-beta-lactamase inhibitor effect, PLIE. EDTA combined with carbapenems produces a significant PLIE on VIM-MBL-positive Pseudomonas aeruginosa strains
-
-
?
additional information
?
-
-
screening for beta-lactamase genes in clincal isolates using Etest MBL screening test, The blaVIM-13-producing isolate shows resistance to all beta-lactams, except aztreonam, gentamicin, tobramycin, and ciprofloxacin, VIM-13 confers slightly higher levels of resistance to piperacillin and lower levels of resistance to ceftazidime and cefepime than VIM-1, MIC values, overview
-
-
?
additional information
?
-
screening for beta-lactamase genes in clincal isolates using Etest MBL screening test, The blaVIM-13-producing isolate shows resistance to all beta-lactams, except aztreonam, gentamicin, tobramycin, and ciprofloxacin, VIM-13 confers slightly higher levels of resistance to piperacillin and lower levels of resistance to ceftazidime and cefepime than VIM-1, MIC values, overview
-
-
?
additional information
?
-
screening for beta-lactamase genes in clincal isolates using Etest MBL screening test, The blaVIM-13-producing isolate shows resistance to all beta-lactams, except aztreonam, gentamicin, tobramycin, and ciprofloxacin, VIM-13 confers slightly higher levels of resistance to piperacillin and lower levels of resistance to ceftazidime and cefepime than VIM-1, MIC values, overview
-
-
?
additional information
?
-
-
screening for strains expressing IMP-15 beta-lactamases in clinical human isolates from a Mexican tertiary-care hospital, overview
-
-
?
additional information
?
-
screening for strains expressing IMP-15 beta-lactamases in clinical human isolates from a Mexican tertiary-care hospital, overview
-
-
?
additional information
?
-
screening for strains expressing IMP-15 beta-lactamases in clinical human isolates from a Mexican tertiary-care hospital, overview
-
-
?
additional information
?
-
-
screening for strains expressing VIM-1, and other beta-lactamases in clinical human isolates from a Mexican tertiary-care hospital, overview
-
-
?
additional information
?
-
screening for strains expressing VIM-1, and other beta-lactamases in clinical human isolates from a Mexican tertiary-care hospital, overview
-
-
?
additional information
?
-
screening for strains expressing VIM-1, and other beta-lactamases in clinical human isolates from a Mexican tertiary-care hospital, overview
-
-
?
additional information
?
-
susceptibility and enzymatic activity of metallo-beta-lactamases in Pseudomonas aeruginosa-producing metallo-beta-lactamases, overview
-
-
?
additional information
?
-
-
susceptibility and enzymatic activity of metallo-beta-lactamases in Pseudomonas aeruginosa-producing metallo-beta-lactamases, overview
-
-
?
additional information
?
-
the IMP-9 variant of metallo-beta-lactamases show a broad spectrum antibiotic resistance resulting in an out break in 2005-2007 in China, multidrug-resistant profile of IMP-9 MBL variants, overview
-
-
?
additional information
?
-
-
the IMP-9 variant of metallo-beta-lactamases show a broad spectrum antibiotic resistance resulting in an out break in 2005-2007 in China, multidrug-resistant profile of IMP-9 MBL variants, overview
-
-
?
additional information
?
-
the Pseudomonas aeruginosa strain that contains the mobile metallo-beta-lactamase gene, designated blaVIM-7, located on a plasmid (p07-406), is resistant to all tested antimicrobials except polymyxin B causing an outbreak of infections in Houston, USA, overview
-
-
?
additional information
?
-
-
the Pseudomonas aeruginosa strain that contains the mobile metallo-beta-lactamase gene, designated blaVIM-7, located on a plasmid (p07-406), is resistant to all tested antimicrobials except polymyxin B causing an outbreak of infections in Houston, USA, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Zn2+
additional information
Co2+
preparation of a Co(II)-substituted VIM-2 analogue, crystal structure analysis, overview
Zn2+
VIM metallo-beta-lactamases, VIM-1 and VIM-13 inactivation by Zn2+ removal
Zn2+
enzyme has a a fourcoordinate Zn2 site and both tetrahedral and pentacoordinated Zn1 sites
Zn2+
Zn2+ ions have a pronounced stabilizing effect and are necessary for preserving the structure
additional information
analysis of the metal content of enzyme VIM-2, metal binding kinetics, overview
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
mercaptoethanol shows no growth inhibition activity on Pseudomonas aeruginosa ATCC 27583 at all tested concentrations between 7.0 and 55 mM
4,7-dichloro benzothien-2-yl sulfonylaminomethyl boronic acid
-
carbapenem antibiotics
-
EDTA combined with carbapenems produces a significant PLIE on VIM-MBL-positive Pseudomonas aeruginosa strains
fosfomycin
-
determination of MIC values for the different isolates: range of 0.004 to over 0.512 mg/ml, MIC50 is 0.032 mg/ml and MIC90 is 0.128 mg/ml
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-[2-(7-chloro-quinolin-4-ylamino)-ethyl]-3-mercapto-propionamide
-
IC50: 0.0063 mM
N-[3-(7-chloro-quinolin-4-ylamino)-propyl]-3-mercapto-propionamide
-
IC50: 0.0065 mM
N-[4-(7-chloro-quinolin-4-ylamino)-butyl]-3-mercapto-propionamide
-
IC50: 0.0024 mM
N-[5-(7-chloro-quinolin-4-ylamino)-pentyl]-3-mercapto-propionamide
-
IC50: 0.0076 mM
N-[6-(7-cloro-quinolin-4-ylamino)-hexyl]-3-mercapto-propionamide
-
IC50: 0.0049 mM
Phenanthroline
-
phenanthroline shows no growth inhibition activity on Pseudomonas aeruginosa ATCC 27583 at all tested concentrations between 1.0 and 8.0 mM
EDTA
-
EDTA combined with carbapenems produces a significant PLIE on VIM-MBL-positive Pseudomonas aeruginosa strains
EDTA
EDTA inhibits the activity of VIM-13 approximately 25 times less than it inhibits the activity of VIM-1
EDTA
-
EDTA, PHEN, and MET present weak bactericidal activity against Pseudomonas aeruginosa with substrate ceftazidime
Mercaptoacetic acid
-
mercaptoacetic acid demonstrates hydrolytic activity against imipenem but not against ceftazidime
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
-
carbapenem resistance screening of diverse clinical strains by a 2-mercaptopropionic acid inhibition test method, determination of 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
metallo-beta-lactamases are not inhibited by clinical beta-lactamase inhibitors
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
2,2-dimethyl-6beta-({[5-methyl-3-(2-chlorophenyl)isoxazol-4-yl]carbonyl}amino)penam-3alpha-carboxylic acid
-
-
additional information
additional information
pre-steady-state and steady-state kinetics, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.019
clavulanic acid
-
pH and temperature not specified in the publication, OXA-10 beta-lactamase
0.104
clavulanic acid
-
pH and temperature not specified in the publication, OXA-10 beta-lactamase
0.004
JDB/ASR-II-292
-
pH and temperature not specified in the publication, OXA-10 beta-lactamase
0.017
JDB/ASR-II-292
-
pH and temperature not specified in the publication, OXA-10 beta-lactamase
0.0014
JDB/LN-1-255
-
pH and temperature not specified in the publication, OXA-10 beta-lactamase
0.008
JDB/LN-1-255
-
pH and temperature not specified in the publication, OXA-10 beta-lactamase
0.03
tazobactam
-
pH and temperature not specified in the publication, OXA-10 beta-lactamase
0.17
tazobactam
-
pH and temperature not specified in the publication, OXA-10 beta-lactamase
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00175
3'-hydroxybiphenyl-2,3-dicarboxylic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.013
3-(3-hydroxypropyl)benzene-1,2-dicarboxylic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.16
3-methylbenzene-1,2-dicarboxylic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.00155
4'-hydroxybiphenyl-2,3-dicarboxylic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0011
4,7-dichloro benzothien-2-yl sulfonylaminomethyl boronic acid
Pseudomonas aeruginosa
pH not specified in the publication, temperature not specified in the publication
0.016
4-butyl-3-methylbenzene-1,2-dicarboxylic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.243
4-butylbenzene-1,2-dicarboxylic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.207
biphenyl-2,2',3-tricarboxylic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0179
biphenyl-2,3,3'-tricarboxylic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.00225
biphenyl-2,3,4'-tricarboxylic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.000968
biphenyl-2,3-dicarboxylic acid
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0063
N-[2-(7-chloro-quinolin-4-ylamino)-ethyl]-3-mercapto-propionamide
Pseudomonas aeruginosa
-
IC50: 0.0063 mM
0.0065
N-[3-(7-chloro-quinolin-4-ylamino)-propyl]-3-mercapto-propionamide
Pseudomonas aeruginosa
-
IC50: 0.0065 mM
0.0024
N-[4-(7-chloro-quinolin-4-ylamino)-butyl]-3-mercapto-propionamide
Pseudomonas aeruginosa
-
IC50: 0.0024 mM
0.0076
N-[5-(7-chloro-quinolin-4-ylamino)-pentyl]-3-mercapto-propionamide
Pseudomonas aeruginosa
-
IC50: 0.0076 mM
0.0049
N-[6-(7-cloro-quinolin-4-ylamino)-hexyl]-3-mercapto-propionamide
Pseudomonas aeruginosa
-
IC50: 0.0049 mM
0.00244
trisodium 2'-oxidobiphenyl-2,3-dicarboxylate
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
class A enzyme PSE-4, the active site structure involves Ser70, Lys73, Ser130, Glu166, Asn170, and Arg234 as catalytic residues
Uniprot
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
screening and identification of MBLs from human clinical isolates, resistance phenotypes, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
GES beta-lactamases are important contributors to carbapenem resistance in clinical bacterial pathogens
additional information
additional information
in GES-2 an extensive hydrogen-bonding network between the acyl-enzyme complex and the active site water attenuates activation of this water molecule, which results in poor deacylation by this enzyme
additional information
in GES-2 an extensive hydrogen-bonding network between the acyl-enzyme complex and the active site water attenuates activation of this water molecule, which results in poor deacylation by this enzyme
additional information
in GES-2 an extensive hydrogen-bonding network between the acyl-enzyme complex and the active site water attenuates activation of this water molecule, which results in poor deacylation by this enzyme
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
53000
in presence of Cd2+, Cu2+ or Zn2+, gel filtration and analytical ultracentrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
enzyme consists of an alpha/beta domain and a predominantly alpha-helical domain
additional information
-
enzyme consists of an alpha/beta domain and a predominantly alpha-helical domain
additional information
cation mediated formation of a homodimer, but NaCl leads to dissociation of the dimer, overview
additional information
-
cation mediated formation of a homodimer, but NaCl leads to dissociation of the dimer, overview
additional information
VIM-2 secondary structure, structure comparison to other VIMs, overview
additional information
-
VIM-2 secondary structure, structure comparison to other VIMs, overview
additional information
folding of alphabeta/betaalpha sandwich, consisting of a core of beta-sheet surrounded by alpha-helices
additional information
-
folding of alphabeta/betaalpha sandwich, consisting of a core of beta-sheet surrounded by alpha-helices
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
0.003 ml 10 mg/ml purified recombinant wild-type enzyme or mutant R234K, mixed with 0.001 ml of well solution containing 2 M ammonium sulfate, 50 mM MOPS pH 6.4, and 0.1 M acetate pH 4.5, respectively, 100 mM MgCl2, 1-2 weeks at room temperature, X-ray diffraction structure determination and analysis at 1.75 A resolution
as the native enzyme, with Cys221 oxidized, and with a sulfur atom bridging the two active-site zinc ions, to 1.9, 1.8 and 2.5 A resolution, respectively. Comparison with VIM-2 and VIM-4 structures suggests an explanation for the reduced catalytic efficiency of VIM-7 against cephalosporins with a positively charged cyclic substituent at the C3 position. Kinetic variations are attributed to substitutions in residues 60–66, that form a loop adjacent to the active site previously implicated in substrate binding, and to the disruption of two hydrogen-bonding clusters through substitutions at positions 218 and 224
in complex with rac-2-omega-phenylpropyl-3-mercaptopropionic acid, in 30% PEG MME5000, 0.1 M MES-NaOH, and 0.2 M ammonium sulfate (pH 6.5)
-
purified recombinant enzyme, sitting drop vapor diffusion method, mixxing of 0001 ml of 10 mg/mL VIM-2 protein with 0.001 ml of reservoir solution containing 0.2 M ammonium acetate, 0.1 mM zinc chloride, 0.1 M HEPES, pH 7.5, and 25% PEG 3350, X-ray diffraction tructure determination and analysis, molecular replacement
purified recombinant native and chloride-treated enzyme, from 1.8 M ammonium sulfate, 0.1 M MES, pH 6.5, 10 mM CoCl2, vapour diffusion method, X-ray diffraction structure determination and analysis at 2.0 A resolution, modeling
purified recombinant native and oxidized VIM-2, hanging drop vapour diffusion method, mixing 0.001 ml of 5.5 mg/ml of protein in 10 mM HEPES, pH 7.5, 0.2 M NaCl, and 1 mM DTT, with 0.001 ml of precipitant solution containing 30% PEG 8000, 0.2 M Na acetate, 0.1 M Na cacodylate/cacodylic acid, pH 6.5, and 0.01 mM ZnCl2, 20°C, 3-4 days, X-ray diffraction structure determination and analysis at 1.9-2.2 A resolution
substrate ertapenem-isozyme GES-2 crystal structure determination and analysis
X-ray data collection and structure refinement of the reduced and oxidised VIM-2
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R234K
site-directed replacement mutagenesis, about 4fold reduced catalytic efficiency compared to the wild-type enzyme
Y218F
substitution may be responsible for the reduced catalytic efficiency against certain cephalosporins, including ceftazidime and cefepime
additional information
additional information
-
a VIM-2 enzyme inserted in integron In58, in an isolate from a female cystic fibrosis patient, is resistant to all antimicrobial agents tested except colistin, this isolate presented a unique random amplified polymorphic DNA, RAPD, type, overview
additional information
-
identification of blaSHV gene mutants SHV-2a, SHV5 et SHV1, that do not seem to be ESBLs, overview
additional information
overproduction of a metallo-beta-lactamase by a strong promoter causes high-level imipenem resistance in a strain KG2505, PAO1 derivative without an AmpC beta-lactamase and a Mex-AB-OprM efflux pump, derived from a clinical human isolate of Pseudomonas aeruginosa, overview
additional information
-
overproduction of a metallo-beta-lactamase by a strong promoter causes high-level imipenem resistance in a strain KG2505, PAO1 derivative without an AmpC beta-lactamase and a Mex-AB-OprM efflux pump, derived from a clinical human isolate of Pseudomonas aeruginosa, overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
crude extract, HCl buffer, 0.05 M triethanolamine, 4 days, 50% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant R234K from Escherichia coli BL21(DE3)
recombinant cobalt-cobtaining enzyme from Escherichia coli strain BL21(DE3) by cobalt affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant R234K in Escherichia coli BL21(DE3)
beta-lactamase genes, DNA and amino acid sequence determination and analysis
-
carbapenemase activity of MBL results from acquisition of carbapenemase-encoding determinants via horizontal gene transfer, overview
cloned into a multicopy plasmid and expressed in Escherichia coli and Pseudomonas aeruginosa
DNA and amino acid sequence determination and analysis, PCR screening for MBL variants in cystic fibrosis patient isolates of Pseudomonas aeruginosa in Portugal, overview
-
expressed in Escherichia coli
expression in Escherichia coli
gene blaIMP-1, quantitative expression analysis in 124 different strains, among metallo-beta-lactamase-producing Gram-negative rods in Japan, 84.45% are blaIMP-1 or blaIMP-2
gene blaIMP-10, DNA and amino acid sequence determination and analysis, promoter analysis, overexpression of metallo-beta-lactamase IMP-10 by the strong promoter of gene blaIMP-10 in Pseudomonas aeruginosa strain KG2505, overview. Genetic structure of the class 1 integron carrying the blaIMP-10 cassette, overview
gene blaIMP-15, the blaIMP-15 gene cassette is inserted in a plasmid-borne integron with a unique array of gene cassettes and named In95, genotyping for beta-lactamase genes in human isolates from a hospital in Mexico, overview. Genetic structure in strain 4677, overview, transformations of plasmid preparations of strains 4677 and 4663 by electroporation into Escherichia coli strain DH10B and Pseudomonas aeruginosa strain PU21
gene blaVIM, genotyping for beta-lactamase genes in human isolates from a hospital in Mexico, overview. Genetic structure in strain 4677, overview, transformations of plasmid preparations of strains 4677 and 4663 by electroporation into Escherichia coli strain DH10B and Pseudomonas aeruginosa strain PU21
gene blaVIM-2, recombinant Co2+-enzyme expression in Escherichia coli strain BL21(DE3) in in minimal medium
gene blaVIM-7, located on a plasmid (p07-406), DNA and amino acid sequence determination and analysis
gene oxa40, DNA and amino acid sequence determination and analysis, the gene is encoded on a plasmid
-
genes blaOXA-10, blaVIM-2, blaPSE-I, blaOXA-4, blaOXA-17, blaOXA-30, DNA and amino acid sequence determination and analysis, genotyping in human isolates and correlation of amikain resistance, overview
-
genes blaPER-1 and blaVIM-2, DNA and amino acid sequence determination and analysis
-
genes blaVIM and blaIMP, DNA and amino acid sequence determination and analysis, overview
-
genes blaVIM1 and blaVIM-13, genetic structure and genotyping, VIM-13 is harbored in a class 1 integron, along with an A108T variant of the aminoglycoside-modifying enzyme encoding gene aacA4, which confers resistance to gentamicin and tobramycin
genotyping and identification of beta-lactamase by PCR amplification followed by sequencing of bla genes
-
genotyping and screening of clinical isolates from human patients, sequencing of gene bla-VIM in MBl variant VIM-2, random amplified polymorphic DNA, RAPD, types, overview
-
genotyping of IMP-9 MBL variants in Pseudomonas aeruginosa patient isolates with multi-drug resistance phenotype, overview
identification of SHV-type extended spectrum beta-lactamase genes in Pseudomonas aeruginosa by PCR-restriction fragment length polymorphism and insertion site restriction-PCR, genotyping, overview
-
macrorestriction profiling of chromosomal DNA from 30 isolates and identification of two different clonal lineages, named cluster A, serotype O11, and cluster B, serotype O12, that produce VIM-1 and VIM-2 MBLs, respectively. The VIM-2-producing isolates from Italy carried identical, or very similar, allelic forms of the oprD gene, harbour a common class 1 integron, belong to the same multilocus sequence type, and show macrorestriction profiles that are related to those of the MBL-negative French strains, overview
screening for genes blaIMP-1, blaVIM and blaVIM-2 in clinical human isolates from a university hospital in Sichuan, China, genotyping and antimicrobial susceptibility, overview
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Murata, T.; Minami, S.; Yasuda, K.; Iyobe, S.; Inoue, M.; Mitsuhashi, S.
Purification and properties of cephalosporinase from Pseudomonas aeruginosa
J. Antibiot.
9
1164-1170
1981
Pseudomonas aeruginosa, Pseudomonas aeruginosa Dalgleish, Pseudomonas aeruginosa GN10362
Matthew, M.
Properies of the beta-lactamase specified by the Pseudomonas plasmid R151
FEMS Microbiol. Lett.
4
241-244
1978
Pseudomonas aeruginosa, Pseudomonas aeruginosa Dalgleish, Pseudomonas aeruginosa PU21 R151
-
Matthew, M.; Sykes, R.B.
Properties of the beta-lactamase specified by the Pseudomonas plasmid RPL11
J. Bacteriol.
132
341-345
1977
Pseudomonas aeruginosa, Pseudomonas aeruginosa Dalgleish, Pseudomonas aeruginosa PU21 RPL11
Furth, A.J.
Purification and properties of a constitutive beta-lactamase from Pseudomonas aeruginosa strain Dalgleish
Biochim. Biophys. Acta
377
431-443
1975
Pseudomonas aeruginosa, Pseudomonas aeruginosa Dalgleish
Hammond, G.G.; Huber, J.L.; Greenlee, M.L.; Laub, J.B.; Young, K.; Silver, L.L.; Balkovec, J.M.; Pryor, K.A.D.; Wu, J-K.; Leiting, B.; Pompliano, D.L.; Toney,J.H.
Inhibition of IMP-1 metallo-beta-lactamase and sensitisation of IMP-1-producing bacteria by thioester derivates
FEMS Microbiol. Lett.
179
2193-2199
1999
Bacteroides fragilis, Pseudomonas aeruginosa, Pseudomonas aeruginosa Dalgleish, Pseudomonas aeruginosa Cl5673
-
Lim, D.; Sanschagrin, F.; Passmore, L.; De Castro, L.; Levesque, R.C.; Strynadka, N.C.
Insights into the molecular basis for the carbenicillinase activity of PSE-4 beta-lactamase from crystallographic and kinetic studies
Biochemistry
40
395-402
2001
Pseudomonas aeruginosa (P16897), Pseudomonas aeruginosa
Paetzel, M.; Danel, F.; de Castro, L.; Mosimann, S.C.; Page, M.G.; Strynadka, N.C.
Crystal structure of the class D beta-lactamase OXA-10
Nat. Struct. Biol.
7
918-925
2000
Pseudomonas aeruginosa (P14489), Pseudomonas aeruginosa
Girlich, D.; Naas, T.; Nordmann, P.
Biochemical characterization of the naturally occurring oxacillinase OXA-50 of Pseudomonas aeruginosa
Antimicrob. Agents Chemother.
48
2043-2048
2004
Pseudomonas aeruginosa (Q6PL88), Pseudomonas aeruginosa
Castanheira, M.; Toleman, M.A.; Jones, R.N.; Schmidt, F.J.; Walsh, T.R.
Molecular characterization of a beta-lactamase gene, blaGIM-1, encoding a new subclass of metallo-beta-lactamase
Antimicrob. Agents Chemother.
48
4654-4661
2004
Pseudomonas aeruginosa (Q704U4), Pseudomonas aeruginosa
Poirel, L.; Brinas, L.; Verlinde, A.; Ide, L.; Nordmann, P.
BEL-1, a novel clavulanic acid-inhibited extended-spectrum beta-lactamase, and the class 1 integron In120 in Pseudomonas aeruginosa
Antimicrob. Agents Chemother.
49
3743-3748
2005
Pseudomonas aeruginosa (Q3SAW3), Pseudomonas aeruginosa
Quinteira, S.; Sousa, J.C.; Peixe, L.
Characterization of In100, a new integron carrying a metallo-{beta}-lactamase and a carbenicillinase, from Pseudomonas aeruginosa
Antimicrob. Agents Chemother.
49
451-453
2005
Pseudomonas aeruginosa (Q9K2N0), Pseudomonas aeruginosa
Jin, W.; Arakawa, Y.; Yasuzawa, H.; Taki, T.; Hashiguchi, R.; Mitsutani, K.; Shoga, A.; Yamaguchi, Y.; Kurosaki, H.; Shibata, N.; Ohta, M.; Goto, M.
Comparative study of the inhibition of metallo-beta-lactamases (IMP-1 and VIM-2) by thiol compounds that contain a hydrophobic group
Biol. Pharm. Bull.
27
851-856
2004
Pseudomonas aeruginosa, Serratia marcescens
Luzzaro, F.; Endimiani, A.; Docquier, J.D.; Mugnaioli, C.; Bonsignori, M.; Amicosante, G.; Rossolini, G.M.; Toniolo, A.
Prevalence and characterization of metallo-beta-lactamases in clinical isolates of Pseudomonas aeruginosa
Diagn. Microbiol. Infect. Dis.
48
131-135
2004
Pseudomonas aeruginosa
Kong, K.F.; Jayawardena, S.R.; Del Puerto, A.; Wiehlmann, L.; Laabs, U.; Tuemmler, B.; Mathee, K.
Characterization of poxB, a chromosomal-encoded Pseudomonas aeruginosa oxacillinase
Gene
358
82-92
2005
Pseudomonas aeruginosa
Marchiaro, P.; Tomatis, P.E.; Mussi, M.A.; Pasteran, F.; Viale, A.M; Limansky, A.S.; Vila, A.J.
Biochemical characterization of metallo-beta-lactamase VIM-11 from a Pseudomonas aeruginosa clinical strain
Antimicrob. Agents Chemother.
52
2250-2252
2007
Pseudomonas aeruginosa, Pseudomonas aeruginosa M5109
Yan, J.J.; Hsueh, P.R.; Lu, J.J.; Chan, F.Y.; Ko, W.C.; Wu, J.J.
Characterization of acquired beta-lactamases and their genetic support in multidrug-resistant Pseudomonas aeruginosa isolates in Taiwan: the prevalence of unusual integrons
J. Antimicrob. Chemother.
58
530-536
2006
Pseudomonas aeruginosa, Pseudomonas aeruginosa (Q27JM4), Pseudomonas aeruginosa (Q6QJ55), Pseudomonas aeruginosa (Q7BHJ5), Pseudomonas aeruginosa (Q9F629)
Yamaguchi, Y.; Jin, W.; Matsunaga, K.; Ikemizu, S.; Yamagata, Y.; Wachino, J.; Shibata, N.; Arakawa, Y.; Kurosaki, H.
Crystallographic investigation of the inhibition mode of a VIM-2 metallo-beta-lactamase from Pseudomonas aeruginosa by a mercaptocarboxylate inhibitor
J. Med. Chem.
50
6647-6653
2007
Pseudomonas aeruginosa
Garza-Ramos, U.; Morfin-Otero, R.; Sader, H.S.; Jones, R.N.; Hernández, E.; Rodriguez-Noriega, E.; Sanchez, A.; Carrillo, B.; Esparza-Ahumada, S.; Silva-Sanchez, J.
Metallo-beta-lactamase gene bla(IMP-15) in a class 1 integron, In95, from Pseudomonas aeruginosa clinical isolates from a hospital in Mexico
Antimicrob. Agents Chemother.
52
2943-2946
2008
Pseudomonas aeruginosa, Pseudomonas aeruginosa (Q53CM3), Pseudomonas aeruginosa (Q7AYX1)
Li, H.; Toleman, M.A.; Bennett, P.M.; Jones, R.N.; Walsh, T.R.
Complete Sequence of p07-406, a 24,179-base-pair plasmid harboring the blaVIM-7 metallo-beta-lactamase gene in a Pseudomonas aeruginosa isolate from the United States
Antimicrob. Agents Chemother.
52
3099-3105
2008
Pseudomonas aeruginosa (Q840P9), Pseudomonas aeruginosa
Juan, C.; Beceiro, A.; Gutiérrez, O.; Albertí, S.; Garau, M.; Pérez, J.L.; Bou, G.; Oliver, A.
Characterization of the new metallo-beta-lactamase VIM-13 and its integron-borne gene from a Pseudomonas aeruginosa clinical isolate in Spain
Antimicrob. Agents Chemother.
52
3589-3596
2008
Pseudomonas aeruginosa, Pseudomonas aeruginosa (Q2HY42), Pseudomonas aeruginosa (Q9XAY4), Pseudomonas aeruginosa SL2 (Q2HY42), Pseudomonas aeruginosa SL2 (Q9XAY4)
Takeda, S.; Nakai, T.; Ikeda, F.; Hatano, K.
Overproduction of a metallo-beta-lactamase by a strong promoter causes high-level imipenem resistance in a clinical isolate of Pseudomonas aeruginosa
Chemotherapy
54
181-187
2008
Pseudomonas aeruginosa (Q7DH52), Pseudomonas aeruginosa
Bedenic, B.; Vranes, J.; Sviben, M.; Beader, N.; Kalenic, S.
Postantibiotic and post-beta-lactamase inhibitor effect of carbapenems combined with EDTA against Pseudomonas aeruginosa strains producing VIM-metallo beta-lactamases
Chemotherapy
54
188-193
2008
Pseudomonas aeruginosa
Edalucci, E.; Spinelli, R.; Dolzani, L.; Riccio, M.L.; Dubois, V.; Tonin, E.A.; Rossolini, G.M.; Lagatolla, C.
Acquisition of different carbapenem resistance mechanisms by an epidemic clonal lineage of Pseudomonas aeruginosa
Clin. Microbiol. Infect.
14
88-90
2008
Pseudomonas aeruginosa, Pseudomonas aeruginosa (Q7BHJ5)
Motoshima, M.; Yanagihara, K.; Yamamoto, K.; Morinaga, Y.; Matsuda, J.; Sugahara, K.; Hirakata, Y.; Yamada, Y.; Kohno, S.; Kamihira, S.
Quantitative detection of metallo-beta-lactamase of blaIMP-cluster-producing Pseudomonas aeruginosa by real-time polymerase chain reaction with melting curve analysis for rapid diagnosis and treatment of nosocomial infection
Diagn. Microbiol. Infect. Dis.
61
222-226
2008
Pseudomonas aeruginosa (Q79MP6), Pseudomonas aeruginosa, Pseudomonas aeruginosa blaIMP-cluster-producing (Q79MP6)
Falagas, M.E.; Kanellopoulou, M.D.; Karageorgopoulos, D.E.; Dimopoulos, G.; Rafailidis, P.I.; Skarmoutsou, N.D.; Papafrangas, E.A.
Antimicrobial susceptibility of multidrug-resistant Gram negative bacteria to fosfomycin
Eur. J. Clin. Microbiol. Infect. Dis.
27
439-443
2008
Pseudomonas aeruginosa
Pena, A.; Donato, A.M.; Alves, A.F.; Leitão, R.; Cardoso, O.M.
Detection of Pseudomonas aeruginosa producing metallo-beta-lactamase VIM-2 in a central hospital from Portugal
Eur. J. Clin. Microbiol. Infect. Dis.
27
1269-1271
2008
Pseudomonas aeruginosa
Cardoso, O.; Alves, A.F.; Leitao, R.
Metallo-beta-lactamase VIM-2 in Pseudomonas aeruginosa isolates from a cystic fibrosis patient
Int. J. Antimicrob. Agents
31
375-379
2008
Pseudomonas aeruginosa
Chao, Z.; Xiao-Feng, W.; Dan-Hong, S.; Jin-Ping, Y.; Nan-Shan, Z.
Outbreak of Pseudomonas aeruginosa producing IMP-9-type metallo-beta-lactamase in Guangzhou, China
Int. J. Antimicrob. Agents
32
363-365
2008
Pseudomonas aeruginosa (P14489), Pseudomonas aeruginosa
Miyajima, Y.; Hiramatsu, K.; Mizukami, E.; Morinaga, R.; Ishii, H.; Shirai, R.; Kishi, K.; Tokimatsu, I.; Saikawa, T.; Kadota, J.
In vitro and in vivo potency of polymyxin B against IMP-type metallo-beta-lactamase-producing Pseudomonas aeruginosa
Int. J. Antimicrob. Agents
32
437-440
2008
Pseudomonas aeruginosa
Yakupogullari, Y.; Poirel, L.; Bernabeu, S.; Kizirgil, A.; Nordmann, P.
Multidrug-resistant Pseudomonas aeruginosa isolate co-expressing extended-spectrum beta-lactamase PER-1 and metallo-beta-lactamase VIM-2 from Turkey
J. Antimicrob. Chemother.
61
221-222
2008
Pseudomonas aeruginosa
Samuelsen, O.; Buarø, L.; Giske, C.G.; Simonsen, G.S.; Aasnaes, B.; Sundsfjord, A.
Evaluation of phenotypic tests for the detection of metallo-beta-lactamase-producing Pseudomonas aeruginosa in a low prevalence country
J. Antimicrob. Chemother.
61
827-830
2008
Pseudomonas aeruginosa
Dubois, V.; Arpin, C.; Dupart, V.; Scavelli, A.; Coulange, L.; André, C.; Fischer, I.; Grobost, F.; Brochet, J.P.; Lagrange, I.; Dutilh, B.; Jullin, J.; Noury, P.; Larribet, G.; Quentin, C.
Beta-lactam and aminoglycoside resistance rates and mechanisms among Pseudomonas aeruginosa in French general practice (community and private healthcare centres)
J. Antimicrob. Chemother.
62
316-323
2008
Pseudomonas aeruginosa
Kim, J.Y.; Park, Y.J.; Kwon, H.J.; Han, K.; Kang, M.W.; Woo, G.J.
Occurrence and mechanisms of amikacin resistance and its association with beta-lactamases in Pseudomonas aeruginosa: a Korean nationwide study
J. Antimicrob. Chemother.
62
479-483
2008
Pseudomonas aeruginosa
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
Cheng, X.; Wang, P.; Wang, Y.; Zhang, H.; Tao, C.; Yang, W.; Liu, M.; Jia, W.
Identification and distribution of the clinical isolates of imipenem-resistant Pseudomonas aeruginosa carrying metallo-beta-lactamase and/or class 1 integron genes
J. Huazhong Univ. Sci. Technol. Med. Sci.
28
235-238
2008
Pseudomonas aeruginosa
Tsuchimochi, N.; Takuma, T.; Shimono, N.; Nagasaki, Y.; Uchida, Y.; Harada, M.
Antimicrobial susceptibility and molecular epidemiological analysis of clinical strains of Pseudomonas aeruginosa
J. Infect. Chemother.
14
99-104
2008
Pseudomonas aeruginosa
Garcia-Saez, I.; Docquier, J.D.; Rossolini, G.M.; Dideberg, O.
The three-dimensional structure of VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa in its reduced and oxidised form
J. Mol. Biol.
375
604-611
2008
Pseudomonas aeruginosa (Q9K2N0), Pseudomonas aeruginosa
David, M.; Lemeland, J.F.; Boyer, S.
Emergence of extended-spectrum beta-lactamases in Pseudomonas aeruginosa: about 24 cases at Rouen university hospital
Pathol. Biol.
56
429-434
2008
Pseudomonas aeruginosa
Kalai Blagui, S.; Achour, W.; Abdeladhim, A.; Ben Hassen, A.
Identification of SHV-type extended spectrum beta-lactamase genes in Pseudomonas aeruginosa by PCR-restriction fragment length polymorphism and insertion site restriction-PCR.
Pathol. Biol.
57
420-424
2008
Pseudomonas aeruginosa
Sevillano, E.; Gallego, L.; García-Lobo, J.M.
First detection of the OXA-40 carbapenemase in P. aeruginosa isolates, located on a plasmid also found in A. baumannii
Pathol. Biol.
57
493-495
2008
Pseudomonas aeruginosa
Kalai Blagui, S.; Achour, W.; Bejaoui, M.; Abdeladhim, A.; Ben Hassen, A.
Detection of SHV-1 beta-lactamase in Pseudomonas aeruginosa strains by genetic methods
Pathol. Biol.
57
e73-e75
2008
Pseudomonas aeruginosa
Samuelsen, O.; Castanheira, M.; Walsh, T.R.; Spencer, J.
Kinetic characterization of VIM-7, a divergent member of the VIM metallo-beta -lactamase family
Antimicrob. Agents Chemother.
52
2905-2908
2008
Pseudomonas aeruginosa (Q840P9)
Drawz, S.M.; Bethel, C.R.; Doppalapudi, V.R.; Sheri, A.; Pagadala, S.R.; Hujer, A.M.; Skalweit, M.J.; Anderson, V.E.; Chen, S.G.; Buynak, J.D.; Bonomo, R.A.
Penicillin sulfone inhibitors of class D beta-lactamases
Antimicrob. Agents Chemother.
54
1414-1424
2010
Acinetobacter sp., Pseudomonas aeruginosa, plasmid RGN238
Hiraiwa, Y.; Morinaka, A.; Fukushima, T.; Kudo, T.
Metallo-beta-lactamase inhibitory activity of phthalic acid derivatives
Bioorg. Med. Chem. Lett.
19
5162-5165
2009
Pseudomonas aeruginosa
Lassaux, P.; Traore, D.A.; Loisel, E.; Favier, A.; Docquier, J.D.; Sohier, J.S.; Laurent, C.; Bebrone, C.; Frere, J.M.; Ferrer, J.L.; Galleni, M.
Biochemical and structural characterization of the subclass B1 metallo-beta-lactamase VIM-4
Antimicrob. Agents Chemother.
55
1248-1255
2011
Pseudomonas aeruginosa (Q8KRJ3), Pseudomonas aeruginosa
Borgianni, L.; Prandi, S.; Salden, L.; Santella, G.; Hanson, N.D.; Rossolini, G.M.; Docquier, J.D.
Genetic context and biochemical characterization of the IMP-18 metallo-beta-lactamase identified in a Pseudomonas aeruginosa isolate from the United States
Antimicrob. Agents Chemother.
55
140-145
2011
Pseudomonas aeruginosa (Q5U807), Pseudomonas aeruginosa, Pseudomonas aeruginosa PS297 (Q5U807)
Santella, G.; Docquier, J.D.; Gutkind, G.; Rossolini, G.M.; Radice, M.
Purification and biochemical characterization of IMP-13 metallo-beta-lactamase
Antimicrob. Agents Chemother.
55
399-401
2011
Pseudomonas aeruginosa (Q7WYA8)
Tan, Q.; Ogawa, A.M.; Painter, R.E.; Park, Y.W.; Young, K.; DiNinno, F.P.
4,7-Dichloro benzothien-2-yl sulfonylaminomethyl boronic acid: first boronic acid-derived beta-lactamase inhibitor with class A, C, and D activity
Bioorg. Med. Chem. Lett.
20
2622-2624
2010
Klebsiella pneumoniae (P0A3M1), Pseudomonas aeruginosa (Q6LBN9), Acinetobacter baumannii (Q8RLA6), Acinetobacter baumannii
Borra, P.S.; Leiros, H.K.; Ahmad, R.; Spencer, J.; Leiros, I.; Walsh, T.R.; Sundsfjord, A.; Samuelsen, O.
Structural and computational investigations of VIM-7: insights into the substrate specificity of vim metallo-beta-lactamases
J. Mol. Biol.
411
174-189
2011
Pseudomonas aeruginosa (Q840P9), Pseudomonas aeruginosa
Aitha, M.; Marts, A.R.; Bergstrom, A.; Moeller, A.J.; Moritz, L.; Turner, L.; Nix, J.C.; Bonomo, R.A.; Page, R.C.; Tierney, D.L.; Crowder, M.W.
Biochemical, mechanistic, and spectroscopic characterization of metallo-beta-lactamase VIM-2
Biochemistry
53
7321-7331
2014
Pseudomonas aeruginosa (Q9K2N0)
Stewart, N.K.; Smith, C.A.; Frase, H.; Black, D.J.; Vakulenko, S.B.
Kinetic and structural requirements for carbapenemase activity in GES-type beta-lactamases
Biochemistry
54
588-597
2015
Pseudomonas aeruginosa (A0EL75), Pseudomonas aeruginosa (Q7BEB3), Pseudomonas aeruginosa (Q93F76)
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Transporter Classification Database (TCDB): 9.B.29.2.7
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