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Information on EC 3.5.2.6 - beta-lactamase and Organism(s) Klebsiella pneumoniae and UniProt Accession Q6XEC0
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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: Klebsiella pneumoniae
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
ESBL
extended-spectrum beta-lactamase
Imipenem-cefoxitin hydrolyzing enzyme
-
-
-
-
imipenemase
-
-
-
-
MBL
metallo-beta-lactamase
neutrapen
-
-
-
-
Oxacillinase
-
-
-
-
penicillinase
-
-
-
-
SHV-1
SHV-2A
-
-
-
-
beta-lactamase
-
-
-
-
carbapenemase
-
-
-
-
metallo-beta-lactamase
-
-
-
-
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-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
-
-
-
?
faropenem + H2O
(2R)-2-[(1S,2R)-1-carboxy-2-hydroxypropyl]-5-[(2R)-tetrahydrofuran-2-yl]-2,3-dihydro-1,3-thiazole-4-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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
panipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S)-1-ethanimidoylpyrrolidin-3-yl]sulfanyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
temocillin + H2O
(2R,4S)-2-[(S)-carboxy[[carboxy(thiophen-3-yl)acetyl]amino]methoxymethyl]-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
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
-
-
-
?
ampicilin + 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
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
carbapenem + H2O
[(2R)-2,3-dihydro-1H-pyrrol-2-yl]acetic acid
-
-
-
?
cefalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cefalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]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
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
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
low activity
-
-
?
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-(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
low activity
-
-
?
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
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[2-(thiophen-2-yl)acetamido]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
-
-
-
?
clavulanic acid + H2O
(2R,4R,5Z)-2-(carboxymethyl)-5-(2-hydroxyethylidene)-1,3-oxazolidine-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
-
-
-
?
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)-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
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[(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
-
-
-
?
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-dioxopiperazine-1-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
sulbactam + H2O
(2R,4S)-2-(carboxymethyl)-5,5-dimethyl-1,1-dioxo-1lambda~6~,3-thiazolidine-4-carboxylic acid
-
-
-
?
tazobactam + H2O
(2R,4S,5S)-2-(carboxymethyl)-5-methyl-1,1-dioxo-5-[(1H-1,2,3-triazol-1-yl)methyl]-1lambda6,3-thiazolidine-4-carboxylic acid
-
mutant enzyme S130G, hydrolysis of the inhibitor molecule acylated by the mutant enzyme
-
-
?
tazobactam + H2O
(2R,4S,5S)-2-(carboxymethyl)-5-methyl-1,1-dioxo-5-[(1H-1,2,3-triazol-1-yl)methyl]-1lambda~6~,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
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
ampicilin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicilin + 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
beta-lactamases CTX-M-26
-
-
?
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
-
-
-
?
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
beta-lactamases CTX-M-26
-
-
?
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
beta-lactamases CTX-M-26
-
-
?
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
beta-lactamases CTX-M-26
-
-
?
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-[(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
beta-lactamases CTX-M-26
-
-
?
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
beta-lactamases CTX-M-26
-
-
?
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
beta-lactamases CTX-M-26
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-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
-
moderate rate of hydrolysis
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
efficient hydrolysis
-
-
?
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
beta-lactamases CTX-M-26
-
-
?
additional information
?
-
-
no hydrolysis of aztreonam, meropenem, ceftazidime, cefoxitin, and cefotaxime
-
-
?
additional information
?
-
the enzyme hydrolyzes penicillins, cephalothin, and the expanded-spectrum cephalosporins cefepime and moxalactam
-
-
?
additional information
?
-
antibiotic sensitivity of recombinant wild-type and mutant blaSHV-14, overview
-
-
-
additional information
?
-
-
antibiotic sensitivity of recombinant wild-type and mutant blaSHV-14, overview
-
-
-
additional information
?
-
resistance to antibiotics of recombinant His-tagged wild-type and mutant enzymes expressed in Escherichia coli strain CS109, overview
-
-
-
additional information
?
-
in vitro activity of 13 antimicrobial agents against 19 multidrug-resistant Klebsiella pneumoniae amikacin resistance isolates, overview
-
-
-
additional information
?
-
in vitro activity of 13 antimicrobial agents against 19 multidrug-resistant Klebsiella pneumoniae amikacin resistance isolates, overview
-
-
-
additional information
?
-
in vitro activity of 13 antimicrobial agents against 19 multidrug-resistant Klebsiella pneumoniae amikacin resistance isolates, overview
-
-
-
additional information
?
-
in vitro activity of 13 antimicrobial agents against 19 multidrug-resistant Klebsiella pneumoniae amikacin resistance isolates, overview
-
-
-
additional information
?
-
in vitro activity of 13 antimicrobial agents against 19 multidrug-resistant Klebsiella pneumoniae amikacin resistance isolates, overview
-
-
-
additional information
?
-
-
in vitro activity of 13 antimicrobial agents against 19 multidrug-resistant Klebsiella pneumoniae amikacin resistance isolates, overview
-
-
-
additional information
?
-
purified enzyme NDM-7 exhibits broad-spectrum enzyme activities with low Km and high kcat values hydrolysing all beta-lactam substrates tested
-
-
-
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
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
ampicilin + 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
carbapenem + H2O
[(2R)-2,3-dihydro-1H-pyrrol-2-yl]acetic 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
-
-
-
?
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
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]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
-
-
-
?
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-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
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
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy([(2R)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)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
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
additional information
?
-
the enzyme hydrolyzes penicillins, cephalothin, and the expanded-spectrum cephalosporins cefepime and moxalactam
-
-
?
additional information
?
-
antibiotic sensitivity of recombinant wild-type and mutant blaSHV-14, overview
-
-
-
additional information
?
-
-
antibiotic sensitivity of recombinant wild-type and mutant blaSHV-14, overview
-
-
-
additional information
?
-
resistance to antibiotics of recombinant His-tagged wild-type and mutant enzymes expressed in Escherichia coli strain CS109, overview
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
Zn2+
the active-site residues His120, His122 and His189 are co-ordinated to Zn1 metal ion, whereas Asp124, Cys208 and His250 are co-ordinated to Zn2 metal ion for their catalytic activity. The di-zinc centre of NDM-7 is located at the bottom of the shallow groove and is a part of the binding pocket of the enzyme. The two Zn metal ions present in the active-site cleft take part in the catalytic activity of the NDM-7 via bridging to different active-site residues by forming strong interactions
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-(7-(4-methoxyphenyl)-5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidin-4-ylidene)-malononitrile
-
-
4-chloro-7-(4-methoxyphenyl)-5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidine
-
-
4-chloro-7-(4-methylphenyl)-5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidine
-
-
7-(4-methylphenyl)-8,9-diphenyl-7H-pyrrolo[3,2-e][1,2,4]triazolo[4,3-c]pyrimidine-3-thione
-
-
beta-lactamase inhibitor protein
i.e. BLIP, 17 kDa protein produced by Streptomyces clavuligerus, specific for class A enzymes, construction of diverse mutants of BLIP for identification of functional epitopes, enzyme-inhibitor complex modeling
-
KCl
-
concentrations of KCl higher than 20 mM weaken slightly the hydrolytic ability of VIM-12
N-benzylidene-N'-(7-(4-methylphenyl)-5,6-diphenyl-7Hpyrrolo[2,3-d]pyramidin-4-yl)-hydrazine
-
-
tazobactam fragment
five-atom vinyl carboxylic acid fragment of tazobactam, bonded to Ser130
-
ZINC01807204
ZINC01807204 might be useful as a lead molecule for further optimization and development of more potent non beta-lactam inhibitors against KPC-2
tazobactam
-
class A-specific inhibitor, inactivation of the wild-type enzyme, binds to Ser70 of the active site, mutant S130G is resistant, inhibition mechanism, the mutation S130G is not essential for resistance but for acylation of the inhibitor molecule, which initiates the fragmentation of tazobactam by the mutant enzyme, mass spectrometry analysis
tazobactam
sulfone inhibitor, acyclic form is covalently bound to ctalytic Ser70 side chain
additional information
poor inhibitory potencies of classic beta-lactamase inhibitors clavulanic acid, tazobactam, and sulbactam, which rather act as substrate with the enzyme. Non beta-lactam inhibitors by structure-based virtual screening of ZINC database. MIC values for cytotoxic effects on Escherichia coli and HeLa cells, overview
-
additional information
-
poor inhibitory potencies of classic beta-lactamase inhibitors clavulanic acid, tazobactam, and sulbactam, which rather act as substrate with the enzyme. Non beta-lactam inhibitors by structure-based virtual screening of ZINC database. MIC values for cytotoxic effects on Escherichia coli and HeLa cells, overview
-
additional information
mutation at the glutamate residues in the omega-loop of SHV-14, i.e. E126, E164, and E167, render beta-lactamase inhibitors more efficient
-
additional information
-
mutation at the glutamate residues in the omega-loop of SHV-14, i.e. E126, E164, and E167, render beta-lactamase inhibitors more efficient
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.027
(2S,5R,6R)-6-[[(2R)-2-carboxy-2-thiophen-3-ylacetyl]amino]-3,3-dimethyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylic acid
beta-lactamases CTX-M-26
0.394
ceftaxidime
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
0.506
cephaloridine
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
0.041
amoxicillin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
0.05414
amoxicillin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
0.0697
amoxicillin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
0.032
ampicillin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
0.414
ampicillin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
0.615
ampicillin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
0.37
benzylpenicillin
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
0.0383
cefoperazone
pH 7.5, 25°C, recombinant His-tagged mutant E162A
0.0574
cefoperazone
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
0.0962
cefoperazone
pH 7.5, 25°C, recombinant His-tagged mutant E164A
0.341
cefotaxime
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
0.65
cefoxitin
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
0.045
cephalothin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
0.057
cephalothin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
0.227
cephalothin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
0.577
cephalothin
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
0.0042
Imipenem
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
0.011
nitrocefin
pH 7.2, 25°C, recombinant enzyme
0.038
nitrocefin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
0.045
nitrocefin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
0.1893
nitrocefin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
0.0557
piperacillin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
0.058
piperacillin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
0.0716
piperacillin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
0.454
piperacillin
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
additional information
additional information
Michaelis-Menten steady-state kinetics studies
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics studies
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
84
(2S,5R,6R)-6-[[(2R)-2-carboxy-2-thiophen-3-ylacetyl]amino]-3,3-dimethyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylic acid
beta-lactamases CTX-M-26
0.3
ceftaxidime
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
190
cephaloridine
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
2.03
amoxicillin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
2.38
amoxicillin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
532.5
amoxicillin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
21.5
ampicillin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
544
ampicillin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
317
benzylpenicillin
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
0.21
cefoperazone
pH 7.5, 25°C, recombinant His-tagged mutant E162A
0.705
cefoperazone
pH 7.5, 25°C, recombinant His-tagged mutant E164A
229.5
cefoperazone
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
2.9
cefotaxime
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
0.43
cephalothin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
0.44
cephalothin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
49.7
cephalothin
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
113
cephalothin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
0.08
nitrocefin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
0.125
nitrocefin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
5.85
nitrocefin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
2.2
piperacillin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
2.46
piperacillin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
4
piperacillin
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
677
piperacillin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
43.96
amoxicillin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
49.51
amoxicillin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
36334.3
amoxicillin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
34.96
ampicillin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
36.23
ampicillin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
17000
ampicillin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
5.48
cefoperazone
pH 7.5, 25°C, recombinant His-tagged mutant E162A
7.33
cefoperazone
pH 7.5, 25°C, recombinant His-tagged mutant E164A
3998.3
cefoperazone
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
1.89
cephalothin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
7.72
cephalothin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
2511.1
cephalothin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
0.21
nitrocefin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
0.66
nitrocefin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
130
nitrocefin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
30.73
piperacillin
pH 7.5, 25°C, recombinant His-tagged mutant E164A
44.17
piperacillin
pH 7.5, 25°C, recombinant His-tagged mutant E162A
11672.4
piperacillin
pH 7.5, 25°C, recombinant His-tagged wild-type enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.029
2-(7-(4-methoxyphenyl)-5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidin-4-ylidene)-malononitrile
-
pH 7.0, temperature not specified in the publication
0.012
4-chloro-7-(4-methoxyphenyl)-5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidine
-
pH 7.0, temperature not specified in the publication
0.019
4-chloro-7-(4-methylphenyl)-5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidine
-
pH 7.0, temperature not specified in the publication
0.033
4-chloro-7-(4-methylphenyl)-5-phenyl-7H-pyrrolo[2,3-d]pyrimidine
-
pH 7.0, temperature not specified in the publication
0.015
7-(4-methylphenyl)-8,9-diphenyl-7H-pyrrolo[3,2-e][1,2,4]triazolo[4,3-c]pyrimidine-3-thione
-
pH 7.0, temperature not specified in the publication
0.0011
beta-lactamase inhibitor protein
wild-type inhibitor protein, pH 7.5, 25°C
-
0.018
N-benzylidene-N'-(7-(4-methylphenyl)-5,6-diphenyl-7Hpyrrolo[2,3-d]pyramidin-4-yl)-hydrazine
-
pH 7.0, temperature not specified in the publication
additional information
additional information
Ki for diverse mutants of beta-lactamase inhibitor protein BLIP, overview
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00057
4,7-dichlorobenzothien-2-yl-sulfonylaminomethylboronic acid
Klebsiella pneumoniae
pH not specified in the publication, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
isoelectric focusing, beta-lactamases CTX-M-26, pH-range 3.5-9.5
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
the recombinant plasmid pVT-1 is used as a source of the blaOXA-48 gene. The blaOXA-48 ORF is subcloned into expression vector pET-9a to yield recombinant plasmid pET-OXA-48. Escherichia coli MCT236(DE3) is used as the host for overproduction of the OXA-48 enzyme
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
mutation at the glutamate residues in the omega-loop of SHV-14, i.e. E126, E164, and E167, can considerably modulate the beta-lactam sensitivity and reduce hydrolysis. The mutations in SHV-14 render beta-lactamase inhibitors more efficient. The mutations alter the active site configuration of SHV-14
physiological function
additional information
evolution
extended-spectrum beta-lactamases (ESBL)-producing Enterobacteriaceae from spring waters can be a thread to human health. ESBL-producing Enterobacteriaceae were found in four out of 50 sampled spring waters (4/50, 8.0%) and a total of 16 non-duplicate ESBL-producing Enterobacteriaceae are obtained, including 13 Escherichia coli and three Klebsiella pneumoniae strains. All 16 nonduplicate ESBL-producing Enterobacteriaceae isolates harbour genes encoding CTX-M ESBLs, among which six expressed CTX-M-15, five produced CTX-M-14, three produced CTX-M-55 and two expressed CTX-M-27. Four multilocus sequence types (ST) are found and ST131 is the dominant type (8/16, 50.0%). The contamination of ESBL-producing Enterobacteriaceae are present in spring waters of Mountain Tai
evolution
-
genotyping and phenotyping of Escherichia coli strains with beta-lactamase activity in faeces from ducks, phylogenetic analysis. In Klebsiella pneumoniae 10, 3, and 4 isolates possess blaTEM, blaSHV, and blaCTX-M genes, respectively. The sequences of selected PCR products are found 98% cognate with blaCTX-M-9, blaSHV-12 and blaTEM-1. 13 Klebsiella pneumoniae isolates (43.33%) are detected as AmpC producers possessing gene blaAmpC. Significantly higher occurrence of beta-lactamase and biofilm producing Enterobacteriaceae isolates is detected in backyard ducks than organized farms
physiological function
New Delhi MBL (NDM)-1 is a clinically significant metallo beta-lactamase
physiological function
84 multidrug-resistant Klebsiella pneumoniae (MDR-KP) clinical isolates studied, 19 isolates exhibit high level resistance to amikacin mediated by the production of the 16S rRNA methylase. CTX-M genes were found in all of the isolates. Among these armA- or rmtB/CTX-M-producing Klebsiella pneumoniae isolates, 31.6% carry the carbapenemase genes (blaKPC-2 [26.3%], blaIMP-4 [10.5%], and blaNDM-1 [5.3%]), which made them resistant to imipenem
physiological function
extensive production of SHV-14 beta-lactamase makes Klebsiella pneumoniae resistant to beta-lactams. The presence of an omega-loop has been reported to influence the beta-lactamase activity, which is also present in SHV-14
additional information
different genotypes of the New Delhi metallo beta-lactamase are identified: the substitutions do not affect the overall folds of the enzyme variants, within limits of detection. Differences in thermal stabilities are observed. kcat/KM values are similar for carbapenem and penicillin substrates for NDM variants, but differences in kinetics are observed for cephalosporin substrates. Apparent substrate inhibition is observed with nitrocefin for variants containing the M154L substitution. In all cases, cefoxitin and ceftazidime are poorly hydrolysed. Clinically observed substitutions can make substantial differences in thermodynamic stability, suggesting that this may be a factor in metallo beta-lactamase evolution. Comparative analysis of the beta-lactam susceptibility of the NDM variants in Escherichia coli, overview
additional information
different genotypes of the New Delhi metallo beta-lactamase are identified: the substitutions do not affect the overall folds of the enzyme variants, within limits of detection. Differences in thermal stabilities are observed. kcat/KM values are similar for carbapenem and penicillin substrates for NDM variants, but differences in kinetics are observed for cephalosporin substrates. Apparent substrate inhibition is observed with nitrocefin for variants containing the M154L substitution. In all cases, cefoxitin and ceftazidime are poorly hydrolysed. Clinically observed substitutions can make substantial differences in thermodynamic stability, suggesting that this may be a factor in metallo beta-lactamase evolution. Comparative analysis of the beta-lactam susceptibility of the NDM variants in Escherichia coli, overview
additional information
different genotypes of the New Delhi metallo beta-lactamase are identified: the substitutions do not affect the overall folds of the enzyme variants, within limits of detection. Differences in thermal stabilities are observed. kcat/KM values are similar for carbapenem and penicillin substrates for NDM variants, but differences in kinetics are observed for cephalosporin substrates. Apparent substrate inhibition is observed with nitrocefin for variants containing the M154L substitution. In all cases, cefoxitin and ceftazidime are poorly hydrolysed. Clinically observed substitutions can make substantial differences in thermodynamic stability, suggesting that this may be a factor in metallo beta-lactamase evolution. Comparative analysis of the beta-lactam susceptibility of the NDM variants in Escherichia coli, overview
additional information
Mox-1 is a unique plasmid-mediated class C beta-lactamase. Structure comparison with other beta-lactamases shows that two region in Mox 1, amino acid residues 214 to 216 positioned in the omega loop and the other in the N-terminus of the B3 beta-strand corresponding to amino acid residues 303 to 306, having significant structural flexibility of these regions, may impact the recognition and binding of substrates in Mox-1 leading to the unique substrate profile of the enzyme, overview. A substrate-induced conformational change underlies the basis of the hydrolytic profile of Mox-1 beta-lactamase, active site structure of enzyme Mox-1, overview
additional information
close to 80% of blaTEM-1 and blaSHV-12 are linked to IS26 while 90% or more of blaCTX-Ms and blaCMYs are linked to ISEcp1. ISAba125 is located upstream of blaNDM-1 and some blaCMY-2 genes. In addition, seven transconjugants are available for further analysis, and armA, qnrS1, acc(6')-Ib-cr, blaCTX-M-15, blaTEM-1, and blaNDM-1 are cotransferred. The dissemination of 16S rRNA methylase genes and the prevalence of selected elements implicated in evolution of antibiotics resistance determinants in collection of clinical Klebsiella pneumoniae in China, overview
additional information
close to 80% of blaTEM-1 and blaSHV-12 are linked to IS26 while 90% or more of blaCTX-Ms and blaCMYs are linked to ISEcp1. ISAba125 is located upstream of blaNDM-1 and some blaCMY-2 genes. In addition, seven transconjugants are available for further analysis, and armA, qnrS1, acc(6')-Ib-cr, blaCTX-M-15, blaTEM-1, and blaNDM-1 are cotransferred. The dissemination of 16S rRNA methylase genes and the prevalence of selected elements implicated in evolution of antibiotics resistance determinants in collection of clinical Klebsiella pneumoniae in China, overview
additional information
close to 80% of blaTEM-1 and blaSHV-12 are linked to IS26 while 90% or more of blaCTX-Ms and blaCMYs are linked to ISEcp1. ISAba125 is located upstream of blaNDM-1 and some blaCMY-2 genes. In addition, seven transconjugants are available for further analysis, and armA, qnrS1, acc(6')-Ib-cr, blaCTX-M-15, blaTEM-1, and blaNDM-1 are cotransferred. The dissemination of 16S rRNA methylase genes and the prevalence of selected elements implicated in evolution of antibiotics resistance determinants in collection of clinical Klebsiella pneumoniae in China, overview
additional information
close to 80% of blaTEM-1 and blaSHV-12 are linked to IS26 while 90% or more of blaCTX-Ms and blaCMYs are linked to ISEcp1. ISAba125 is located upstream of blaNDM-1 and some blaCMY-2 genes. In addition, seven transconjugants are available for further analysis, and armA, qnrS1, acc(6')-Ib-cr, blaCTX-M-15, blaTEM-1, and blaNDM-1 are cotransferred. The dissemination of 16S rRNA methylase genes and the prevalence of selected elements implicated in evolution of antibiotics resistance determinants in collection of clinical Klebsiella pneumoniae in China, overview
additional information
close to 80% of blaTEM-1 and blaSHV-12 are linked to IS26 while 90% or more of blaCTX-Ms and blaCMYs are linked to ISEcp1. ISAba125 is located upstream of blaNDM-1 and some blaCMY-2 genes. In addition, seven transconjugants are available for further analysis, and armA, qnrS1, acc(6')-Ib-cr, blaCTX-M-15, blaTEM-1, and blaNDM-1 are cotransferred. The dissemination of 16S rRNA methylase genes and the prevalence of selected elements implicated in evolution of antibiotics resistance determinants in collection of clinical Klebsiella pneumoniae in China, overview
additional information
-
close to 80% of blaTEM-1 and blaSHV-12 are linked to IS26 while 90% or more of blaCTX-Ms and blaCMYs are linked to ISEcp1. ISAba125 is located upstream of blaNDM-1 and some blaCMY-2 genes. In addition, seven transconjugants are available for further analysis, and armA, qnrS1, acc(6')-Ib-cr, blaCTX-M-15, blaTEM-1, and blaNDM-1 are cotransferred. The dissemination of 16S rRNA methylase genes and the prevalence of selected elements implicated in evolution of antibiotics resistance determinants in collection of clinical Klebsiella pneumoniae in China, overview
additional information
-
consumption of antibiotic through feed or during therapy is considered as potential reason for generation of antimicrobial resistant bacteria in birds
additional information
Glu152 and Ser191 are the key residues required for the metallo-beta-lactamase activity of strain NDM-7. Three-dimensional structure homology modelling of wild-type BlaNDM-7 and mutant enzymes
additional information
substrate binding to active site residues of SHV-14 wild-type and mutant enzyme proteins, structures, overview
additional information
-
substrate binding to active site residues of SHV-14 wild-type and mutant enzyme proteins, structures, 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
38000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 30000, about, recombinant wild-type and mutant enzymes, SDS-PAGE and MALDI-ToF MS analysis
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop method, crystal structure of the OXA-48 carbapenemase is determined at pH 7.5 and at a resolution of 1.9 A. The enzyme shows a noncrystallographic pseudo 2-fold axis
crystal structure of the complex of SHV-1 mutant D104E with beta-lactamse inhibitor protein BLIP, to 1.6 A resolution. Mutation D104E results in a 1000fold enhancement in binding affinity to BLIP, as it restores a salt bridge to BLIP. Mutation of a neighboring residue, BLIP E73M, results in salt bridge formation between SHV-1 D104 and BLIP K74 and a 400fold increase in binding affinity. BLIP F142 cooperatively stabilizes both interactions
purified recombinant enzyme, hanging-drop or sitting-drop vapor diffusion, mixing of 10 mg/ml protein in 10 mM Tris-HCl, pH 7.0, with reservoir solution containing of 20% PEG 8000, 100 mM sodium cacodylate, pH 6.5, and 0.2 M zinc acetate, to a finaal volume of 0.01 ml, equilibration against 0.5 ml reservoir solution, 1 month, 16°C, X-ray diffraction structure determination and analysis at 1.54 A resolution, modeling and molecular replacement
vapour diffusion method, 1.5 A resolution, space group 2(1), a = 49.7 A, b = 59.5 A, c = 63.75 A, beta = 102.57°
-
vapour diffusion method, 2.5 A resolution, space group 2(1), a = 49.73 A, b = 59.54 A, c = 63.78 A, beta = 102.52°
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D104E
mutation results in a 1000fold enhancement in binding affinity to beta-lactamase inhibitor protein BLIP, as it restores a salt bridge to BLIP. Mutation of a neighboring residue, BLIP E73M, results in salt bridge formation between SHV-1 D104 and BLIP K74 and a 400fold increase in binding affinity. BLIP F142 cooperatively stabilizes both interactions
D223A
site-directed mutagenesis, the mutation does not signifcantly affect resistance of the cells against antibiotics
E152A
site-directed mutagenesis, the mutant shows highly declined resistance to antibiotics compared to wild-type NDM-7
E152A/S191A
site-directed mutagenesis, the double mutant shows 2fold reduced antibiotic resistance compared to single mutants, but substantially declined resistance compared to wild-type NDM-7
E162A
site-directed mutagenesis, mutation of the an omega loop glutamate, the mutant shows reduced activity against penicilin and cepahlosporin antibiotics in recombinant Escherichia coli cells and reduces the resistance level of the cells
E164A
site-directed mutagenesis, mutation of the an omega loop glutamate, the mutant shows highly reduced activity against penicilin and cepahlosporin antibiotics in recombinant Escherichia coli cells and potently reduces the resistance level of the cells
E167A
site-directed mutagenesis, mutation of the an omega loop glutamate, the mutant shows reduced activity against penicilin and cepahlosporin antibiotics in recombinant Escherichia coli cells and reduces the resistance level of the cells
G69S/A74T/G200R
naturally occuring genetic variation
K216A
site-directed mutagenesis, the mutation does not signifcantly affect resistance of the cells against antibiotics
S130G
S191A
site-directed mutagenesis, mutant shows highly declined resistance to antibiotics compared to wild-type NDM-7
S213A
site-directed mutagenesis, the mutation does not signifcantly affect resistance of the cells against antibiotics
additional information
S130G
-
site-directed mutagenesis, resistant to inhibition by taxobactam in contrast to the wild-type enzyme
S130G
-
mutant resistant to tazobactam, sulbactam, clavulanic acid, and 2'-glutaroxy penem sulfone
additional information
construction of diverse mutant of the beta-lactamase inhibitor protein BLIP by alanine scanning mutation
additional information
TEM-107 extended-spectrum beta-lactamase detected in a Klebsiella pneumoniae clinical isolate has a Gly238Ser substitution compared to the TEM-43 beta-lactamase
additional information
-
TEM-107 extended-spectrum beta-lactamase detected in a Klebsiella pneumoniae clinical isolate has a Gly238Ser substitution compared to the TEM-43 beta-lactamase
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
59.5
melting temperature of the purified NDM-1 variant
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
recombinant active N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography to homogeneity
recombinant His-tagged enzyme from Escherichia coli BL21(DE3)/pLysS by nickel affinity chhromatography and gel filtration
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, cleavage of the N-terminal His6-tag using recombinant human Rhinovirus 3C protease, and further purification of the untagged protein by affinity chromatography, followed by ultrafiltration
recombinant N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene blaCTX-M-14, extended-spectrum beta-lactamases (ESBL), genotyping
gene blaCTX-M-15, extended-spectrum beta-lactamases (ESBL), genotyping
gene blaKPC-2, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene blaNDM-1, genotyping, recombinant N-terminally His6-tagged enzyme expression in Escherichia coli strain BL21(DE3)
gene blaNDM-10, genotyping, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene blaNDM-7, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strains BL21(DE3) and CS109, subcloning in Escherichia coli strain XL-1 Blue. Host Escherichia coli strain CS109 harbouring cloned blaNDM-7 displays a resistant status with over 60fold increased resistance compared to control strain CS109 for all penicillins, cephalosporin and carbapenems tested
gene blaNDM-9, genotyping, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene blaSHV-14, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strains BL21(DE3) and CS109. On expression, the clone of wild-type SHV-14 aggravates the resistance of host by 60-500 folds against penicillin and cephalosporin groups of antibiotics, while the expression of mutated enzymes (especially E164A) substantially reduces the resistance level as compared to the wild-type, and the results are in synchrony with the estimated enzymatic efficiencies of wild-type and mutated proteins
genotyping and phenotyping of Klebsiella strains with beta-lactamase activity in faeces from ducks
-
Mox-1 is a unique plasmid-mediated class C beta-lactamase, recombinant expression of His-tagged enzyme in Escherichia coli BL21(DE3)/pLysS
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
ZINC01807204 might be useful as a lead molecule for further optimization and development of more potent non beta-lactam inhibitors against KPC-2
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
Kuzin, A.P.; Nukaga, M.; Nukaga, Y.; Hujer, A.; Bonomo, R.A.; Knox, J.R.
Inhibition of the SHV-1 beta-lactamase by sulfones: crystallographic observation of two reaction intermediates with tazobactam
Biochemistry
40
1861-1866
2001
Klebsiella pneumoniae (P0AD64), Klebsiella pneumoniae 15571 (P0AD64)
Pagan-Rodriguez, D.; Zhou, X.; Simmons, R.; Bethel, C.R.; Hujer, A.M.; Helfand, M.S.; Jin, Z.; Guo, B.; Anderson, V.E.; Ng, L.M.; Bonomo, R.A.
Tazobactam inactivation of SHV-1 and the inhibitor-resistant Ser130 -->Gly SHV-1 beta-lactamase: insights into the mechanism of inhibition
J. Biol. Chem.
279
19494-19501
2004
Klebsiella pneumoniae
Zhang, Z.; Palzkill, T.
Dissecting the protein-protein interface between beta-lactamase inhibitory protein and class A beta-lactamases
J. Biol. Chem.
279
42860-42866
2004
Bacillus anthracis, Serratia marcescens, Klebsiella pneumoniae (P0AD64), Escherichia coli (P62593)
Lee, S.J.; Kim, J.Y.; Jung, H.I.; Suh, P.G.; Lee, H.S.; Lee, S.H.; Cha, S.S.
Crystallization and preliminary X-ray crystallographic analyses of CMY-1 and CMY-10, plasmidic class C beta-lactamases with extended substrate spectrum
Acta Crystallogr. Sect. D
60
382-384
2004
Klebsiella pneumoniae
Munday, C.J.; Boyd, D.A.; Brenwald, N.; Miller, M.; Andrews, J.M.; Wise, R.; Mulvey, M.R.; Hawkey, P.M.
Molecular and kinetic comparison of the novel extended-spectrum beta-lactamases CTX-M-25 and CTX-M-26
Antimicrob. Agents Chemother.
48
4829-4834
2004
Klebsiella pneumoniae (Q8GD10), Klebsiella pneumoniae, Escherichia coli (Q8KSA6), Escherichia coli
Villegas, M.V.; Correa, A.; Perez, F.; Miranda, M.C.; Zuluaga, T.; Quinn, J.P.; Quinn, J.P.
Prevalence and characterization of extended-spectrum beta-lactamases in Klebsiella pneumoniae and Escherichia coli isolates from Colombian hospitals
Diagn. Microbiol. Infect. Dis.
49
217-222
2004
Escherichia coli, Klebsiella pneumoniae
Kontou, M.; Pournaras, S.; Kristo, I.; Ikonomidis, A.; Maniatis, A.N.; Stathopoulos, C.
Molecular cloning and biochemical characterization of VIM-12, a novel hybrid VIM-1/VIM-2 metallo-beta-lactamase from a Klebsiella pneumoniae clinical isolate, reveal atypical substrate specificity
Biochemistry
46
13170-13178
2007
Klebsiella pneumoniae, Klebsiella pneumoniae 2873
Helfand, M.S.; Taracila, M.A.; Totir, M.A.; Bonomo, R.A.; Buynak, J.D.; van den Akker, F.; Carey, P.R.
Raman crystallographic studies of the intermediates formed by Ser130Gly SHV, a beta-lactamase that confers resistance to clinical inhibitors
Biochemistry
46
8689-8699
2007
Klebsiella pneumoniae
Bae, I.K.; Lee, Y-N.; Jeong, S.H.; Hong, S.G.; Lee, J.H.; Lee, S.H.; Kim, H.J.; Youn, H.
Genetic and biochemical characterization of GES-5, an extended-spectrum class A beta-lactamase from Klebsiella pneumoniae
Diagn. Microbiol. Infect. Dis.
58
465-468
2007
Klebsiella pneumoniae (Q09HD0), Klebsiella pneumoniae, Klebsiella pneumoniae CHAK36 (Q09HD0)
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
Mendonca, N.; Manageiro, V.; Bonnet, R.; Canica, M.
Biochemical characterization of SHV-55, an extended-spectrum class a beta -lactamase from Klebsiella pneumoniae
Antimicrob. Agents Chemother.
52
1897-1898
2008
Klebsiella pneumoniae (Q4TVR4), Klebsiella pneumoniae
Chen, Y.; Cheng, J.; Wang, Q.; Ye, Y.; Li, J.; Zhang, X.
ACT-3, a novel plasmid-encoded class C beta -lactamase in a Klebsiella pneumoniae isolate from China
Int. J. Antimicrob. Agents
33
95-96
2009
Klebsiella pneumoniae (A1EGT8), Klebsiella pneumoniae
Docquier, J.D.; Calderone, V.; De Luca, F.; Benvenuti, M.; Giuliani, F.; Bellucci, L.; Tafi, A.; Nordmann, P.; Botta, M.; Rossolini, G.M.; Mangani, S.
Crystal structure of the OXA-48 beta-lactamase reveals mechanistic diversity among class D carbapenemases
Chem. Biol.
16
540-547
2009
Klebsiella pneumoniae (Q6XEC0)
Lee, K.; Yum, J.H.; Yong, D.; Jeong, S.H.; Rossolini, G.M.; Docquier, J.D.; Chong, Y.
Biochemical characterization of the TEM-107 extended-spectrum beta-lactamase in a Klebsiella pneumoniae isolate from South Korea
Antimicrob. Agents Chemother.
55
5930-5932
2011
Klebsiella pneumoniae (Q8KQ59), Klebsiella pneumoniae
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
Mohamed, M.S.; Hussein, W.M.; McGeary, R.P.; Vella, P.; Schenk, G.; Abd El-Hameed, R.H.
Synthesis and kinetic testing of new inhibitors for a metallo-beta-lactamase from Klebsiella pneumonia and Pseudomonas aeruginosa
Eur. J. Med. Chem.
46
6075-6082
2011
Klebsiella pneumoniae
Hanes, M.; Reynolds, K.; Mcnamara, C.; Ghosh, P.; Bonomo, R.; Kirsch, J.; Handel, T.
Specificity and cooperativity at beta-lactamase position 104 in TEM-1/BLIP and SHV-1/BLIP interactions
Proteins Struct. Funct. Bioinform.
79
1267-1276
2011
Klebsiella pneumoniae (P0AD64)
Oguri, T.; Furuyama, T.; Okuno, T.; Ishii, Y.; Tateda, K.; Bonomo, R.A.; Shimizu-Ibuka, A.
Crystal structure of Mox-1, a unique plasmid-mediated class C beta-lactamase with hydrolytic activity towards moxalactam
Antimicrob. Agents Chemother.
58
3914-3920
2014
Klebsiella pneumoniae (Q51578), Klebsiella pneumoniae NU2936 (Q51578)
Makena, A.; Brem, J.; Pfeffer, I.; Geffen, R.E.; Wilkins, S.E.; Tarhonskaya, H.; Flashman, E.; Phee, L.M.; Wareham, D.W.; Schofield, C.J.
Biochemical characterization of New Delhi metallo-beta-lactamase variants reveals differences in protein stability
J. Antimicrob. Chemother.
70
463-469
2015
Escherichia coli (A0A024FRL9), Escherichia coli (A0A0F6N6D4), Escherichia coli (H6WET3), Escherichia coli (H6WZS9), Escherichia coli (I3VKD5), Escherichia coli (J7I0S9), Escherichia coli (M1VE66), Klebsiella pneumoniae (C7C422), Klebsiella pneumoniae (S5ZIP8), Klebsiella pneumoniae (T2A6Y2), Acinetobacter baumannii (F2YZ26)
Khan, A.; Faheem, M.; Danishuddin, M.; Khan, A.U.
Evaluation of inhibitory action of novel non beta-lactam inhibitor against Klebsiella pneumoniae carbapenemase (KPC-2)
PLoS ONE
9
e108246
2014
Klebsiella pneumoniae (G3GCC6), Klebsiella pneumoniae, Klebsiella pneumoniae NP6 (G3GCC6)
Kumar, G.; Biswal, S.; Nathan, S.; Ghosh, A.S.
Glutamate residues at positions 162 and 164 influence the beta-lactamase activity of SHV-14 obtained from Klebsiella pneumoniae
FEMS Microbiol. Lett.
365
fnx259
2018
Klebsiella pneumoniae (Q9F918), Klebsiella pneumoniae, Klebsiella pneumoniae MTCC 3384 (Q9F918)
Kumar, G.; Issa, B.; Biswal, S.; Jain, D.; Bhattacharjee, A.; Ghosh, A.S.
Glutamic acid at position 152 and serine at position 191 are the key residues required for the metallo-beta-lactamase activity of NDM-7
Int. J. Antimicrob. Agents
55
105824
2019
Klebsiella pneumoniae (A0A173MZL7), Klebsiella pneumoniae NDM-7 (A0A173MZL7)
Li, S.; Zhu, Z.C.; Wang, L.; Zhou, Y.F.; Tang, Y.J.; Miao, Z.M.
Prevalence and characterization of extended-spectrum beta-lactamase-producing Enterobacteriaceae in spring waters
Lett. Appl. Microbiol.
61
544-548
2015
Klebsiella pneumoniae (D2D9A0), Klebsiella pneumoniae (Q2PUH3), Klebsiella pneumoniae, Escherichia coli (Q0GA57), Escherichia coli (Q840M4), Escherichia coli (Q9EXV5), Escherichia coli (Q9L5C7), Escherichia coli
Banerjee, A.; Bardhan, R.; Chowdhury, M.; Joardar, S.N.; Isore, D.P.; Batabyal, K.; Dey, S.; Sar, T.K.; Bandyopadhyay, S.; Dutta, T.K.; Samanta, I.
Characterization of beta-lactamase and biofilm producing Enterobacteriaceae isolated from organized and backyard farm ducks
Lett. Appl. Microbiol.
69
110-115
2019
Escherichia coli, Klebsiella pneumoniae, Salmonella sp.
Wei, D.D.; Wan, L.G.; Yu, Y.; Xu, Q.F.; Deng, Q.; Cao, X.W.; Liu, Y.
Characterization of extended-spectrum beta-lactamase, carbapenemase, and plasmid quinolone determinants in Klebsiella pneumoniae isolates carrying distinct types of 16S rRNA methylase genes, and their association with mobile genetic elements
Microb. Drug Resist.
21
186-193
2015
Klebsiella pneumoniae (C7C422), Klebsiella pneumoniae (Q2PUH3), Klebsiella pneumoniae (Q48434), Klebsiella pneumoniae (Q4LDF1), Klebsiella pneumoniae (Q93LQ9), Klebsiella pneumoniae
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