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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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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.2 In cyclic amides
                3.5.2.6 beta-lactamase
IUBMB Comments
A group of enzymes of varying specificity hydrolysing beta-lactams; some act more rapidly on penicillins, some more rapidly on cephalosporins. The latter were formerly listed as EC 3.5.2.8, cephalosporinase.
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Select one or more organisms in this record:
This record set is specific for:
Klebsiella pneumoniae
UNIPROT: Q6XEC0
Word Map
The taxonomic range for the selected organisms is: Klebsiella pneumoniae
The enzyme appears in selected viruses and cellular organisms
Synonyms
ACT-3, ALI-1, Ambler class A beta-lactamase, AmpC, AmpC beta-lactamase, AmpC beta-lactamases M19, AmpC beta-lactamases M29, AmpC beta-lactamases M37, AmpC M19, AmpC M29, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACT-3
289026
plasmid-encoded class C beta-lactamase
AmpC-type beta-lactamase
289026
-
Beta lactamase OXA-10
-
-
-
-
beta-lactamase
beta-lactamase AME I
-
-
-
-
beta-lactamase II
-
-
-
-
beta-lactamases CTX-M-26
278955
-
BLAIMP
-
-
-
-
carbapenemase
Carbenicillinase
-
-
-
-
cefotaximase
-
-
-
-
ceftazidimase
-
-
-
-
cefurooximase
-
-
-
-
Cefuroximase
-
-
-
-
Cephalosporinase
-
-
-
-
class A beta-lactamase
297944
-
class C beta-lactamase
extended-spectrum beta-lactamase
GES-5
285108
an extended-spectrum class A beta-lactamase
Imipenem-cefoxitin hydrolyzing enzyme
-
-
-
-
imipenemase
-
-
-
-
KPC-2
303925
-
metallo-beta-lactamase
Mox-1
303926
-
Mox-1 beta-lactamase
303926
-
NDM
303912, 303920, 303921
-
NDM-1
303912
-
NDM-10
303921
-
NDM-9
303920
-
neutrapen
-
-
-
-
New Delhi MBL
303912, 303920, 303921
-
New Delhi metallo-beta-lactamase
303912, 303920, 303921
-
OXA-48 carbapenemase
293339
-
Oxacillinase
-
-
-
-
penicillinase
-
-
-
-
plasmidic class C beta-lactamase
758
-
SHV beta-lactamase
758
-
SHV-1
SHV-2A
-
-
-
-
SHV-5
297940
-
SHV-55
289019
-
TEM-107
297944
-
VIM-12
758
a hybrid VIM-1/VIM-2 metallo-beta-lactamase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amide hydrolysis
-
-
-
-
hydrolysis
-
-
SYSTEMATIC NAME
IUBMB Comments
beta-lactam hydrolase
A group of enzymes of varying specificity hydrolysing beta-lactams; some act more rapidly on penicillins, some more rapidly on cephalosporins. The latter were formerly listed as EC 3.5.2.8, cephalosporinase.
CAS REGISTRY NUMBER
COMMENTARY hide
9073-60-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
faropenem + H2O
(2R)-2-[(1S,2R)-1-carboxy-2-hydroxypropyl]-5-[(2R)-tetrahydrofuran-2-yl]-2,3-dihydro-1,3-thiazole-4-carboxylic acid
show the reaction diagram
-
-
-
?
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
temocillin + H2O
(2R,4S)-2-[(S)-carboxy[[carboxy(thiophen-3-yl)acetyl]amino]methoxymethyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
-
-
-
?
a beta-lactam + H2O
a substituted beta-amino acid
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
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
show the reaction diagram
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
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
show the reaction diagram
C7C422, S5ZIP8, T2A6Y2
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
cefepime + H2O
?
show the reaction diagram
-
-
-
?
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
C7C422, S5ZIP8, T2A6Y2
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
C7C422, S5ZIP8, T2A6Y2
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
show the reaction diagram
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
show the reaction diagram
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
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
show the reaction diagram
-
-
-
?
cephalothin + H2O
?
show the reaction diagram
-
-
-
?
cephalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
-
-
-
?
clavulanic acid + H2O
(2R,4R,5Z)-2-(carboxymethyl)-5-(2-hydroxyethylidene)-1,3-oxazolidine-4-carboxylic acid
show the reaction diagram
-
-
-
?
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
show the reaction diagram
C7C422, S5ZIP8, T2A6Y2
-
-
-
?
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
show the reaction diagram
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([2-[(iminomethyl)amino]ethyl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
show the reaction diagram
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
show the reaction diagram
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
show the reaction diagram
moxalactam + H2O
?
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
C7C422, S5ZIP8, T2A6Y2
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
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
show the reaction diagram
sulbactam + H2O
(2R,4S)-2-(carboxymethyl)-5,5-dimethyl-1,1-dioxo-1lambda~6~,3-thiazolidine-4-carboxylic acid
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
a beta-lactam + H2O
a substituted beta-amino acid
show the reaction diagram
-
-
-
-
?
cefepime + H2O
?
show the reaction diagram
Q51578
-
-
-
?
cephalothin + H2O
?
show the reaction diagram
Q51578
-
-
-
?
moxalactam + H2O
?
show the reaction diagram
Q51578
-
-
-
?
additional information
?
-
Q51578
the enzyme hydrolyzes penicillins, cephalothin, and the expanded-spectrum cephalosporins cefepime and moxalactam
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-(7-(4-methoxyphenyl)-5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidin-4-ylidene)-malononitrile
-
-
4,7-dichlorobenzothien-2-yl-sulfonylaminomethylboronic acid
-
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
-
-
4-chloro-7-(4-methylphenyl)-5-phenyl-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
-
ceftazidime
-
acts as a very weak simple noncompetitive inhibitor
clavulanic acid
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
-
-
Sulbactam
tazobactam
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
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.395
ampicillin
pH 7.0, 30°C
0.195
Cephalothin
pH 7.0, 30°C
0.1
ertapenem
pH 7.0, 30°C
0.013
faropenem
pH 7.0, 30°C
0.013
Imipenem
pH 7.0, 30°C
0.011
meropenem
pH 7.0, 30°C
0.12
nitrocefin
pH 7.0, 30°C
0.095
Oxacillin
pH 7.0, 30°C
0.014
panipenem
pH 7.0, 30°C
0.045
temocillin
pH 7.0, 30°C
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
0.01
amoxicillin
-
0.001 - 0.11
ampicillin
0.005 - 0.13
aztreonam
0.06 - 0.37
benzylpenicillin
0.06
cefalothin
-
0.029
cefalotin
C7C422, S5ZIP8, T2A6Y2
pH 7.2, 25°C, recombinant enzyme
0.026 - 0.149
cefepime
0.021 - 0.341
cefotaxime
0.043 - 0.65
cefoxitin
0.394
ceftaxidime
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
0.058 - 3.3
ceftazidime
0.023 - 0.3
cefuroxime
0.506
Cephaloridine
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
0.009 - 0.577
Cephalothin
0.01
cephalotin
pH 7.0, 30°C
0.119
doripenem
C7C422, S5ZIP8, T2A6Y2
pH 7.2, 25°C, recombinant enzyme
0.0042 - 0.094
Imipenem
0.057
meropenem
C7C422, S5ZIP8, T2A6Y2
pH 7.2, 25°C, recombinant enzyme
0.005 - 0.011
nitrocefin
0.005 - 0.28
penicillin G
0.003 - 0.454
piperacillin
0.006
ticarcillin
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
955
ampicillin
pH 7.0, 30°C
44
Cephalothin
pH 7.0, 30°C
0.13
ertapenem
pH 7.0, 30°C
0.038
faropenem
pH 7.0, 30°C
4.8
Imipenem
pH 7.0, 30°C
0.07
meropenem
pH 7.0, 30°C
940
nitrocefin
pH 7.0, 30°C
130
Oxacillin
pH 7.0, 30°C
1.4
panipenem
pH 7.0, 30°C
0.3
temocillin
pH 7.0, 30°C
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
5 - 447
ampicillin
0.1 - 100
aztreonam
317 - 420
benzylpenicillin
75
cefalotin
C7C422, S5ZIP8, T2A6Y2
pH 7.2, 25°C, recombinant enzyme
3 - 30
cefepime
2.9 - 120
cefotaxime
9.6 - 10
cefoxitin
0.3
ceftaxidime
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
0.015 - 24
ceftazidime
2 - 21
cefuroxime
190
Cephaloridine
at 30°C in 100 mM sodium phosphate buffer, pH 7.0
38 - 530
Cephalothin
1
cephalotin
pH 7.0, 30°C
226
doripenem
C7C422, S5ZIP8, T2A6Y2
pH 7.2, 25°C, recombinant enzyme
0.028 - 600
Imipenem
301
meropenem
C7C422, S5ZIP8, T2A6Y2
pH 7.2, 25°C, recombinant enzyme
65 - 72
nitrocefin
23 - 34
penicillin G
4 - 27
piperacillin
8 - 84
ticarcillin
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2400
ampicillin
pH 7.0, 30°C
1.1
cefepime
pH 7.0, 30°C
10
cefotaxime
pH 7.0, 30°C
0.26
cefoxitin
pH 7.0, 30°C
230
Cephalothin
pH 7.0, 30°C
1.3
ertapenem
pH 7.0, 30°C
2.9
faropenem
pH 7.0, 30°C
370
Imipenem
pH 7.0, 30°C
6.2
meropenem
pH 7.0, 30°C
7700
nitrocefin
pH 7.0, 30°C
1400
Oxacillin
pH 7.0, 30°C
100
panipenem
pH 7.0, 30°C
6.6
temocillin
pH 7.0, 30°C
4100 - 4200
ampicillin
1200
aztreonam
pH 7.0, 30°C
2600
cefalotin
C7C422, S5ZIP8, T2A6Y2
pH 7.2, 25°C, recombinant enzyme
1300
cefepime
pH 7.0, 30°C
1200
cefotaxime
pH 7.0, 30°C
230
cefoxitin
C7C422, S5ZIP8, T2A6Y2
pH 7.2, 25°C, recombinant enzyme
230 - 1800
ceftazidime
6700
cefuroxime
pH 7.0, 30°C
7900
cephalotin
pH 7.0, 30°C
1900
doripenem
C7C422, S5ZIP8, T2A6Y2
pH 7.2, 25°C, recombinant enzyme
7600
Imipenem
C7C422, S5ZIP8, T2A6Y2
pH 7.2, 25°C, recombinant enzyme
5200
meropenem
C7C422, S5ZIP8, T2A6Y2
pH 7.2, 25°C, recombinant enzyme
1400 - 5900
nitrocefin
3300
piperacillin
pH 7.0, 30°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
-
0.03
clavulanic acid
pH 7.0, 30°C
0.0806
Imipenem
-
at 40?C in 50 mM HEPES buffer (pH 6.8)
0.0042
meropenem
-
at 40?C in 50 mM HEPES buffer (pH 6.8)
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
0.023
Sulbactam
pH 7.0, 30°C
0.022
tazobactam
pH 7.0, 30°C
0.0438
ZINC01807204
pH 7.0, 30°C
additional information
additional information
-
Ki for diverse mutants of beta-lactamase inhibitor protein BLIP, overview
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00057
4,7-dichlorobenzothien-2-yl-sulfonylaminomethylboronic acid
Klebsiella pneumoniae
P0A3M1
pH not specified in the publication, temperature not specified in the publication
0.00002 - 0.137
clavulanic acid
0.106
Sulbactam
Klebsiella pneumoniae
G3GCC6
pH 7.0, 30°C
0.099
tazobactam
Klebsiella pneumoniae
G3GCC6
pH 7.0, 30°C
0.2
ZINC01807204
Klebsiella pneumoniae
G3GCC6
pH 7.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
C7C422, S5ZIP8, T2A6Y2
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
isoelectric focusing, beta-lactamases CTX-M-26, pH-range 3.5-9.5
ORGANISM
COMMENTARY hide
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
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
C7C422, S5ZIP8, T2A6Y2
New Delhi MBL (NDM)-1 is a clinically significant metallo beta-lactamase
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
Q6XEC0_KLEPN
265
0
30359
TrEMBL
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
x * 29000, beta-lactamases CTX-M-26, SDS-PAGE
38000
-
x * 38000, CMY-10, SDS-PAGE; x * 38000, CMY-1, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
three-dimensional structure, overview
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 hide
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
E152K
C7C422, S5ZIP8, T2A6Y2
naturally occuring genetic variation
E166A
-
SHV deacylation deficient enzyme
G69S/A74T/G200R
C7C422, S5ZIP8, T2A6Y2
naturally occuring genetic variation
S130G
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
59.5
C7C422, S5ZIP8, T2A6Y2
melting temperature of the purified NDM-1 variant
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
beta-lactamases CTX-M-26
CMY-1; CMY-10
-
Ni-NTA column chromatography
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
C7C422, S5ZIP8, T2A6Y2
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
beta-lactamases CTX-M-26
expressed in Escherichia coli BL21 (DE3) cells
expressed in Escherichia coli BL21 cells
-
expression in Escherichia coli
expression of CMY-10 in Escherichia coli; expression of CMY-1 in Escherichia coli
-
expression of wild-type and mutants in Escherichia coli DH10B
-
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)
C7C422, S5ZIP8, T2A6Y2
gene blaNDM-10, genotyping, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
C7C422, S5ZIP8, T2A6Y2
gene blaNDM-9, genotyping, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
C7C422, S5ZIP8, T2A6Y2
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 hide
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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, Escherichia coli (P62593), Klebsiella pneumoniae (P0AD64), Serratia marcescens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Escherichia coli, Escherichia coli (Q8KSA6), Klebsiella pneumoniae, Klebsiella pneumoniae (Q8GD10)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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, Klebsiella pneumoniae (Q09HD0), Klebsiella pneumoniae CHAK36 (Q09HD0)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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, Klebsiella pneumoniae (Q4TVR4)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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, Klebsiella pneumoniae (Q8KQ59)
Manually annotated by BRENDA team
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
Acinetobacter baumannii, Acinetobacter baumannii (Q8RLA6), Klebsiella pneumoniae (P0A3M1), Pseudomonas aeruginosa (Q6LBN9)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Acinetobacter baumannii (F2YZ26), 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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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