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Information on EC 3.5.2.6 - beta-lactamase

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.2 In cyclic amides
                3.5.2.6 beta-lactamase
IUBMB Comments
A group of enzymes of varying specificity hydrolysing beta-lactams; some act more rapidly on penicillins, some more rapidly on cephalosporins. The latter were formerly listed as EC 3.5.2.8, cephalosporinase.
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This record set is specific for:
UNIPROT: Q9K2N0
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
beta-lactamase, carbapenemase, extended-spectrum beta-lactamase, ndm-1, penicillinase, tem-1, blandm-1, ges-1, blactx-m-15, kpc-2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carbapenem-hydrolysing MBL
-
metallo-beta-L-lactamase
-
metallo-beta-lactamase
-
Verona integron-encoded MBL
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Verona integron-encoded MBL-2
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Zn-beta-lactamase
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Beta lactamase OXA-10
-
-
-
-
beta-lactamase
-
-
-
-
beta-lactamase AME I
-
-
-
-
beta-lactamase II
-
-
-
-
BLAIMP
-
-
-
-
carbapenemase
-
-
-
-
Carbenicillinase
-
-
-
-
cefotaximase
-
-
-
-
ceftazidimase
-
-
-
-
cefurooximase
-
-
-
-
Cefuroximase
-
-
-
-
Cephalosporinase
-
-
-
-
Imipenem-cefoxitin hydrolyzing enzyme
-
-
-
-
imipenemase
-
-
-
-
metallo-beta-lactamase
-
-
-
-
neutrapen
-
-
-
-
Oxacillinase
-
-
-
-
penicillinase
-
-
-
-
SHV-2A
-
-
-
-
additional information
VIM-2 belongs to the B1 subfamily ofMBLs
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a beta-lactam + H2O = a substituted beta-amino acid
show the reaction diagram
VIM-2 catalytic Cys221, located in the Cys site, shows a high tendency to be strongly oxidized becoming a cysteinesulfonic residue, active site structure, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amide 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
carbapenem + H2O
[(2R)-2,3-dihydro-1H-pyrrol-2-yl]acetic acid
show the reaction diagram
-
-
-
?
chromacef + H2O
(2S)-2-[(S)-carboxy(2-phenylacetamido)methyl]-5-[(E)-2-(4-nitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
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
-
-
-
?
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
-
-
-
?
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
carbapenem + H2O
[(2R)-2,3-dihydro-1H-pyrrol-2-yl]acetic acid
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
preparation of a Co(II)-substituted VIM-2 analogue, crystal structure analysis, overview
additional information
analysis of the metal content of enzyme VIM-2, metal binding kinetics, overview
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
pre-steady-state and steady-state kinetics, overview
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q9K2N0_PSEAI
266
0
28327
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29700
x * 29700, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 29700, SDS-PAGE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, sitting drop vapor diffusion method, mixxing of 0001 ml of 10 mg/mL VIM-2 protein with 0.001 ml of reservoir solution containing 0.2 M ammonium acetate, 0.1 mM zinc chloride, 0.1 M HEPES, pH 7.5, and 25% PEG 3350, X-ray diffraction tructure determination and analysis, molecular replacement
purified recombinant native and oxidized VIM-2, hanging drop vapour diffusion method, mixing 0.001 ml of 5.5 mg/ml of protein in 10 mM HEPES, pH 7.5, 0.2 M NaCl, and 1 mM DTT, with 0.001 ml of precipitant solution containing 30% PEG 8000, 0.2 M Na acetate, 0.1 M Na cacodylate/cacodylic acid, pH 6.5, and 0.01 mM ZnCl2, 20°C, 3-4 days, X-ray diffraction structure determination and analysis at 1.9-2.2 A resolution
X-ray data collection and structure refinement of the reduced and oxidised VIM-2
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant cobalt-cobtaining enzyme from Escherichia coli strain BL21(DE3) by cobalt affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene blaVIM-2, recombinant Co2+-enzyme expression in Escherichia coli strain BL21(DE3) in in minimal medium
overexpression of VIM-2 in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Quinteira, S.; Sousa, J.C.; Peixe, L.
Characterization of In100, a new integron carrying a metallo-{beta}-lactamase and a carbenicillinase, from Pseudomonas aeruginosa
Antimicrob. Agents Chemother.
49
451-453
2005
Pseudomonas aeruginosa (Q9K2N0), Pseudomonas aeruginosa
Manually annotated by BRENDA team
Garcia-Saez, I.; Docquier, J.D.; Rossolini, G.M.; Dideberg, O.
The three-dimensional structure of VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa in its reduced and oxidised form
J. Mol. Biol.
375
604-611
2008
Pseudomonas aeruginosa (Q9K2N0), Pseudomonas aeruginosa
Manually annotated by BRENDA team
Aitha, M.; Marts, A.R.; Bergstrom, A.; Moeller, A.J.; Moritz, L.; Turner, L.; Nix, J.C.; Bonomo, R.A.; Page, R.C.; Tierney, D.L.; Crowder, M.W.
Biochemical, mechanistic, and spectroscopic characterization of metallo-beta-lactamase VIM-2
Biochemistry
53
7321-7331
2014
Pseudomonas aeruginosa (Q9K2N0)
Manually annotated by BRENDA team