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Information on EC 3.5.2.6 - beta-lactamase and Organism(s) Aeromonas hydrophila and UniProt Accession P26918

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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:
Aeromonas hydrophila
UNIPROT: P26918
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Word Map
The taxonomic range for the selected organisms is: Aeromonas hydrophila
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carbapenemase CphA
-
metallo-beta-lactamase
-
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
-
-
-
-
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
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
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
-
-
-
?
biapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[(6,7-dihydro-5H-pyrazolo[1,2-a][1,2,4]triazol-4-ium-6-yl)sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylate
show the reaction diagram
carbapenem + H2O
[(2R)-2,3-dihydro-1H-pyrrol-2-yl]acetic acid
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
-
-
-
?
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
-
-
-
?
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
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
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zinc
enzyme contains one zinc ion
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-picolinic acid
competitive inhibitor, 8% residual activity at 0.1 mM
EDTA
inactivation of CphA wild-type and the H118A, H196A, H263A and D120A mutants by EDTA is studied in 15 mM sodium cacodylate (pH 6.5) at 30°C in the presence of different concentrations of EDTA
pyridine-2,4-dicarboxylic acid
competitive inhibitor, 38% residual activity at 0.1 mM
pyridine-2,6-dicarboxylic acid
12% residual activity at 0.1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridine-2,3-dicarboxylic acid
30% increase of activity at 0.1 mM
pyridine-2,5-dicarboxylic acid
14% increase of activity at 0.1 mM
pyridine-3,4-dicarboxylic acid
16% increase of activity at 0.1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15 - 5
benzylpenicillin
0.1 - 1.5
biapenem
0.05 - 0.7
cefotaxime
0.053 - 6
cephaloridine
0.05 - 4.3
Imipenem
0.004 - 2
nitrocefin
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004 - 3.3
benzylpenicillin
0.0015 - 1000
biapenem
0.0002 - 0.3
cefotaxime
0.006 - 0.9
cephaloridine
0.02 - 1770
Imipenem
0.0002 - 0.7
nitrocefin
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0057 - 0.013
2-picolinic acid
0.0045 - 0.028
pyridine-2,4-dicarboxylic acid
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?
BLAB_AERHY
254
0
28016
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25120
25130
25150
25160
25180
25190
25200
25210
D120A mutant, native, measured mass
25220
25240
D120T mutant, native, measured mass
25250
25270
V67I mutant, native, measured mass
25810
V67LFKHV mutant, denatured, measured mass
25880
V67LFKHV mutant, native, measured mass, 1 Zn2+-ion
25900
V67LFKHV mutant, denatured, calculated mass
25940
V67LFKHV mutant, native, measured mass, 2 Zn2+-ions
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of wild-type enzyme mutant enzyme N220G, and of the complex of wild-type enzyme with biapenem
hanging drop vapour diffusion method with 30% (w/v) polyethylene glycol 8000, 0.6 M ammonium sulfate, and 100 mM Na-citrate, pH 6.5
hanging-drop vapor-diffusion method, crystals exhibit orthorhombic symmetry P2(1)2(1)2(1), with unit-cell parameters a = 40.75, b = 42.05, c = 128.88 A. There is one monomer in the asymmetric unit
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D120A
site-directed mutant of CphA, generated and characterized
D120T
site-directed mutant of CphA, generated and characterized
H118A
site-directed mutant of CphA, generated and characterized, H118A and H196A mutations lead to a decrease of at least 1000fold in activity against carbapenems compared with the wild-type enzyme
H196A
site-directed mutant of CphA, generated and characterized, H118A and H196A mutations lead to a decrease of at least 1000fold in activity against carbapenems compared with the wild-type enzyme
H263A
site-directed mutant of CphA, generated and characterized
K224Q
site-directed mutant of CphA, generated and characterized
K226Q
site-directed mutant of CphA, generated and characterized
N116H/N220G
N116H/N220G/K224Q
site-directed mutant of CphA, generated and characterized
N220G
kinetic parameters of the wild-type and N220G mutant enzymes are not significantly different
T157A
site-directed mutant of CphA, generated and characterized
V67A
site-directed mutant of CphA, generated and characterized
V67D
site-directed mutant of CphA, generated and characterized
V67I
site-directed mutant of CphA, generated and characterized
V67LFKHV
site-directed mutant of CphA, generated and characterized
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sharma, N.; Toney, J.H.; Fitzgerald, P.M.
Expression, purification, crystallization and preliminary X-ray analysis of Aeromonas hydrophilia metallo-beta-lactamase
Acta Crystallogr. Sect. F
61
180-182
2005
Aeromonas hydrophila
Manually annotated by BRENDA team
Garau, G.; Bebrone, C.; Anne, C.; Galleni, M.; Frere, J.M.; Dideberg, O.
A metallo-beta-lactamase enzyme in action: crystal structures of the monozinc carbapenemase CphA and its complex with biapenem
J. Mol. Biol.
345
785-795
2005
Aeromonas hydrophila (P26918), Aeromonas hydrophila
Manually annotated by BRENDA team
Horsfall, L.E.; Garau, G.; Lienard, B.M.; Dideberg, O.; Schofield, C.J.; Frere, J.M.; Galleni, M.
Competitive inhibitors of the CphA metallo-beta-lactamase from Aeromonas hydrophila
Antimicrob. Agents Chemother.
51
2136-2142
2007
Aeromonas hydrophila (P26918), Aeromonas hydrophila
Manually annotated by BRENDA team
Bebrone, C.; Anne, C.; Kerff, F.; Garau, G.; De Vriendt, K.; Lantin, R.; Devreese, B.; Van Beeumen, J.; Dideberg, O.; Frere, J.; Galleni, M.
Mutational analysis of the zinc- and substrate-binding sites in the CphA metallo-beta -lactamase from Aeromonas hydrophila
Biochem. J.
414
151-159
2008
Aeromonas hydrophila (P26918), Aeromonas hydrophila
Manually annotated by BRENDA team