Information on EC 3.5.2.B2 - (+)-gamma-lactamase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.5.2.B2
-
RECOMMENDED NAME
GeneOntology No.
(+)-gamma-lactamase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a (+)-gamma-lactam + H2O = a substituted gamma-amino acid
show the reaction diagram
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-
-
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SYSTEMATIC NAME
IUBMB Comments
(+)-gamma-lactam hydrolase
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
additionally acts as isochorismatase, EC 3.3.2.1, and amidase, EC 3.5.1.4
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1S,4R)-2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(1R,4S)-4-aminocyclopent-2-ene-1-carbaldehyde
show the reaction diagram
(3S,4R)-cis-3-(acetyloxy)-4-phenyl-2-azetidinone + H2O
?
show the reaction diagram
1,3-benzoxazol-2(3H)-one + H2O
2-aminophenol + CO2
show the reaction diagram
6-methoxy-1,3-benzoxazol-2(3H)-one + H2O
2-amino-5-methoxyphenol + CO2
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(1S,4R)-2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(1R,4S)-4-aminocyclopent-2-ene-1-carbaldehyde
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ni2+
1 mM, 110% of initial activity
Zn2+
1 mM, 170% of initial activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.378
(1S,4R)-2-azabicyclo[2.2.1]hept-5-en-3-one
pH 9.0, 30°C
0.19
1,3-benzoxazol-2(3H)-one
pH 7.0, temperature not specified in the publication
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.2
1,3-benzoxazol-2(3H)-one
Fusarium pseudograminearum
K3VFR8
pH 7.0, temperature not specified in the publication
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22
1,3-benzoxazol-2(3H)-one
Fusarium pseudograminearum
K3VFR8
pH 7.0, temperature not specified in the publication
210620
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
60% of maximum activity
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
rapid loss of activity above
80 - 100
more than 60% of maximum activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19700
2 * 19700, calculated, 2 * 20000, SDS-PAGE
20000
2 * 19700, calculated, 2 * 20000, SDS-PAGE
35000
x * 35000, SDS-PAGE
47000
-
x * 47000, SDS-PAGE
49000
1 * 49000, calculated
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 19700, calculated, 2 * 20000, SDS-PAGE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
molecular modeling. Structure does not show similartity to the domain structure of known gamma-lactamases, leading to gamma lactamase type II
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homology modeling and molecular docking. The active site is located in the middle of the core structure, the catalytic triad is constituted by residues S171, S195, C145
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
stable within
735762
6 - 10
stable within
735550
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
30 min, 38% residual activity
100
-
12 h, no loss of activity
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
increased expression upon treatment with benzoxazolin-2-one
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C145A
mutation in catalytic triad, complete loss of activity
S171A
mutation in catalytic triad, complete loss of activity
S195A
mutation in catalytic triad, complete loss of activity
C145A
-
mutation in catalytic triad, complete loss of activity
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S171A
-
mutation in catalytic triad, complete loss of activity
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S195A
-
mutation in catalytic triad, complete loss of activity
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C118A
complete loss of activity
D9A
complete loss of activity
H51A
complete loss of activity
K84A
9% decrease in activity compared to wild-type
Q11A
20% decrease in activity compared to wild-type
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis