Information on EC 3.5.2.B3 - (-)-gamma-lactamase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.5.2.B3
-
RECOMMENDED NAME
GeneOntology No.
(-)-gamma-lactamase
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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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
additionally acts as amidase, EC 3.5.1.4
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1R,4S)-2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(1S,4R)-4-aminocyclopent-2-ene-1-carbaldehyde
show the reaction diagram
additional information
?
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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
(1R,4S)-2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
(1S,4R)-4-aminocyclopent-2-ene-1-carbaldehyde
show the reaction diagram
Q8GJP7
-
-
-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
1 mM, 130% of initial activity
EDTA
1 mM, 110% of initial activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31300
2 * 31300, calculated, 2 * 33000, SDS-PAGE
33000
2 * 31300, calculated, 2 * 33000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 31300, calculated, 2 * 33000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the catalytic triad of the (-)-gamma-lactamase is comprised of residues Ser98, Asp230, and His259 and an oxyanion hole is formed by Tyr32 and Met99 according to the alignment results
to 1.73 A resolution, cubic space group F23 with unit cell parameters a=b=c=240.6 A. The trimeric enzyme has an alpha/beta hydrolase fold and closely resembles the cofactor free haloperoxidases
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli