Information on EC 6.3.3.4 - (carboxyethyl)arginine beta-lactam-synthase

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The expected taxonomic range for this enzyme is: Streptomyces clavuligerus

EC NUMBER
COMMENTARY hide
6.3.3.4
-
RECOMMENDED NAME
GeneOntology No.
(carboxyethyl)arginine beta-lactam-synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-N2-(2-carboxyethyl)arginine = AMP + diphosphate + deoxyamidinoproclavaminate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cyclization
-
-
-
-
formation of cyclic amides
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
clavulanate biosynthesis
-
-
Clavulanic acid biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
L-N2-(2-carboxyethyl)arginine cyclo-ligase (AMP-forming)
Forms part of the pathway for the biosythesis of the beta-lactamase inhibitor clavulanate in Streptomyces clavuligerus. It has been proposed [3] that L-N2-(2-carboxyethyl)arginine is first converted into an acyl-AMP by reaction with ATP and loss of diphosphate, and that the beta-lactam ring is then formed by the intramolecular attack of the beta-nitrogen on the activated carboxy group.
CAS REGISTRY NUMBER
COMMENTARY hide
68247-54-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + (2'R)-methyl-L-N2-(2-carboxyethyl)arginine
?
show the reaction diagram
-
-
-
-
?
ATP + (2'S)-ethyl-L-N2-(2-carboxyethyl)arginine
?
show the reaction diagram
-
-
-
-
?
ATP + (2'S)-methyl-L-N2-(2-carboxyethyl)arginine
?
show the reaction diagram
-
-
-
-
?
ATP + L-N2-(2-carboxyethyl)arginine
AMP + diphosphate + deoxyamidinoproclavaminate
show the reaction diagram
-
-
-
-
?
N2-(carboxyethyl)-L-arginine + ATP
AMP + diphosphate + deoxyamidinoproclavaminate
show the reaction diagram
additional information
?
-
-
no activity with (2'R)-ethyl-L-N2-(2-carboxyethyl)arginine
-
-
-
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
ATP + L-N2-(2-carboxyethyl)arginine
AMP + diphosphate + deoxyamidinoproclavaminate
show the reaction diagram
-
-
-
-
?
N2-(carboxyethyl)-L-arginine + ATP
AMP + diphosphate + deoxyamidinoproclavaminate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
deoxyamidinoproclavaminate
-
product inhibition
diphosphate
-
product inhibition
N2-(carboxymethyl)-L-arginine
-
competitive to N2-(carboxyethyl)-L-arginine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04 - 1.9
(2'R)-methyl-L-N2-(2-carboxyethyl)arginine
0.04 - 0.06
(2'S)-ethyl-L-N2-(2-carboxyethyl)arginine
0.06 - 1.2
(2'S)-methyl-L-N2-(2-carboxyethyl)arginine
0.153
ATP
-
pH 7.5
0.037 - 1
L-N2-(2-carboxyethyl)arginine
0.22
N2-(carboxyethyl)-L-arginine
-
pH 7.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.014 - 0.07
(2'R)-methyl-L-N2-(2-carboxyethyl)arginine
0.0023 - 0.004
(2'S)-ethyl-L-N2-(2-carboxyethyl)arginine
0.013 - 0.34
(2'S)-methyl-L-N2-(2-carboxyethyl)arginine
0.016 - 0.87
L-N2-(2-carboxyethyl)arginine
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54500
-
x * 54500, deduced from gene sequence
56000
-
x * 56000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM Tris-HCl, 10% glycerol, 2 mM dithiothreitol, 0.01 mM EDTA, pH 7.5, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant protein expressed in E. coli
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
homologous to Class B asparagine synthases
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H447A
-
the mutant shows severely reduced turnover number compared to the wild type enzyme
V446A
-
the mutant shows reduced turnover number compared to the wild type enzyme
V446G
-
the mutant shows strongly reduced turnover number compared to the wild type enzyme
additional information
-
disruption mutant, complete loss of clavulanic acid production, accumulation of N2-(carboxyethyl)-L-arginine, but no effect on synthesis of penicillin or cephamycin