Information on EC 6.3.2.B11 - beta-citrylglutamate synthase

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The expected taxonomic range for this enzyme is: Mus musculus

EC NUMBER
COMMENTARY hide
6.3.2.B11
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
beta-citrylglutamate synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + citrate + L-glutamate = ADP + phosphate + N-citryl-L-glutamate
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
citrate:L-glutamate ligase (ADP-forming)
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is involved in the biosynthesis of the dipeptide N-citryl-L-glutamate, an abundant neuropeptide in the mammalian brain
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + citrate + L-glutamate
ADP + phosphate + N-citryl-L-glutamate
show the reaction diagram
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 + citrate + L-glutamate
ADP + phosphate + N-citryl-L-glutamate
show the reaction diagram
Q80WS1
the enzyme is involved in the biosynthesis of the dipeptide N-citryl-L-glutamate, an abundant neuropeptide in the immature mammalian brain and in the testis
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?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0096
ATP
pH 8.0, 30°C
1.24
citrate
pH 8.0, 30°C
0.73
L-glutamate
pH 8.0, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Mus musculus
Q80WS1
from the Vmax, kcat values of 3 and 1.5/s are calculated for the beta-citrylglutamate synthase activity and and N-acetylaspartyl-glutamate synthase activity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
synthesis of N-citryl-L-glutamate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9
pH 7.5: about 40% of maximal activity, pH 9.0: about 95% of maximal activity, synthesis of N-citryl-L-glutamate
additional information
the rates for beta-citrylglutamate synthesis and N-acetylaspartyl-glutamate synthesis are similar between pH 7 and 8, but the beta-citrylglutamate synthetase is severalfold higher than the N-acetylaspartyl-glutamate synthetase activity at more alkaline pH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
gel filtration
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
produced it in Escherichia coli either unmodified or as a fusion protein with a poly-His tag at the C terminus. Extracts of cells expressing these recombinant proteins display N-acetylaspartylglutamate synthase activity