Information on EC 6.3.1.17 - beta-citrylglutamate synthase

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The expected taxonomic range for this enzyme is: Mus musculus

EC NUMBER
COMMENTARY hide
6.3.1.17
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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 + beta-citryl-L-glutamate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Alanine, aspartate and glutamate metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
citrate:L-glutamate ligase |ADP-forming||
The enzyme, found in animals, also has the activity of EC 6.3.2.41, N-acetylaspartylglutamate synthase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
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
ADP + phosphate + beta-citryl-L-glutamate
ATP + citrate + L-glutamate
show the reaction diagram
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isoform GCP3 acts preferentially on beta-citryl-L-glutamate in the presence of Ca2+. Its activity on this substrate is lower in the presence of Mn2+ and completely cancelled in the presence of Zn2+
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-
?
ADP + phosphate + N-acetyl-aspartylglutamate
?
show the reaction diagram
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in the presence of Ca2+, the purified enzyme specifically hydrolyzes beta-citrylglutamate and does not act on N-acetyl-aspartylglutamate. However, both compounds were hydrolyzed in the presence of Mn2+
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-
?
ATP + citrate + L-glutamate
ADP + phosphate + beta-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
ADP + phosphate + beta-citryl-L-glutamate
ATP + citrate + L-glutamate
show the reaction diagram
-
isoform GCP3 acts preferentially on beta-citryl-L-glutamate in the presence of Ca2+. Its activity on this substrate is lower in the presence of Mn2+ and completely cancelled in the presence of Zn2+
-
-
?
ADP + phosphate + N-acetyl-aspartylglutamate
?
show the reaction diagram
-
in the presence of Ca2+, the purified enzyme specifically hydrolyzes beta-citrylglutamate and does not act on N-acetyl-aspartylglutamate. However, both compounds were hydrolyzed in the presence of Mn2+
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-
?
ATP + citrate + L-glutamate
ADP + phosphate + beta-citryl-L-glutamate
show the reaction diagram
Q80WS1
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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beta-citryl-L-glutamate is the preferred substrate in the presence of Ca2+
Mg2+
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Mg2+ stimulates very poorly the activity of the enzyme
Mn2+
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The N-acetyl-aspartylglutamate hydrolase activity of the enzyme is stimulated by Mn2+, but not by Ca2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
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stimulates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0096
ATP
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pH 8.0, 30°C
0.0035
beta-Citryl-L-glutamate
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in 25 mM HEPES, pH 7.1, at 30°C
1.24
citrate
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pH 8.0, 30°C
0.73
L-glutamate
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pH 8.0, 30°C
0.0076
N-acetyl-aspartylglutamate
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in 25 mM HEPES, pH 7.1, at 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5
L-glutamate
Mus musculus
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pH 8.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.7
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pH 8.0, 30°C, formation of beta-citryl-L-glutamate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
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x * 42000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 42000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose column chromatography, ConA-Sepharose column chromatography, and Superdex S-200 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in bacteria or HEK293T cells
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