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Information on EC 6.3.1.17 - beta-citrylglutamate synthase and Organism(s) Mus musculus and UniProt Accession Q80WS1

for references in articles please use BRENDA:EC6.3.1.17
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IUBMB Comments
The enzyme, found in animals, also has the activity of EC 6.3.2.41, N-acetylaspartylglutamate synthase.
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This record set is specific for:
Mus musculus
UNIPROT: Q80WS1
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The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
rimklb, naags-i, naag synthetase i, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NAAG synthetase I
-
RIMKLB
PATHWAY SOURCE
PATHWAYS
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.
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
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+
-
-
?
ATP + citrate + L-glutamate
ADP + phosphate + beta-citryl-L-glutamate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL 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
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+
-
-
?
ATP + citrate + L-glutamate
ADP + phosphate + beta-citryl-L-glutamate
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
beta-citryl-L-glutamate is the preferred substrate in the presence of Ca2+
Mg2+
Mg2+ stimulates very poorly the activity of the enzyme
Mn2+
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
stimulates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0096
ATP
pH 8.0, 30°C
0.0035
beta-Citryl-L-glutamate
in 25 mM HEPES, pH 7.1, at 30°C
1.24
citrate
pH 8.0, 30°C
0.73
L-glutamate
pH 8.0, 30°C
0.0076
N-acetyl-aspartylglutamate
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
pH 8.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.7
pH 8.0, 30°C, formation of beta-citryl-L-glutamate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RIMKB_MOUSE
387
0
42528
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
x * 42000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 42000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose column chromatography, ConA-Sepharose column chromatography, and Superdex S-200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in bacteria or HEK293T cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Collard, F.; Stroobant, V.; Lamosa, P.; Kapanda, C.N.; Lambert, D.M.; Muccioli, G.G.; Poupaert, J.H.; Opperdoes, F.; van Schaftingen, E.
Molecular identification of N-acetylaspartylglutamate synthase and beta-citrylglutamate synthase
J. Biol. Chem.
285
29826-29833
2010
Mus musculus (Q80WS1)
Manually annotated by BRENDA team
Collard, F.; Vertommen, D.; Constantinescu, S.; Buts, L.; Van Schaftingen, E.
Molecular identification of beta-citrylglutamate hydrolase as glutamate carboxypeptidase 3
J. Biol. Chem.
286
38220-38230
2011
Mus musculus (Q80WS1), Mus musculus
Manually annotated by BRENDA team