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Information on EC 6.3.2.B11 - beta-citrylglutamate synthase and Organism(s) Mus musculus and UniProt Accession Q80WS1

for references in articles please use BRENDA:EC6.3.2.B11
preliminary BRENDA-supplied EC number
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This record set is specific for:
Mus musculus
UNIPROT: Q80WS1 not found.
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The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Mus musculus
Synonyms
N-acetylaspartylglutamate synthase, NAAG synthetase B, NAAGS B, RIMKLB, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N-acetylaspartylglutamate synthase
ambiguous
NAAG synthetase B
-
SYSTEMATIC NAME
IUBMB Comments
citrate:L-glutamate ligase (ADP-forming)
-
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 SUBSTRATE
NATURAL 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
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
-
-
?
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
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
-
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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
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
-
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
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