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Information on EC 6.3.2.41 - N-acetylaspartylglutamate synthase and Organism(s) Mus musculus and UniProt Accession Q80WS1

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IUBMB Comments
The enzyme, found in animals, produces the neurotransmitter N-acetyl-L-aspartyl-L-glutamate. One isoform also has the activity of EC 6.3.1.17, beta-citrylglutamate synthase , while another isoform has the activity of EC 6.3.2.42, N-acetylaspartylglutamylglutamate 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
naag synthetase, rimkla, naags-ii, naags, n-acetylaspartylglutamate synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N-acetylaspartylglutamate synthetase
-
NAAG synthetase
-
RIMKLB
gene name, ambiguous
N-acetylaspartylglutamate synthetase
N-acetylaspartylglutamate synthetase II
-
-
NAAG synthetase
NAAGS
NAAGS-II
-
-
RIMKLA
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
N-acetyl-L-aspartate:L-glutamate ligase (ADP, N-acetyl-L-aspartyl-L-glutamate-forming)
The enzyme, found in animals, produces the neurotransmitter N-acetyl-L-aspartyl-L-glutamate. One isoform also has the activity of EC 6.3.1.17, beta-citrylglutamate synthase [2], while another isoform has the activity of EC 6.3.2.42, N-acetylaspartylglutamylglutamate synthase [3].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + N-acetyl-L-aspartate + L-glutamate
ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate
show the reaction diagram
ATP + N-acetyl-L-aspartate + citrate
?
show the reaction diagram
-
-
-
?
ATP + N-acetyl-L-aspartate + L-glutamate
ADP + phosphate + N-acetyl-L-aspartyl-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 + N-acetyl-L-aspartate + L-glutamate
ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-L-aspartate + L-glutamate
ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
stimulates
dithiothreitol
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0096
ATP
pH 8.0, 30°C
0.73
L-glutamate
pH 8.0, 30°C
4.59
N-acetyl-L-aspartate
pH 8.0, 30°C
0.065
ATP
0.87
citrate
at pH 8.0 and 37°C
0.88
L-glutamate
1.48
N-acetyl-L-aspartate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3
N-acetyl-L-aspartate
pH 8.0, 30°C
2.6
N-acetyl-L-aspartate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.4
pH 8.0, 30°C, formation of N-acetyl-L-aspartyl-L-glutamate
1.09
pH 8.0, 30°C, formation of N-acetyl-L-aspartyl-L-glutamate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
very low expression
Manually annotated by BRENDA team
-
very low expression
Manually annotated by BRENDA team
-
very low expression
Manually annotated by BRENDA team
additional information
-
the enzyme is undetectable in liver
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
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
42000
-
x * 42000, SDS-PAGE
43000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 42000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose column chromatography, Q-Sepharose column chromatography, and S-200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in bacteria or HEK293T cells
expressed as FLAG epitope-tagged protein in HEK-293T and CHO-K1 cells
-
expressed in CHO-K1 and HEK-293T cells
-
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3)pLysS cells and in HEK-293T 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 (Q6PFX8), Mus musculus (Q80WS1)
Manually annotated by BRENDA team
Lodder-Gadaczek, J.; Becker, I.; Gieselmann, V.; Wang-Eckhardt, L.; Eckhardt, M.
N-Acetylaspartylglutamate synthetase II synthesizes N-acetylaspartylglutamylglutamate
J. Biol. Chem.
286
16693-16706
2011
Mus musculus
Manually annotated by BRENDA team
Becker, I.; Lodder, J.; Gieselmann, V.; Eckhardt, M.
Molecular characterization of N-acetylaspartylglutamate synthetase
J. Biol. Chem.
285
29156-29164
2010
Mus musculus
Manually annotated by BRENDA team