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Information on EC 6.3.2.41 - N-acetylaspartylglutamate synthase for references in articles please use BRENDA:EC6.3.2.41
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EC Tree
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 .
The enzyme appears in viruses and cellular organisms
Synonyms
N-acetylaspartylglutamate synthetase, N-acetylaspartylglutamate synthetase II, NAAG synthetase, NAAGS, NAAGS-II, RIMKLA, RIMKLB,
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N-acetylaspartylglutamate synthetase
N-acetylaspartylglutamate synthetase II
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RIMKLA
; gene name, ambiguous
RIMKLB
gene name, ambiguous
N-acetylaspartylglutamate synthetase
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N-acetylaspartylglutamate synthetase
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N-acetylaspartylglutamate synthetase
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NAAG synthetase
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NAAGS
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ATP + N-acetyl-L-aspartate + L-glutamate = ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate
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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].
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ATP + N-acetyl-L-aspartate + citrate
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ATP + N-acetyl-L-aspartate + L-glutamate
ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate
ATP + N-acetyl-L-aspartate + L-glutamate
ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate
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ATP + N-acetyl-L-aspartate + L-glutamate
ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate
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ATP + N-acetyl-L-aspartate + L-glutamate
ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate
isoform RIMKLA also catalyses the synthesis of beta-citryl-L-glutamate with an activity that is 75fold lower than its N-acetyl-L-aspartyl-L-glutamate synthase activity
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ATP + N-acetyl-L-aspartate + L-glutamate
ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate
isoform RIMKLB catalyses the synthesis of beta-citryl-L-glutamate and N-acetyl-L-aspartyl-L-glutamate at nearly equal rates, cf. EC 6.3.1.17, beta-citrylglutamate synthase
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ATP + N-acetyl-L-aspartate + L-glutamate
ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate
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ATP + N-acetyl-L-aspartate + L-glutamate
ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate
ATP + N-acetyl-L-aspartate + L-glutamate
ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate
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ATP + N-acetyl-L-aspartate + L-glutamate
ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate
Q6PFX8, Q80WS1
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ATP + N-acetyl-L-aspartate + L-glutamate
ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate
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ATP
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dithiothreitol
stimulates; stimulates; the enzyme is markedly stimulated by dithiothreitol, which increases the activity by about 5fold
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0.87
citrate
at pH 8.0 and 37°C
1.48 - 4.59
N-acetyl-L-aspartate
0.0096
ATP
pH 8.0, 30°C
0.065
ATP
pH 8.0, 30°C; with 5 mM MgATP, at pH 8.0 and 37°C
0.73
L-glutamate
pH 8.0, 30°C
0.88
L-glutamate
at pH 8.0 and 37°C; pH 8.0, 30°C
1.48
N-acetyl-L-aspartate
at pH 8.0 and 37°C; pH 8.0, 30°C
4.59
N-acetyl-L-aspartate
pH 8.0, 30°C
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2.6 - 3
N-acetyl-L-aspartate
2.6
N-acetyl-L-aspartate
at pH 8.0 and 37°C; pH 8.0, 30°C
3
N-acetyl-L-aspartate
pH 8.0, 30°C
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1.09
pH 8.0, 30°C, formation of N-acetyl-L-aspartyl-L-glutamate
1.4
pH 8.0, 30°C, formation of N-acetyl-L-aspartyl-L-glutamate
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SwissProt
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cerebellar glia cell
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very low expression
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cerebellar neuron
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very low expression
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very low expression
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additional information
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the enzyme is undetectable in liver
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highest expression
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high expression
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RIMKA_HUMAN
391
0
42864
Swiss-Prot
RIMKA_MOUSE
380
0
41504
Swiss-Prot
RIMKB_BOVIN
386
0
42550
Swiss-Prot
RIMKB_DANRE
405
0
44500
Swiss-Prot
RIMKB_HUMAN
386
0
42464
Swiss-Prot
RIMKB_MOUSE
387
0
42528
Swiss-Prot
A0A1B2H2K7_STRNR
338
0
35239
TrEMBL
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43000
x * 43000, contains at least six subunits, SDS-PAGE; x * 43000, SDS-PAGE
42000
x * 42000, SDS-PAGE
42000
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x * 42000, SDS-PAGE
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x * 42000, SDS-PAGE; x * 43000, contains at least six subunits, SDS-PAGE; x * 43000, SDS-PAGE
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DEAE-Sepharose column chromatography, Q-Sepharose column chromatography, and S-200 gel filtration
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expressed as FLAG epitope-tagged protein in HEK-293T and CHO-K1 cells
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expressed in bacteria or HEK293T cells; expressed in Escherichia coli; expressed in Escherichia coli BL21(DE3)pLysS cells and in HEK-293T cells
expressed in CHO-K1 and HEK-293T cells
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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)
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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
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Becker, I.; Lodder, J.; Gieselmann, V.; Eckhardt, M.
Molecular characterization of N-acetylaspartylglutamate synthetase
J. Biol. Chem.
285
29156-29164
2010
Mus musculus
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Gehl, L.M.; Saab, O.H.; Bzdega, T.; Wroblewska, B.; Neale, J.H.
Biosynthesis of NAAG by an enzyme-mediated process in rat central nervous system neurons and glia
J. Neurochem.
90
989-997
2004
Rattus norvegicus
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