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Literature summary extracted from

  • 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 (2010), J. Biol. Chem., 285, 29826-29833.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.3.1.17 dithiothreitol stimulates Mus musculus
6.3.2.41 dithiothreitol stimulates Mus musculus
6.3.2.41 dithiothreitol the enzyme is markedly stimulated by dithiothreitol, which increases the activity by about 5fold Mus musculus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.1.17 expressed in bacteria or HEK293T cells Mus musculus
6.3.2.B11 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 Mus musculus
6.3.2.41 expressed in bacteria or HEK293T cells Mus musculus
6.3.2.41 expressed in Escherichia coli Mus musculus
6.3.2.41 expressed in Escherichia coli BL21(DE3)pLysS cells and in HEK-293T cells Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.1.17 0.0096
-
ATP pH 8.0, 30°C Mus musculus
6.3.1.17 0.73
-
L-glutamate pH 8.0, 30°C Mus musculus
6.3.1.17 1.24
-
citrate pH 8.0, 30°C Mus musculus
6.3.2.B11 0.0096
-
ATP pH 8.0, 30°C Mus musculus
6.3.2.B11 0.73
-
L-glutamate pH 8.0, 30°C Mus musculus
6.3.2.B11 1.24
-
citrate pH 8.0, 30°C Mus musculus
6.3.2.41 0.0096
-
ATP pH 8.0, 30°C Mus musculus
6.3.2.41 0.065
-
ATP pH 8.0, 30°C Mus musculus
6.3.2.41 0.065
-
ATP with 5 mM MgATP, at pH 8.0 and 37°C Mus musculus
6.3.2.41 0.73
-
L-glutamate pH 8.0, 30°C Mus musculus
6.3.2.41 0.87
-
citrate at pH 8.0 and 37°C Mus musculus
6.3.2.41 0.88
-
L-glutamate pH 8.0, 30°C Mus musculus
6.3.2.41 0.88
-
L-glutamate at pH 8.0 and 37°C Mus musculus
6.3.2.41 1.48
-
N-acetyl-L-aspartate pH 8.0, 30°C Mus musculus
6.3.2.41 1.48
-
N-acetyl-L-aspartate at pH 8.0 and 37°C Mus musculus
6.3.2.41 4.59
-
N-acetyl-L-aspartate pH 8.0, 30°C Mus musculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.3.1.17 42000
-
x * 42000, SDS-PAGE Mus musculus
6.3.2.B11 42000
-
gel filtration Mus musculus
6.3.2.41 42000
-
x * 42000, SDS-PAGE Mus musculus
6.3.2.41 43000
-
x * 43000, SDS-PAGE Mus musculus
6.3.2.41 43000
-
x * 43000, contains at least six subunits, SDS-PAGE Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.1.17 ATP + citrate + L-glutamate Mus musculus
-
ADP + phosphate + beta-citryl-L-glutamate
-
?
6.3.2.B11 ATP + citrate + L-glutamate Mus musculus 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 ADP + phosphate + N-citryl-L-glutamate
-
?
6.3.2.41 ATP + N-acetyl-L-aspartate + L-glutamate Mus musculus
-
ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate
-
?

Organism

EC Number Organism UniProt Comment Textmining
6.3.1.17 Mus musculus Q80WS1
-
-
6.3.2.B11 Mus musculus Q80WS1
-
-
6.3.2.41 Mus musculus Q6PFX8
-
-
6.3.2.41 Mus musculus Q80WS1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.1.17
-
Mus musculus
6.3.2.B11
-
Mus musculus
6.3.2.41
-
Mus musculus
6.3.2.41 DEAE-Sepharose column chromatography, Q-Sepharose column chromatography, and S-200 gel filtration Mus musculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.3.1.17 central nervous system
-
Mus musculus
-
6.3.1.17 placenta
-
Mus musculus
-
6.3.1.17 testis
-
Mus musculus
-
6.3.2.B11 brain
-
Mus musculus
-
6.3.2.B11 central nervous system
-
Mus musculus
-
6.3.2.B11 placenta
-
Mus musculus
-
6.3.2.B11 testis
-
Mus musculus
-
6.3.2.41 central nervous system
-
Mus musculus
-
6.3.2.41 dorsal root ganglion
-
Mus musculus
-
6.3.2.41 placenta
-
Mus musculus
-
6.3.2.41 spinal cord
-
Mus musculus
-
6.3.2.41 testis
-
Mus musculus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.3.1.17 0.7
-
pH 8.0, 30°C, formation of beta-citryl-L-glutamate Mus musculus
6.3.2.41 1.09
-
pH 8.0, 30°C, formation of N-acetyl-L-aspartyl-L-glutamate Mus musculus
6.3.2.41 1.4
-
pH 8.0, 30°C, formation of N-acetyl-L-aspartyl-L-glutamate Mus musculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.1.17 ATP + citrate + L-glutamate
-
Mus musculus ADP + phosphate + beta-citryl-L-glutamate
-
?
6.3.1.17 ATP + citrate + L-glutamate the enzyme also has the activity of EC 6.3.2.41, N-acetylaspartylglutamate synthase. It catalyses the synthesis of beta-citryl-L-glutamate and N-acetyl-L-aspartyl-L-glutamate at nearly equal rates Mus musculus ADP + phosphate + beta-citryl-L-glutamate
-
?
6.3.2.B11 ATP + citrate + L-glutamate 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 Mus musculus ADP + phosphate + N-citryl-L-glutamate
-
?
6.3.2.B11 ATP + citrate + L-glutamate Vmax/Km for the synthesis of beta-citrylglutamate is 4fold higher than the Vmax/Km value for the synthesis of N-acetylaspartyl-glutamate Mus musculus ADP + phosphate + N-citryl-L-glutamate
-
?
6.3.2.41 ATP + N-acetyl-L-aspartate + citrate
-
Mus musculus ?
-
?
6.3.2.41 ATP + N-acetyl-L-aspartate + L-glutamate
-
Mus musculus ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate
-
?
6.3.2.41 ATP + N-acetyl-L-aspartate + 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 Mus musculus ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate
-
?
6.3.2.41 ATP + N-acetyl-L-aspartate + 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 Mus musculus ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate
-
?

Subunits

EC Number Subunits Comment Organism
6.3.1.17 ? x * 42000, SDS-PAGE Mus musculus
6.3.2.41 ? x * 42000, SDS-PAGE Mus musculus
6.3.2.41 ? x * 43000, SDS-PAGE Mus musculus
6.3.2.41 ? x * 43000, contains at least six subunits, SDS-PAGE Mus musculus

Synonyms

EC Number Synonyms Comment Organism
6.3.1.17 NAAG synthetase I
-
Mus musculus
6.3.1.17 NAAGS-I
-
Mus musculus
6.3.1.17 RIMKLB gene name, ambiguous Mus musculus
6.3.2.B11 N-acetylaspartylglutamate synthase ambiguous Mus musculus
6.3.2.B11 NAAG synthetase B
-
Mus musculus
6.3.2.B11 NAAGS B
-
Mus musculus
6.3.2.B11 RIMKLB
-
Mus musculus
6.3.2.41 N-acetylaspartylglutamate synthetase
-
Mus musculus
6.3.2.41 NAAG synthetase
-
Mus musculus
6.3.2.41 NAAGS
-
Mus musculus
6.3.2.41 RIMKLA
-
Mus musculus
6.3.2.41 RIMKLA gene name, ambiguous Mus musculus
6.3.2.41 RIMKLB gene name, ambiguous Mus musculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.3.1.17 30
-
assay at Mus musculus
6.3.2.B11 30
-
assay at Mus musculus
6.3.2.41 30
-
assay at Mus musculus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.3.1.17 1.5
-
L-glutamate pH 8.0, 30°C Mus musculus
6.3.2.B11 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 Mus musculus
6.3.2.41 2.6
-
N-acetyl-L-aspartate pH 8.0, 30°C Mus musculus
6.3.2.41 2.6
-
N-acetyl-L-aspartate at pH 8.0 and 37°C Mus musculus
6.3.2.41 3
-
N-acetyl-L-aspartate pH 8.0, 30°C Mus musculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.1.17 8
-
assay at Mus musculus
6.3.2.B11 8.5
-
synthesis of N-citryl-L-glutamate Mus musculus
6.3.2.41 8
-
-
Mus musculus
6.3.2.41 8
-
assay at Mus musculus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
6.3.2.B11 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 Mus musculus
6.3.2.B11 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 Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.2.41 ATP
-
Mus musculus

General Information

EC Number General Information Comment Organism
6.3.2.B11 physiological function the enzyme is involved in the biosynthesis of the dipeptide N-citryl-L-glutamate, an abundant neuropeptide in the mammalian brain Mus musculus