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 |
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 |
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 |
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 |
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 | - |
? |
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 | - |
- |
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 |
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 | - |
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 |
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 | - |
? |
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 |
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 |
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 |
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 |
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 |
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 |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
6.3.2.41 | ATP | - |
Mus musculus |
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 |