Activating Compound | Comment | Organism | Structure |
---|---|---|---|
L-arginine | - |
Homo sapiens | |
additional information | dilution of the purified recombinant enzyme results in an increase in activity | Homo sapiens |
Cloned (Comment) | Organism |
---|---|
gene structure, His-tagged wild-type and mutant enzymes in enzyme-deficient Escherichia coli strain NK 5992 | Homo sapiens |
mutent enzymes from patients with NAGS missense mutations are overexpressed in Escherichia coli NK5992. All mutated proteins show severe decrease in enzyme activity providing evidence for the disease-causing nature of the mutations | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
A518T | naturally occurring mutation of a turkish patient suffering hyperammonemia, reconstruction of the mutation by site-directed mutagenesis, mutant enzyme shows over 95% reduced activity compared to the wild-type enzyme | Homo sapiens |
A518T | mutant enzymes from patients with NAGS missense mutations are overexpressed in Escherichia coli NK5992. All mutated proteins show severe decrease in enzyme activity providing evidence for the disease-causing nature of the mutations | Homo sapiens |
C200R | naturally occurring mutation of a french patient suffering hyperammonemia, reconstruction of the mutation by site-directed mutagenesis, mutant enzyme shows over 95% reduced activity compared to the wild-type enzyme | Homo sapiens |
C200R | mutant enzymes from patients with NAGS missense mutations are overexpressed in Escherichia coli NK5992. All mutated proteins show severe decrease in enzyme activity providing evidence for the disease-causing nature of the mutations | Homo sapiens |
L430P | naturally occurring mutation of a turkish patient suffering hyperammonemia, reconstruction of the mutation by site-directed mutagenesis, mutant enzyme shows reduced activity compared to the wild-type enzyme | Homo sapiens |
S410P | naturally occurring mutation of an algerian patient suffering hyperammonemia, reconstruction of the mutation by site-directed mutagenesis, mutant enzyme shows over 95% reduced activity compared to the wild-type enzyme | Homo sapiens |
S410P | mutant enzymes from patients with NAGS missense mutations are overexpressed in Escherichia coli NK5992. All mutated proteins show severe decrease in enzyme activity providing evidence for the disease-causing nature of the mutations | Homo sapiens |
W484R | naturally occurring mutation of a turkish patient suffering hyperammonemia, reconstruction of the mutation by site-directed mutagenesis, mutant enzyme reduced activity compared to the wild-type enzyme | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | - |
Homo sapiens | 5739 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + L-glutamate | Homo sapiens | - |
CoA + N-acetyl-L-glutamate | - |
? | |
acetyl-CoA + L-glutamate | Homo sapiens | the product N-acetyl-L-glutamate serves as an allosteric activator of carbamoylphosphate synthetase 1, the first enzyme of the urea cycle. Autosomal recessive inherited NAGS deficiency leads to severe neonatal or late-onset hyperammonemia | CoA + N-acetyl-L-glutamate | - |
? | |
additional information | Homo sapiens | autosomal recessively inherited enzyme deficiency causes severe neonatal or late-onset hyperammonemia, the enzyme is an allosteric activator of the carbamoylphosphate synthase I, the first enzyme of the urea cycle | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Homo sapiens | - |
3 families of patients with naturally occurring mutations leading to enzyme deficiency | - |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged wild-type enzyme by nickel affinity chromatography | Homo sapiens |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.053 | - |
purified recombinant His-tagged enzyme, in absence of L-arginine | Homo sapiens |
0.081 | - |
purified recombinant His-tagged enzyme, in presence of L-arginine | Homo sapiens |
0.139 | - |
purified recombinant His-tagged enzyme in 10fold dilution, in absence of L-arginine | Homo sapiens |
0.163 | - |
purified recombinant His-tagged enzyme in 10fold dilution, in presence of L-arginine | Homo sapiens |
0.325 | - |
purified recombinant His-tagged enzyme in 50fold dilution, in absence of L-arginine | Homo sapiens |
0.359 | - |
purified recombinant His-tagged enzyme in 50fold dilution, in presence of L-arginine | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + L-glutamate | - |
Homo sapiens | CoA + N-acetyl-L-glutamate | - |
? | |
acetyl-CoA + L-glutamate | the product N-acetyl-L-glutamate serves as an allosteric activator of carbamoylphosphate synthetase 1, the first enzyme of the urea cycle. Autosomal recessive inherited NAGS deficiency leads to severe neonatal or late-onset hyperammonemia | Homo sapiens | CoA + N-acetyl-L-glutamate | - |
? | |
additional information | autosomal recessively inherited enzyme deficiency causes severe neonatal or late-onset hyperammonemia, the enzyme is an allosteric activator of the carbamoylphosphate synthase I, the first enzyme of the urea cycle | Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
N-acetylglutamate synthase | - |
Homo sapiens |
NAGS | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.5 | - |
assay at | Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
acetyl-CoA | - |
Homo sapiens |