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Literature summary for 2.3.1.1 extracted from

  • Schmidt, E.; Nuoffer, J.M.; Haberle, J.; Pauli, S.; Guffon, N.; Vianey-Saban, C.; Wermuth, B.; Koch, H.G.
    Identification of novel mutations of the human N-acetylglutamate synthase gene and their functional investigation by expression studies (2005), Biochim. Biophys. Acta, 1740, 54-59.
    View publication on PubMed

Activating Compound

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(Commentary)

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

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

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Homo sapiens 5739
-

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Homo sapiens
-
3 families of patients with naturally occurring mutations leading to enzyme deficiency
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type enzyme by nickel affinity chromatography Homo sapiens

Specific Activity [micromol/min/mg]

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 and Products (Substrate)

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

Synonyms Comment Organism
N-acetylglutamate synthase
-
Homo sapiens
NAGS
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
-
Homo sapiens