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Information on EC 2.3.1.1 - amino-acid N-acetyltransferase
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2.3.1.1 amino-acid N-acetyltransferaseIUBMB Comments
Also acts with L-aspartate and, more slowly, with some other amino acids.
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Word Map
- 2.3.1.1
- ammonia
-
hyperammonemia
- ornithine
- l-arginine
- citrulline
- carbamylphosphate
-
ureagenesis
-
transcarbamylase
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carglumic
- accoa
-
6.3.4.16
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gcn5-related
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protein-restricted
- carbamylglutamate
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nagks
-
feedback-resistant
- phenylbutyrate
-
ureotelic
- analysis
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
n-acetylglutamate synthase, n-acetylglutamate synthetase, acetylglutamate synthase, n-acetyl-l-glutamate synthase, nags-k, nags/k, acetylglutamate synthetase, ngnags, rv2747, n-acetyl-l-glutamate synthetase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylglutamate synthase
acetylglutamate synthetase
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acetylglutamic synthetase
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acetyltransferase, amino acid
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AGAS
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amino acid acetyltransferase
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ArgA
ArgH(A)
argJ
Cg3035
N-acetyl-glutamate synthase
N-acetyl-L-glutamate synthase
N-acetyl-L-glutamate synthase/kinase
N-acetyl-L-glutamate synthetase
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N-acetylglutamate synthase
N-acetylglutamate synthetase
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NAGS
NAGS/K
Rv2747
additional information
acetylglutamate synthase
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ArgH(A)
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acetyltransferase domain in ArgH(A) fusions. The last enzyme in arginine biosynthesis (argH) is fused to a short sequence that corresponds to the C-terminal, N-acetyltransferase-encoding domain of classical N-acetylglutamate synthase and is able to complement an argA mutant of Escherichia coli
ArgH(A)
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acetyltransferase domain in ArgH(A) fusions. The last enzyme in arginine biosynthesis (argH) is fusedto a short sequence that corresponds to the C-terminal, N-acetyltransferase-encoding domain of classical N-acetylglutamate synthase and is able to complement an argA mutant of Escherichia coli
ArgH(A)
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acetyltransferase domain in ArgH(A) fusions. The last enzyme in arginine biosynthesis (argH) is fused to a short sequence that corresponds to the C-terminal, N-acetyltransferase-encoding domain of classical N-acetylglutamate synthase and is able to complement an argA mutant of Escherichia coli
ArgH(A)
-
acetyltransferase domain in ArgH(A) fusions. The last enzyme in arginine biosynthesis (argH) is fused to a short sequence that corresponds to the C-terminal, N-acetyltransferase-encoding domain of classical N-acetylglutamate synthase and is able to complement an argA mutant of Escherichia coli
ArgH(A)
-
acetyltransferase domain in ArgH(A) fusions. The last enzyme in arginine biosynthesis (argH) is fused to a short sequence that corresponds to the C-terminal, N-acetyltransferase-encoding domain of classical N-acetylglutamate synthase and is able to complement an argA mutant of Escherichia coli
ArgH(A)
-
acetyltransferase domain in ArgH(A) fusions. The last enzyme in arginine biosynthesis (argH) is fused to a short sequence that corresponds to the C-terminal, N-acetyltransferase-encoding domain of classical N-acetylglutamate synthase and is able to complement an argA mutant of Escherichia coli
ArgH(A)
-
acetyltransferase domain in ArgH(A) fusions. The last enzyme in arginine biosynthesis (argH) is fusedto a short sequence that corresponds to the C-terminal, N-acetyltransferase-encoding domain of classical N-acetylglutamate synthase and is able to complement an argA mutant of Escherichia coli
ArgH(A)
-
acetyltransferase domain in ArgH(A) fusions. The last enzyme in arginine biosynthesis (argH) is fused to a short sequence that corresponds to the C-terminal, N-acetyltransferase-encoding domain of classical N-acetylglutamate synthase and is able to complement an argA mutant of Escherichia coli
N-acetyl-L-glutamate synthase
inactive T-state with L-arginine bound and active R-state complexed with CoA and L-glutamate
N-acetylglutamate synthase
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additional information
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the enzyme is a member of the GCN5-related N-acetyltransferase superfamily
additional information
pitax belongs to the GCN5-related N-acetyltransferase family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate
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acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate
rapid-equilibrium random bi bi mechanism
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acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate
sequential kinetic mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:L-glutamate N-acetyltransferase
Also acts with L-aspartate and, more slowly, with some other amino acids.
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CAS REGISTRY NUMBER
COMMENTARY
9029-88-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartate
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3.0% of activity with L-glutamate
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?
acetyl-CoA + L-glutamate
N-acetyl-L-glutamate + CoA
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assay at pH 8.5, 30°C, 5 min
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-
?
acetyl-CoA + L-glutamate-gamma-hydroxamate
CoA + N-acetyl-L-glutamate-gamma-hydroxamate
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15.5% of activity with glutamate
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?
acetyl-CoA + L-methionine
CoA + N-acetyl-L-methionine
pitax is an acetyltransferase and weakly catalyses the acetylation of l-methionine and l-methionine sulfoxide. Pitax belongs to the GCN5-related N-acetyltransferase family and contains all four sequence motifs conserved among family members. The beta4-strand structure in one of these motifs is disrupted, which is believed to affect binding of the substrate that accepts the acetyl group from acetyl-CoA
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-
?
acetyl-CoA + L-methionine sulfoxide
CoA + N-acetyl-L-methionine sulfoxide
pitax is an acetyltransferase and weakly catalyses the acetylation of l-methionine and l-methionine sulfoxide. Pitax belongs to the GCN5-related N-acetyltransferase family and contains all four sequence motifs conserved among family members. The beta4-strand structure in one of these motifs is disrupted, which is believed to affect binding of the substrate that accepts the acetyl group from acetyl-CoA
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?
benzoyl-CoA + L-glutamate
CoA + N-benzoyl-L-glutamate
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very low activity
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?
n-butyryl-CoA + L-glutamate
CoA + N-butyryl-L-glutamate
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1.5% of the activity with acetyl-CoA
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?
n-propionyl-CoA + L-glutamate
CoA + N-propionyl-L-glutamate
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23% of the activity with acetyl-CoA
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?
acetyl-CoA + DL-2-aminopimelate
CoA + 2-acetylaminoheptanedioate
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?
acetyl-CoA + DL-2-aminopimelate
CoA + 2-acetylaminoheptanedioate
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?
acetyl-CoA + DL-2-aminopimelate
CoA + 2-acetylaminoheptanedioate
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5.2% of activity with L-glutamate
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?
acetyl-CoA + glycine
CoA + acetylaminoacetate
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2.9% of activity with L-glutamate
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?
acetyl-CoA + L-2-aminoadipate
CoA + 2-acetylaminohexanedioate
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1.3% of activity with L-glutamate
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?
acetyl-CoA + L-2-aminoadipate
CoA + 2-acetylaminohexanedioate
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?
acetyl-CoA + L-2-aminoadipate
CoA + 2-acetylaminohexanedioate
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DL-2-aminoadipate, 5.2% of activity with L-glutamate
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
CAF20762, Q8NM40
ability of protein Cg3035 to acetylate L-glutamate in vitro and in vivo
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
CAF20762, Q8NM40
ability of protein Cg3035 to acetylate L-glutamate in vitro and in vivo. L-Glutamate most probably is the preferred amino acid substrate for Cg3035
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
CAF20762, Q8NM40
ability of protein Cg3035 to acetylate L-glutamate in vitro and in vivo
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
CAF20762, Q8NM40
ability of protein Cg3035 to acetylate L-glutamate in vitro and in vivo. L-Glutamate most probably is the preferred amino acid substrate for Cg3035
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
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enzyme catalyzes the first step in the biosynthesis of arginine
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
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enzyme catalyzes the first step in the biosynthesis of arginine
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
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CoA and N-acetyl-L-glutamate binding sites structure analysis from crystal structure, detailed overview
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
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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
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
first enzyme in urea cycle
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
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initial step of the L-arginine biosynthesis, pathway overview
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
assay at pH 8.5, 30°C, inactive T-state with L-arginine bound and active R-state complexed with CoA and L-glutamate
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
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indispensible enzyme of arginine biosynthesis
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
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enzyme catalyzes the first step in the biosynthesis of arginine
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
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enzyme catalyzes the first step in the biosynthesis of arginine
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
NAGS is the first enzyme of arginine biosynthesis, microbial arginine biosynthesis pathway, overview. Arginine is an allosteric inhibitor of microbial NAGS, arginine is also an inhibitor of plant NAGS, a partial inhibitor of fish NAGS, but an allosteric activator of mammalian NAGS
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
assay at pH 9, 37°C
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
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enzyme activates carbamoyl-phosphate synthase ammonia in small intestine mucosa, to allow citrulline synthesis in the tissue
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
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enzyme catalyzes the first step in arginine biosynthesis
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
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enzyme catalyzes the first step in the biosynthesis of arginine
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
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no activity with D-glutamate and L-glutamine
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?
acetyl-CoA + L-glutamine
CoA + N-acetyl-L-glutamine
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?
acetyl-CoA + L-glutamine
CoA + N-acetyl-L-glutamine
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?
acetyl-CoA + L-glutamine
CoA + N-acetyl-L-glutamine
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5% of the activity with L-glutamate
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?
butyryl-CoA + L-glutamate
CoA + N-butyryl-L-glutamate
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low activity compared to acetyl-CoA
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?
butyryl-CoA + L-glutamate
CoA + N-butyryl-L-glutamate
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very low activity
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?
propionyl-CoA + L-glutamate
CoA + N-propionyl-L-glutamate
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4% of activity with acetyl-CoA
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?
propionyl-CoA + L-glutamate
CoA + N-propionyl-L-glutamate
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low activity compared to acetyl-CoA
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?
propionyl-CoA + L-glutamate
CoA + N-propionyl-L-glutamate
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18% of activity with acetyl-CoA
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?
propionyl-CoA + L-glutamate
CoA + N-propionyl-L-glutamate
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4.3% of activity with acetyl-CoA
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?
additional information
?
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the enzyme has little activity with glutamine (5.0%) and glycine (2.9%) and no acetylation of other amino acids (less than 1.0%) as well as low activity with propionyl-CoA (4.3%) and no activity with other acyl-CoA derivatives
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?
additional information
?
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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
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?
additional information
?
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enzyme deficiency causes hyperammonemia, presumably due to loss of carbamoylphosphate synthase I activity
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?
additional information
?
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the N-acetyl-L-glutamate synthase contains an N-terminal catalytic N-acetyltransferase domain and a C-terminal amino acid kinase domain
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?
additional information
?
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the N-acetyl-L-glutamate synthase contains an N-terminal catalytic N-acetyltransferase domain and a C-terminal amino acid kinase domain
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?
additional information
?
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no activity with isobutyryl-CoA, isovaleryl-CoA, 3-methylcrotonyl-CoA, methylmalonyl-CoA, succinyl-CoA, and glutaryl-CoA
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?
additional information
?
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the enzyme has little activity with glutamine (5.0%) and glycine (2.9%) and no acetylation of other amino acids (less than 1.0%) as well as low activity with propionyl-CoA (4.3%) and no activity with other acyl-CoA derivatives
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?
additional information
?
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enzyme deficiency causes hyperammonemia, presumably due to loss of carbamoylphosphate synthase I activity
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?
additional information
?
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no substrate: L-aspartate, acetyl phosphate, N-acetyl-L-ornithine
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?
additional information
?
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the bifunctional N-acetyl-L-glutamate synthase/kinase contains an N-terminal catalytic N-acetyltransferase (NAT) domain, substrate N-acetyl-l-glutamate binding structure analysis, overview
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?
additional information
?
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the bifunctional N-acetyl-L-glutamate synthase/kinase contains an N-terminal catalytic N-acetyltransferase (NAT) domain, substrate N-acetyl-l-glutamate binding structure analysis, overview
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?
additional information
?
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the bifunctional N-acetyl-L-glutamate synthase/kinase contains an N-terminal catalytic N-acetyltransferase (NAT) domain, substrate N-acetyl-l-glutamate binding structure analysis, overview
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
CAF20762, Q8NM40
ability of protein Cg3035 to acetylate L-glutamate in vitro and in vivo
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
CAF20762, Q8NM40
ability of protein Cg3035 to acetylate L-glutamate in vitro and in vivo
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
enzyme catalyzes the first step in the biosynthesis of arginine
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
enzyme catalyzes the first step in the biosynthesis of arginine
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-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
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
first enzyme in urea cycle
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
initial step of the L-arginine biosynthesis, pathway overview
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
indispensible enzyme of arginine biosynthesis
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
enzyme catalyzes the first step in the biosynthesis of arginine
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
enzyme catalyzes the first step in the biosynthesis of arginine
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
NAGS is the first enzyme of arginine biosynthesis, microbial arginine biosynthesis pathway, overview. Arginine is an allosteric inhibitor of microbial NAGS, arginine is also an inhibitor of plant NAGS, a partial inhibitor of fish NAGS, but an allosteric activator of mammalian NAGS
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
enzyme activates carbamoyl-phosphate synthase ammonia in small intestine mucosa, to allow citrulline synthesis in the tissue
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
enzyme catalyzes the first step in arginine biosynthesis
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
enzyme catalyzes the first step in the biosynthesis of arginine
-
?