2.3.1.1: amino-acid N-acetyltransferase
This is an abbreviated version!
For detailed information about amino-acid N-acetyltransferase, go to the full flat file.
Word Map on EC 2.3.1.1
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2.3.1.1
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ammonia
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hyperammonemia
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ornithine
-
l-arginine
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citrulline
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carbamylphosphate
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ureagenesis
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transcarbamylase
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carglumic
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accoa
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6.3.4.16
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gcn5-related
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protein-restricted
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carbamylglutamate
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nagks
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feedback-resistant
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phenylbutyrate
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ureotelic
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analysis
-
medicine
- 2.3.1.1
- ammonia
-
hyperammonemia
- ornithine
- l-arginine
- citrulline
- carbamylphosphate
-
ureagenesis
-
transcarbamylase
-
carglumic
- accoa
-
6.3.4.16
-
gcn5-related
-
protein-restricted
- carbamylglutamate
-
nagks
-
feedback-resistant
- phenylbutyrate
-
ureotelic
- analysis
- medicine
Reaction
Synonyms
acetylglutamate synthase, acetylglutamate synthetase, acetylglutamic synthetase, acetyltransferase, amino acid, AGAS, amino acid acetyltransferase, ARG2, ArgA, ArgH(A), argJ, Cg3035, More, N-acetyl-glutamate synthase, N-acetyl-L-glutamate synthase, N-acetyl-L-glutamate synthase/kinase, N-acetyl-L-glutamate synthetase, N-acetylglutamate synthase, N-acetylglutamate synthase/kinase, N-acetylglutamate synthetase, NAGS, NAGS-K, NAGS/K, NAT, ngNAGS, PaNAGS, pitax, Rv2747, SINAGS1, XcNAGS
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2.3.1.1 amino-acid N-acetyltransferaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 2.3.1.1 - amino-acid N-acetyltransferase
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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
-
3.0% of activity with L-glutamate
-
?
acetyl-CoA + L-glutamate
N-acetyl-L-glutamate + CoA
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assay at pH 8.5, 30°C, 5 min
-
-
?
acetyl-CoA + L-glutamate-gamma-hydroxamate
CoA + N-acetyl-L-glutamate-gamma-hydroxamate
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15.5% of activity with glutamate
-
?
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
-
-
?
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
-
-
?
benzoyl-CoA + L-glutamate
CoA + N-benzoyl-L-glutamate
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very low activity
-
?
n-butyryl-CoA + L-glutamate
CoA + N-butyryl-L-glutamate
-
-
1.5% of the activity with acetyl-CoA
-
?
n-propionyl-CoA + L-glutamate
CoA + N-propionyl-L-glutamate
-
-
23% of the activity with acetyl-CoA
-
?
acetyl-CoA + DL-2-aminopimelate
CoA + 2-acetylaminoheptanedioate
-
-
-
?
acetyl-CoA + DL-2-aminopimelate
CoA + 2-acetylaminoheptanedioate
-
-
-
?
acetyl-CoA + DL-2-aminopimelate
CoA + 2-acetylaminoheptanedioate
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5.2% of activity with L-glutamate
-
?
acetyl-CoA + glycine
CoA + acetylaminoacetate
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2.9% of activity with L-glutamate
-
?
acetyl-CoA + L-2-aminoadipate
CoA + 2-acetylaminohexanedioate
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1.3% of activity with L-glutamate
-
?
acetyl-CoA + L-2-aminoadipate
CoA + 2-acetylaminohexanedioate
-
-
-
?
acetyl-CoA + L-2-aminoadipate
CoA + 2-acetylaminohexanedioate
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DL-2-aminoadipate, 5.2% of activity with L-glutamate
-
?
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. 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
-
-
?
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
-
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
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
-
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
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
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
-
-
-
?
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
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
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enzyme catalyzes the first step in the biosynthesis of arginine
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
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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
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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
-
-
-
-
?
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
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
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enzyme catalyzes the first step in the biosynthesis of arginine
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
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no activity with D-glutamate and L-glutamine
-
-
?
acetyl-CoA + L-glutamine
CoA + N-acetyl-L-glutamine
-
-
-
?
acetyl-CoA + L-glutamine
CoA + N-acetyl-L-glutamine
-
-
-
?
acetyl-CoA + L-glutamine
CoA + N-acetyl-L-glutamine
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5% of the activity with L-glutamate
-
-
?
butyryl-CoA + L-glutamate
CoA + N-butyryl-L-glutamate
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low activity compared to acetyl-CoA
-
-
?
butyryl-CoA + L-glutamate
CoA + N-butyryl-L-glutamate
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very low activity
-
?
propionyl-CoA + L-glutamate
CoA + N-propionyl-L-glutamate
-
4% of activity with acetyl-CoA
-
?
propionyl-CoA + L-glutamate
CoA + N-propionyl-L-glutamate
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low activity compared to acetyl-CoA
-
-
?
propionyl-CoA + L-glutamate
CoA + N-propionyl-L-glutamate
-
18% of activity with acetyl-CoA
-
?
propionyl-CoA + L-glutamate
CoA + N-propionyl-L-glutamate
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4.3% of activity with acetyl-CoA
-
?
additional information
?
-
-
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
-
-
?
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
-
-
?
additional information
?
-
-
enzyme deficiency causes hyperammonemia, presumably due to loss of carbamoylphosphate synthase I activity
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-
?
additional information
?
-
-
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
?
-
the N-acetyl-L-glutamate synthase contains an N-terminal catalytic N-acetyltransferase domain and a C-terminal amino acid kinase domain
-
-
?
additional information
?
-
-
no activity with isobutyryl-CoA, isovaleryl-CoA, 3-methylcrotonyl-CoA, methylmalonyl-CoA, succinyl-CoA, and glutaryl-CoA
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
enzyme deficiency causes hyperammonemia, presumably due to loss of carbamoylphosphate synthase I activity
-
-
?
additional information
?
-
-
no substrate: L-aspartate, acetyl phosphate, N-acetyl-L-ornithine
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-
?
additional information
?
-
-
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
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
