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
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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
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medicine
- 2.3.1.1
- ammonia
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hyperammonemia
- ornithine
- l-arginine
- citrulline
- carbamylphosphate
-
ureagenesis
-
transcarbamylase
-
carglumic
- accoa
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6.3.4.16
-
gcn5-related
-
protein-restricted
- carbamylglutamate
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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
ECTree
2.3.1.1 amino-acid N-acetyltransferaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 2.3.1.1 - amino-acid N-acetyltransferase
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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
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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
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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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-
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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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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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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
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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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enzyme catalyzes the first step in the biosynthesis of arginine
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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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enzyme deficiency causes hyperammonemia, presumably due to loss of carbamoylphosphate synthase I activity
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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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?
