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
-
hyperammonemia
- ornithine
- l-arginine
- citrulline
- carbamylphosphate
-
ureagenesis
-
transcarbamylase
-
carglumic
- accoa
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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
ECTree
2.3.1.1 amino-acid N-acetyltransferaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.3.1.1 - amino-acid N-acetyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A518T
C200R
L430P
N479A
S410P
W484R
Y441F
Y485F
S387A
the mutant shows reduced activity compared to the wild type enzyme
E354A
F121C
G360P
G362S
delE283delQ284
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decrease of enzyme activity, induced substrate inhibition by acetyl-CoA
delQ284
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increase of enzyme activity, triggered acetyl-CoA inhibition
E352A
mutation affects the GCN5-related N-acetyltransferase domain
E352D
mutation affects the GCN5-related N-acetyltransferase domain
G339A
mutation affects the GCN5-related N-acetyltransferase domain
G368A
mutation affects the GCN5-related N-acetyltransferase domain
ins284Ains285A
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lower enzyme acitivity, decreased inhibition by arginine
V358A
mutation affects the GCN5-related N-acetyltransferase domain
E280A
F35C
G286P
G288S
additional information
A518T
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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
A518T
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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
C200R
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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
C200R
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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
L430P
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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
N479A
site-directed mutagenesis, an active site mutant with reduced activity compared to the wild-type enzyme
S410P
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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
S410P
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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
W484R
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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
Y441F
site-directed mutagenesis, an active site mutant with reduced activity compared to the wild-type enzyme
Y485F
site-directed mutagenesis, an active site mutant with reduced activity compared to the wild-type enzyme
E354A
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specific activity (micromol/min/mg): 15.47, 15.28 (+ 1mM arginine), arginine activation is abolished
E354A
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specific activity (micromol/min/mg): 15.47, 15.28 (+1mM arginine), arginine activation is abolished
F121C
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specific activity (micromol/min/mg): 12.22, 13.08 (+ 1mM arginine), arginine activation is abolished
F121C
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specific activity (micromol/min/mg): 12.22, 13.08 (+1mM arginine), arginine activation is abolished
G360P
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specific activity (micromol/min/mg): 13.00, 12.57 (+ 1mM arginine), arginine activation is abolished
G360P
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specific activity (micromol/min/mg): 13.00, 12.57 (+1mM arginine), arginine activation is abolished
G362S
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specific activity (micromol/min/mg): 3.22, 3.19 (+ 1mM arginine), arginine activation is abolished
G362S
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specific activity (micromol/min/mg): 3.22, 3.19 (+1mM arginine), arginine activation is abolished
E280A
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specific activity (micromol/min/mg): 26.93, 26.68 (+ 1mM arginine), arginine inhibition is abolished
E280A
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specific activity (micromol/min/mg): 26.93, 26.68 (+1mM arginine), arginine inhibition is abolished
F35C
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specific activity (micromol/min/mg): 9.66, 4.31 (+ 1mM arginine), only partial inhibition by arginine
F35C
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specific activity (micromol/min/mg): 9.66, 4.31 (+1mM arginine), only partial inhibition by arginine
G286P
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specific activity (micromol/min/mg): 3.51, 3.39 (+ 1mM arginine), no inhibition by arginine
G286P
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specific activity (micromol/min/mg): 3.51, 3.39 (+1mM arginine), no inhibition by arginine
G288S
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specific activity (micromol/min/mg): 46.04, 42.55 (+ 1mM arginine), no inhibition by arginine
G288S
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specific activity (micromol/min/mg): 46.04, 42.55 (+1mM arginine), no inhibition by arginine
additional information
CAF20762
after 48 h at 30°C the mutant DELTAcg3035 exhibits poor growth on unsupplemented MM1 plates in comparison to the Corynebacterium glutamicum wild-type, indicating a bradytrophy of the mutant due to arginine limitation
additional information
after 48 h at 30°C the mutant DELTAcg3035 exhibits poor growth on unsupplemented MM1 plates in comparison to the Corynebacterium glutamicum wild-type, indicating a bradytrophy of the mutant due to arginine limitation
additional information
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after 48 h at 30°C the mutant DELTAcg3035 exhibits poor growth on unsupplemented MM1 plates in comparison to the Corynebacterium glutamicum wild-type, indicating a bradytrophy of the mutant due to arginine limitation
additional information
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after 48 h at 30°C the mutant DELTAcg3035 exhibits poor growth on unsupplemented MM1 plates in comparison to the Corynebacterium glutamicum wild-type, indicating a bradytrophy of the mutant due to arginine limitation
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additional information
report of 21 mutations that cause NAGS deficiency. A total of 10 disease-causing mutations are associated with acute neonatal hyperammonemia. The remaining mutations are found in patients with late onset disease. Residual enzymatic activities are included in this report and the deleterious effects of eight mutations are confirmed by expression studies
additional information
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report of 21 mutations that cause NAGS deficiency. A total of 10 disease-causing mutations are associated with acute neonatal hyperammonemia. The remaining mutations are found in patients with late onset disease. Residual enzymatic activities are included in this report and the deleterious effects of eight mutations are confirmed by expression studies
additional information
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the isolated catalytic N-acetyltransferase domain retains catalytic activity in the absence of the amino acid kinase domain
additional information
the isolated catalytic N-acetyltransferase domain retains catalytic activity in the absence of the amino acid kinase domain
