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acetyl-CoA + DL-2-aminopimelate
CoA + 2-acetylaminoheptanedioate
acetyl-CoA + glycine
CoA + acetylaminoacetate
acetyl-CoA + L-2-aminoadipate
CoA + 2-acetylaminohexanedioate
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartate
-
3.0% of activity with L-glutamate
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
acetyl-CoA + L-glutamate
N-acetyl-L-glutamate + CoA
-
assay at pH 8.5, 30°C, 5 min
-
-
?
acetyl-CoA + L-glutamate-gamma-hydroxamate
CoA + N-acetyl-L-glutamate-gamma-hydroxamate
-
15.5% of activity with glutamate
-
?
acetyl-CoA + L-glutamine
?
acetyl-CoA + L-glutamine
CoA + N-acetyl-L-glutamine
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
-
very low activity
-
?
butyryl-CoA + L-glutamate
CoA + N-butyryl-L-glutamate
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
-
?
propionyl-CoA + L-glutamate
CoA + N-propionyl-L-glutamate
additional information
?
-
acetyl-CoA + DL-2-aminopimelate
CoA + 2-acetylaminoheptanedioate
-
-
-
?
acetyl-CoA + DL-2-aminopimelate
CoA + 2-acetylaminoheptanedioate
-
-
-
?
acetyl-CoA + DL-2-aminopimelate
CoA + 2-acetylaminoheptanedioate
-
5.2% of activity with L-glutamate
-
?
acetyl-CoA + glycine
CoA + acetylaminoacetate
-
-
-
?
acetyl-CoA + glycine
CoA + acetylaminoacetate
-
-
-
?
acetyl-CoA + glycine
CoA + acetylaminoacetate
-
-
-
?
acetyl-CoA + glycine
CoA + acetylaminoacetate
-
2.9% of activity with L-glutamate
-
?
acetyl-CoA + L-2-aminoadipate
CoA + 2-acetylaminohexanedioate
-
1.3% of activity with L-glutamate
-
?
acetyl-CoA + L-2-aminoadipate
CoA + 2-acetylaminohexanedioate
-
-
-
?
acetyl-CoA + L-2-aminoadipate
CoA + 2-acetylaminohexanedioate
-
DL-2-aminoadipate, 5.2% of activity with L-glutamate
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
ability of protein Cg3035 to acetylate L-glutamate in vitro and in vivo
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
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
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
ability of protein Cg3035 to acetylate L-glutamate in vitro and in vivo
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
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
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
?
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
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
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
-
?
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
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
indispensible enzyme of arginine biosynthesis
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
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
assay at pH 9, 37°C
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
-
?
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
-
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
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
-
-
-
?
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
-
no activity with D-glutamate and L-glutamine
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
-
-
-
-
?
acetyl-CoA + L-glutamine
?
-
5% of activity with acetyl-CoA
-
-
?
acetyl-CoA + L-glutamine
?
-
-
-
-
?
acetyl-CoA + L-glutamine
?
-
6.8% of activity with L-glutamate
-
-
?
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
-
-
-
?
acetyl-CoA + L-glutamine
CoA + N-acetyl-L-glutamine
-
5% of the activity with L-glutamate
-
-
?
butyryl-CoA + L-glutamate
CoA + N-butyryl-L-glutamate
-
low activity compared to acetyl-CoA
-
-
?
butyryl-CoA + L-glutamate
CoA + N-butyryl-L-glutamate
-
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
-
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
-
-
-
?
propionyl-CoA + L-glutamate
CoA + N-propionyl-L-glutamate
-
-
-
?
propionyl-CoA + L-glutamate
CoA + N-propionyl-L-glutamate
-
-
-
?
propionyl-CoA + L-glutamate
CoA + N-propionyl-L-glutamate
-
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
-
-
?
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
?
-
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
-
-
?
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
-
-
?
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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G287S
arginine feedback resistant mutant enzyme
H15Y
arginine feedback resistant mutant enzyme
Q432R
arginine feedback resistant mutant enzyme
R58H
arginine feedback resistant mutant enzyme
S54N
arginine feedback resistant mutant enzyme
Y19C
arginine feedback resistant mutant enzyme
A279T
mutations that causes NAGS deficiency, late onset of disease
E433D
mutations that causes NAGS deficiency, late onset of disease
L312P
mutations that causes NAGS deficiency, late onset of disease
L442V
mutations that causes NAGS deficiency, late onset of disease
R509Q
mutations that causes NAGS deficiency, late onset of disease
T431I
mutations that causes NAGS deficiency, late onset of disease
V173E
mutations that causes NAGS deficiency, late onset of disease
V350I
mutations that causes NAGS deficiency, late onset of disease
W324X
mutations that causes NAGS deficiency, neonatal onset of disease
S387A
the mutant shows reduced activity compared to the wild type enzyme
S387A
-
the mutant shows reduced activity compared to the wild type enzyme
-
delE283delQ284
-
decrease of enzyme activity, induced substrate inhibition by acetyl-CoA
delQ284
-
increase of enzyme activity, triggered acetyl-CoA inhibition
E269A
mutation affects the putative arginine site
E352A
mutation affects the GCN5-related N-acetyltransferase domain
E352D
mutation affects the GCN5-related N-acetyltransferase domain
G146C
corresponding to clinical mutation
G275A
mutation affects the putative arginine site
G339A
mutation affects the GCN5-related N-acetyltransferase domain
G368A
mutation affects the GCN5-related N-acetyltransferase domain
ins284A
-
lower enzyme activity, decreased inhibition by arginine
ins284Ains285A
-
lower enzyme acitivity, decreased inhibition by arginine
K199A
mutation affects the putative arginine site
L353V
corresponding to clinical mutation
V358A
mutation affects the GCN5-related N-acetyltransferase domain
Y14A
mutation affects the putative arginine site
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
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
A518T
mutations that causes NAGS deficiency, neonatal onset of disease
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
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
C200R
mutations that causes NAGS deficiency, late onset of disease
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
L430P
mutations that causes NAGS deficiency, neonatal onset of disease
N479A
the mutant 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
-
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
-
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
S410P
mutations that causes NAGS deficiency, neonatal onset of disease
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
W484R
mutations that causes NAGS deficiency, neonatal onset of disease
Y441F
the mutant shows 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
the mutant shows 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
-
specific activity (micromol/min/mg): 15.47, 15.28 (+ 1mM arginine), arginine activation is abolished
E354A
-
specific activity (micromol/min/mg): 15.47, 15.28 (+1mM arginine), arginine activation is abolished
F121C
-
specific activity (micromol/min/mg): 12.22, 13.08 (+ 1mM arginine), arginine activation is abolished
F121C
-
specific activity (micromol/min/mg): 12.22, 13.08 (+1mM arginine), arginine activation is abolished
G360P
-
specific activity (micromol/min/mg): 13.00, 12.57 (+ 1mM arginine), arginine activation is abolished
G360P
-
specific activity (micromol/min/mg): 13.00, 12.57 (+1mM arginine), arginine activation is abolished
G362S
-
specific activity (micromol/min/mg): 3.22, 3.19 (+ 1mM arginine), arginine activation is abolished
G362S
-
specific activity (micromol/min/mg): 3.22, 3.19 (+1mM arginine), arginine activation is abolished
E280A
-
specific activity (micromol/min/mg): 26.93, 26.68 (+ 1mM arginine), arginine inhibition is abolished
E280A
-
specific activity (micromol/min/mg): 26.93, 26.68 (+1mM arginine), arginine inhibition is abolished
F35C
-
specific activity (micromol/min/mg): 9.66, 4.31 (+ 1mM arginine), only partial inhibition by arginine
F35C
-
specific activity (micromol/min/mg): 9.66, 4.31 (+1mM arginine), only partial inhibition by arginine
G286P
-
specific activity (micromol/min/mg): 3.51, 3.39 (+ 1mM arginine), no inhibition by arginine
G286P
-
specific activity (micromol/min/mg): 3.51, 3.39 (+1mM arginine), no inhibition by arginine
G288S
-
specific activity (micromol/min/mg): 46.04, 42.55 (+ 1mM arginine), no inhibition by arginine
G288S
-
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
-
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
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
-
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
-
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
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Reduced expression of intestinal N-acetylglutamate synthase in suckling piglets: a novel molecular mechanism for arginine as a nutritionally essential amino acid for neonates
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Sus scrofa (A4GTP3), Sus scrofa
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Homo sapiens, Maricaulis maris (Q0ASS9), Maricaulis maris
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Xylella fastidiosa, Xylella fastidiosa (Q87EL2), Xylella fastidiosa ATCC 35881D
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Zhao, G.; Haskins, N.; Jin, Z.; M Allewell, N.; Tuchman, M.; Shi, D.
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Maricaulis maris (Q0ASS9), Maricaulis maris
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Inhibition of N-acetylglutamate synthase by various monocarboxylic and dicarboxylic short-chain coenzyme A esters and the production of alternative glutamate esters
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Homo sapiens
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A novel type of N-acetylglutamate synthase is involved in the first step of arginine biosynthesis in Corynebacterium glutamicum
BMC Genomics
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Corynebacterium glutamicum (CAF20762), Corynebacterium glutamicum (Q8NM40), Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 (CAF20762), Corynebacterium glutamicum ATCC 13032 (Q8NM40)
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Escherichia coli, Homo sapiens, Rattus norvegicus
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Crystal structure of the N-acetyltransferase domain of human N-acetyl-L-glutamate synthase in complex with N-acetyl-L-glutamate provides insights into its catalytic and regulatory mechanisms
PLoS ONE
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Homo sapiens, Homo sapiens (Q8N159)
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Yang, X.; Wu, L.; Ran, Y.; Xu, A.; Zhang, B.; Yang, X.; Zhang, R.; Rao, Z.; Li, J.
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Mycobacterium tuberculosis (O33289), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (O33289)
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Homo sapiens (Q8N159), Homo sapiens
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