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EC Tree
IUBMB Comments Also acts with L-aspartate and, more slowly, with some other amino acids.
The taxonomic range for the selected organisms is: Mus musculus 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, acetylglutamate synthetase, nags/k, n-acetyl-l-glutamate synthetase, n-acetylglutamate synthase/kinase, ngnags,
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acetylglutamate synthase
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acetylglutamate synthetase
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acetylglutamic synthetase
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acetyltransferase, amino acid
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amino acid acetyltransferase
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N-acetyl-L-glutamate synthetase
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N-acetylglutamate synthase
N-acetylglutamate synthetase
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N-acetylglutamate synthase
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N-acetylglutamate synthase
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Acyl group transfer
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acetyl-CoA:L-glutamate N-acetyltransferase
Also acts with L-aspartate and, more slowly, with some other amino acids.
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acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
additional information
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enzyme deficiency causes hyperammonemia, presumably due to loss of carbamoylphosphate synthase I activity
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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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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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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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additional information
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enzyme deficiency causes hyperammonemia, presumably due to loss of carbamoylphosphate synthase I activity
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arginine
1 mM, 2-6fold activation of recombinant enzyme
arginine
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arginine
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activation is high if the enzyme is purified from fed mice and low if purified from fasted mice, thiol/disulfide interchange may be responsible for arginine sensitivity
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1.01
acetyl-CoA
mature enzyme with polyhistidine tag and thrombin protease recognition sequence
2.91
L-glutamate
mature enzyme with polyhistidine tag and thrombin protease recognition sequence
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0.346
mature recombinant enzyme in the absence of arginine
0.803
mature recombinant enzyme in the presence of 1 mM arginine
13.08
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mutant F121C + 1 mM arginine
15.28
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mutant E354A + 1 mM arginine
25.56
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wild-type + 1 mM arginine
3.19
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mutant G362S + 1 mM arginine
12.57
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mutant G360P + 1 mM arginine
12.57
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mutant G360P + 1mM arginine
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additional information
specific activity decreases from 30°C to 50°C. In the presence of L-arginine, specific activity increases 1.5fold between 30°C and 45°C
additional information
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specific activity decreases from 30°C to 50°C. In the presence of L-arginine, specific activity increases 1.5fold between 30°C and 45°C
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SwissProt
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recombinant
SwissProt
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the enzyme contains an N-terminal putative mitochondrial targeting sequence
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NAGS_MOUSE
527
0
57489
Swiss-Prot
Mitochondrion (Reliability: 2 )
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additional information
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enzyme possesses a carbamate kinase fold and an acyl-CoA N-acyltransferase fold
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proteolytic modification
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2 processed forms with different N-terminal truncations are produced, i.e. a long and a short mature form
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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
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50.78
melting temperature, presence of 1 mM L-Arg
52.96
melting temperature, presence of 10 mM L-Arg
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recombinant enzyme, Ni2+-affinity column
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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using Ni-NTA chromatography
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expression in Escherichia coli
cloned in Escherichia coli as a His-tagged fusion protein
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overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3), functional complementation of an enzyme-deficient Escherichia coli strain argA-, overexpression of the preenzyme in insect cells via baculovirus infection system, 2 processed forms with different N-terminal truncations are produced
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expression in Escherichia coli
expression in Escherichia coli
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Kawamoto, S.; Sonoda, T.; Ohtake, A.; Suzuki, Y.; Okuda, K.; Tatibana, M.
Alteration in arginine activation of N-acetylglutamate synthetase in vitro by disulfide or thiol compounds
J. Mol. Catal. B
10
191-197
2000
Mus musculus
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Caldovic, L.; Morizono, H.; Yu, X.; Thompson, M.; Shi, D.; Gallegos, R.; Allewell, N.M.; Malamy, M.H.; Tuchman, M.
Identification, cloning and expression of the mouse N-acetylglutamate synthase gene
Biochem. J.
364
825-831
2002
Mus musculus (Q8R4H7), Mus musculus
brenda
Morizono, H.; Caldovic, L.; Shi, D.; Tuchman, M.
Mammalian N-acetylglutamate synthase
Mol. Genet. Metab.
81 Suppl 1
S4-11
2004
Homo sapiens, Mus musculus
brenda
Caldovic, L.; Lopez, G.Y.; Haskins, N.; Panglao, M.; Shi, D.; Morizono, H.; Tuchman, M.
Biochemical properties of recombinant human and mouse N-acetylglutamate synthase
Mol. Genet. Metab.
87
226-232
2006
Homo sapiens (Q8N159), Homo sapiens, Mus musculus (Q8R4H7), Mus musculus
brenda
Haskins, N.; Panglao, M.; Qu, Q.; Majumdar, H.; Cabrera-Luque, J.; Morizono, H.; Tuchman, M.; Caldovic, L.
Inversion of allosteric effect of arginine on N-acetylglutamate synthase, a molecular marker for evolution of tetrapods
BMC Biochem.
9
24
2008
Arabidopsis thaliana, Danio rerio, Escherichia coli, Maricaulis maris, Mus musculus, Pseudomonas aeruginosa (P22567), Pseudomonas aeruginosa, Takifugu rubripes, Xanthomonas campestris, Xenopus laevis, Xenopus tropicalis
brenda
Haskins, N.; Mumo, A.; Brown, P.H.; Tuchman, M.; Morizono, H.; Caldovic, L.
Effect of arginine on oligomerization and stability of N-acetylglutamate synthase
Sci. Rep.
6
38711
2016
Maricaulis maris (Q0ASS9), Maricaulis maris, Mus musculus (Q8R4H7), Mus musculus, Xanthomonas campestris
brenda