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Information on EC 2.3.1.1 - amino-acid N-acetyltransferase and Organism(s) Mus musculus and UniProt Accession Q8R4H7
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2.3.1.1 amino-acid N-acetyltransferaseIUBMB Comments
Also acts with L-aspartate and, more slowly, with some other amino acids.
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Word Map
- 2.3.1.1
- ammonia
-
hyperammonemia
- ornithine
- l-arginine
- citrulline
- carbamylphosphate
-
ureagenesis
-
transcarbamylase
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carglumic
- accoa
-
6.3.4.16
-
gcn5-related
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protein-restricted
- carbamylglutamate
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nagks
-
feedback-resistant
- phenylbutyrate
-
ureotelic
- analysis
- medicine
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylglutamate synthase
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-
-
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acetylglutamate synthetase
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-
-
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acetylglutamic synthetase
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-
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acetyltransferase, amino acid
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-
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AGAS
-
-
-
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amino acid acetyltransferase
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-
-
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N-acetyl-L-glutamate synthetase
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-
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N-acetylglutamate synthase
N-acetylglutamate synthetase
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-
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N-acetylglutamate synthase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:L-glutamate N-acetyltransferase
Also acts with L-aspartate and, more slowly, with some other amino acids.
CAS REGISTRY NUMBER
COMMENTARY
9029-88-3
-
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
additional information
?
-
-
enzyme deficiency causes hyperammonemia, presumably due to loss of carbamoylphosphate synthase I activity
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
first enzyme in urea cycle
-
?
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
first enzyme in urea cycle
-
?
additional information
?
-
-
enzyme deficiency causes hyperammonemia, presumably due to loss of carbamoylphosphate synthase I activity
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
arginine
-
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12.57
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
-
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
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme contains an N-terminal putative mitochondrial targeting sequence
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NAGS_MOUSE
527
0
57489
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme possesses a carbamate kinase fold and an acyl-CoA N-acyltransferase fold
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
2 processed forms with different N-terminal truncations are produced, i.e. a long and a short mature form
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E354A
F121C
G360P
G362S
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
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
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
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
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
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
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