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Information on EC 2.3.1.1 - amino-acid N-acetyltransferase and Organism(s) Escherichia coli and UniProt Accession P0A6C5

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IUBMB Comments
Also acts with L-aspartate and, more slowly, with some other amino acids.
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This record set is specific for:
Escherichia coli
UNIPROT: P0A6C5
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The taxonomic range for the selected organisms is: Escherichia coli
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, rv2747, n-acetyl-l-glutamate synthetase, n-acetylglutamate synthase/kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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AGAS
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-
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amino acid acetyltransferase
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N-acetyl-L-glutamate synthase
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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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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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 hide
9029-88-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
show the reaction diagram
-
-
?
acetyl-CoA + DL-2-aminopimelate
CoA + 2-acetylaminoheptanedioate
show the reaction diagram
-
-
-
?
acetyl-CoA + L-2-aminoadipate
CoA + 2-acetylaminohexanedioate
show the reaction diagram
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1.3% of activity with L-glutamate
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?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
show the reaction diagram
acetyl-CoA + L-glutamine
?
show the reaction diagram
-
5% of activity with acetyl-CoA
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-
?
propionyl-CoA + L-glutamate
CoA + N-propionyl-L-glutamate
show the reaction diagram
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4% of activity with acetyl-CoA
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?
additional information
?
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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
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
arginine
Cd2+
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0.1 mM, 94% inhibition
CoA
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50% activity reduction at 2.5 mM
coenzyme A
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2.5 mM, 50% inhibition
Cu2+
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0.1 mM, 68% inhibition
high ionic strength
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KCl
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100 mM, 36% inhibition after 1 h, 300 mM, 74% inhibition after 1 h, 500 mM, 87% inhibition after 1 h
L-arginine
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50% activity reduction at 2 mM
L-citrulline
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10 mM, 75% inhibition
L-Indospicine
N-acetyl-L-glutamate
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50% activity reduction at 25 mM
N-acetylglutamate
N-ethylmaleimide
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-
O-(L-Norvalyl-5)-isourea
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0.02 mM, 50% inhibition
p-chloromercuribenzoate
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p-hydroxymercuribenzoate
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Zn2+
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0.1 mM, 43% inhibition
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.5
CoA
Escherichia coli
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pH and temperature not specified in the publication
2
L-arginine
Escherichia coli
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pH and temperature not specified in the publication
25
N-acetyl-L-glutamate
Escherichia coli
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pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00013
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1.84
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wild-type + 1mM arginine
5.85
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wild-type
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Uniprot
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51700
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6 * 51700, SDS-PAGE, cross-linking studies with dimethylsuberimidate, in the maximally aggregated state the enzyme exists as a hexamer
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
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6 * 51700, SDS-PAGE, cross-linking studies with dimethylsuberimidate, in the maximally aggregated state the enzyme exists as a hexamer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
highest stability
486061, 486063
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol stabilizes
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L-arginine or N-acetyl-L-glutamate stabilizes the high molecular weight form of 300000 Da
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use of silicone-treated glassware or plastic tubes, e.g. polyethylene, polycarbonate or polypropylene stabilizes the enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-cellulose, hydroxylapatite
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using Ni-NTA chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of N-acetylglutamate synthase gene argA and a mutant gene fbr-argA responsible for arginine feedback resistance
cloned in Escherichia coli as a His-tagged fusion protein
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Powers-Lee, S.G.
N-Acetylglutamate synthase
Methods Enzymol.
113
27-35
1985
Escherichia coli, Homo sapiens, Pseudomonas aeruginosa, Rattus norvegicus, Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
Marvil, D.K.; Leisinger, T.
N-Acetylglutamate synthase of Escherichia coli: purification, characterization, and molecular properties
J. Biol. Chem.
252
3295-3303
1977
Escherichia coli
Manually annotated by BRENDA team
Leisinger, T.; Haas, D.
N-Acetylglutamate synthase of Escherichia coli: regulation of synthesis and activity by arginine
J. Biol. Chem.
250
1690-1693
1975
Escherichia coli
Manually annotated by BRENDA team
Rajagopal, B.S.; Deponte, J.; Tuchman, M.; Malamy, M.H.
Use of inducible feedback-resistant N-acetylglutamate synthetase (argA) genes for enhanced arginine biosynthesis by genetically engineered Escherichia coli K-12 strains
Appl. Environ. Microbiol.
64
1805-1811
1998
Escherichia coli (P0A6C5), Escherichia coli
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Shi, D.; Allewell, N.M.; Tuchman, M.
The N-acetylglutamate synthase family: structures, function and mechanisms
Int. J. Mol. Sci.
16
13004-13022
2015
Escherichia coli, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team