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Information on EC 2.3.1.1 - amino-acid N-acetyltransferase and Organism(s) Pseudomonas aeruginosa

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EC Tree
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:
Pseudomonas aeruginosa
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The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
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, nags/k, acetylglutamate synthetase, rv2747, n-acetyl-l-glutamate synthetase, n-acetylglutamate synthase/kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylglutamate synthase
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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-
-
-
N-acetyl-L-glutamate synthase
N-acetyl-L-glutamate synthetase
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-
-
-
N-acetylglutamate synthase
N-acetylglutamate synthetase
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-
-
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additional information
pitax belongs to the GCN5-related N-acetyltransferase family
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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-
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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 + L-glutamine
CoA + N-acetyl-L-glutamine
show the reaction diagram
-
5% of the activity with L-glutamate
-
-
?
acetyl-CoA + L-methionine
CoA + N-acetyl-L-methionine
show the reaction diagram
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
show the reaction diagram
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
-
-
?
n-butyryl-CoA + L-glutamate
CoA + N-butyryl-L-glutamate
show the reaction diagram
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-
1.5% of the activity with acetyl-CoA
-
?
n-propionyl-CoA + L-glutamate
CoA + N-propionyl-L-glutamate
show the reaction diagram
-
-
23% of the activity with acetyl-CoA
-
?
additional information
?
-
-
no substrate: L-aspartate, acetyl phosphate, N-acetyl-L-ornithine
-
-
?
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,3-diaminopropane
-
10 mM, 88% inhibition in the presence of 0.5 mM N-acetyl-L-glutamate
arginine
cadaverine
-
10 mM, 80% inhibition in the presence of 0.5 mM N-acetyl-L-glutamate
L-arginine
-
0.1 mM, 50% inhibition
L-glutamate
-
-
polyamines
-
-
-
putrescine
-
10 mM, 74% inhibition in the presence of 0.5 mM N-acetyl-L-glutamate
spermidine
-
1 mM, 78% inhibition in the presence of 0.5 mM N-acetyl-L-glutamate
spermine
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1 mM, 88% inhibition in the presence of 0.5 mM N-acetyl-L-glutamate
additional information
-
not inhibitory: N-acetyl-L-ornithine, L-ornithine, L-citrulline
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05 - 2.7
acetyl-CoA
2.1 - 557
L-glutamate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.6 - 15.1
acetyl-CoA
60 - 152
L-glutamate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
114.9
-
mutant delQ284
24
-
mutant delE283delQ284
43.6
-
mutant ins284Ains285A
48.8
-
mutant ins284A
79.4
-
wild-type enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A8G5CID9_PSEAI
432
0
47889
TrEMBL
-
A0A8G4TMV4_PSEAI
405
0
41777
TrEMBL
-
A0A3M5E7E5_PSEAI
597
0
62250
TrEMBL
-
A0A8G3X8R7_PSEAI
405
0
41772
TrEMBL
-
A0A8G7HWL8_PSEAI
405
0
41793
TrEMBL
-
A0A8G7Q022_PSEAI
432
0
47843
TrEMBL
-
A0A8E5UXE1_PSEAI
405
0
41762
TrEMBL
-
A0A8G3YBA3_PSEAI
405
0
41791
TrEMBL
-
A0A8G4MS13_PSEAI
432
0
47806
TrEMBL
-
A0A8G7D0J2_PSEAI
405
0
41837
TrEMBL
-
A0A069PY38_PSEAI
405
0
41763
TrEMBL
-
A0A8B4ZLF2_PSEAI
405
0
41781
TrEMBL
-
A0A072ZJQ5_PSEAI
432
0
47859
TrEMBL
-
A0A8G3P1V6_PSEAI
405
0
41733
TrEMBL
-
A0A6B1Y8B3_PSEAI
405
0
41723
TrEMBL
-
A0A8G7GGM8_PSEAI
405
0
41703
TrEMBL
-
A0A8F9NUJ3_PSEAI
405
0
41705
TrEMBL
-
A0A2R3IYI6_PSEAI
432
0
47875
TrEMBL
-
A0A4U0JMB5_PSEAI
405
0
41791
TrEMBL
-
A0A8F9NX24_PSEAI
405
0
41809
TrEMBL
-
A0A3S0IXD4_PSEAI
405
0
41802
TrEMBL
-
A0A3M5EH19_PSEAI
385
0
41961
TrEMBL
-
A0A5N3ZCA8_PSEAI
405
0
41744
TrEMBL
-
A0A8G2Z403_PSEAI
432
0
47829
TrEMBL
-
A0A2R3ITB4_PSEAI
405
0
41814
TrEMBL
-
A0A8G3JGN9_PSEAI
432
0
47829
TrEMBL
-
A0A8G3W480_PSEAI
405
0
41825
TrEMBL
-
A0A8G7A9W5_PSEAI
432
0
47806
TrEMBL
-
A0A8F9IWI2_PSEAI
405
0
41773
TrEMBL
-
A0A8G2VAJ1_PSEAI
405
0
41793
TrEMBL
-
A0A8G3EDU6_PSEAI
405
0
41774
TrEMBL
-
A0A4P0TEI1_PSEAI
237
0
24868
TrEMBL
-
A0A8G6H1R7_PSEAI
432
0
47958
TrEMBL
-
A0A8G5M3F9_PSEAI
405
0
41809
TrEMBL
-
A0A8G6Y058_PSEAI
432
0
47874
TrEMBL
-
A0A8G2ZHI3_PSEAI
432
0
47799
TrEMBL
-
A0A8G6NM26_PSEAI
432
0
47889
TrEMBL
-
A0A5K1S684_PSEAI
432
0
47849
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, hanging drop vapour diffusion method, mixing of 0.001 ml protein solution containing 13 mg/ml protein with 0.001 ml of reservoir solution containing 0.1 M Tris-HCl, pH 6.5, 1.6 M ammonium sulfate, and 0.1% w/v sodium azide, 18°C, 1-2 days, cryoprotection in 0.1 M Tris-HCl, pH 6.5, 1.6 M ammonium sulfate, 30% v/v glycerol and 0.1% w/v sodium azide, X-ray diffraction structure determination and analysis at 2.25 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
use of silicone-treated glassware or plastic tubes, e.g. polyethylene, polycarbonate or polypropylene stabilizes the enzyme
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, hydroxyapatite, 10fold purification
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21
gene PA1377, cloning in Escherichia coli strain JM109, expression in Escherichia coli strain BL21(DE3)
phylogenetic analysis
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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
Haas, D.; Leisinger, T.
Multiple control of N-acetylglutamate synthetase from Pseudomonas aeruginosa: synergistic inhibition by acetylglutamate and polyamines
Biochem. Biophys. Res. Commun.
60
42-47
1974
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Haas, D.; Kurer, V.; Leisinger, T.
N-acetylglutamate synthetase of Pseudomonas aeruginosa. An assay in vitro and feedback inhibition by arginine
Eur. J. Biochem.
31
290-295
1972
Pseudomonas aeruginosa
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
Davies, A.M.; Tata, R.; Chauviac, F.X.; Sutton, B.J.; Brown, P.R.
Structure of a putative acetyltransferase (PA1377) from Pseudomonas aeruginosa
Acta Crystallogr. Sect. F
64
338-342
2008
Pseudomonas aeruginosa (Q9I3W7), Pseudomonas aeruginosa
Manually annotated by BRENDA team
Sancho-Vaello, E.; Fernandez-Murga, M.L.; Rubio, V.
Site-directed mutagenesis studies of acetylglutamate synthase delineate the site for the arginine inhibitor
FEBS Lett.
582
1081-1086
2008
Pseudomonas aeruginosa (P22567), Pseudomonas aeruginosa
Manually annotated by BRENDA team
Sancho-Vaello, E.; Fernandez-Murga, M.L.; Rubio, V.
Mechanism of arginine regulation of acetylglutamate synthase, the first enzyme of arginine synthesis
FEBS Lett.
583
202-206
2009
Pseudomonas aeruginosa
Manually annotated by BRENDA team