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EC Tree
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
n-acetyl-l-glutamate kinase, acetylglutamate kinase, n-acetylglutamate kinase, mmnags/k, n-acetyl glutamate kinase, ynagk, n-acetylglutamate 5-phosphotransferase, ccnagk, ecnagk, acetylglutamate phosphokinase,
more
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N-acetyl-L-glutamate 5-phosphotransferase
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N-acetyl-L-glutamate kinase
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N-acetylglutamate kinase
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acetylglutamate phosphokinase
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kinase, acetylglutamate (phosphorylating)
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N-acetylglutamate 5-phosphotransferase
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N-acetylglutamate phosphokinase
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N-acetylglutamate-5-phosphotransferase
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N-acetylglutamic 5-phosphotransferase
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N-acetylglutamate kinase
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N-acetylglutamate kinase
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phospho group transfer
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ATP:N-acetyl-L-glutamate 5-phosphotransferase
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ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
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-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
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-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
ATP + N-carbamoyl-L-glutamate
ADP + N-carbamoyl-L-glutamate 5-phosphate
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at 33% of the activity with N-acetyl-L-glutamate
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-
?
ATP + N-formyl-L-glutamate
ADP + N-formyl-L-glutamate 5-phosphate
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at 20% of the activity with N-acetyl-L-glutamate
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-
?
dATP + N-acetyl-L-glutamate
dADP + N-acetyl-L-glutamate 5-phosphate
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as effective as ATP
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-
?
additional information
?
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ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
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?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
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in presence of hydroxylamine formation of N-acetyl-L-glutamate 5-hydroxamate + ADP + phosphate
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
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enzyme synthesis not repressed by exogenous L-arginine or its precursors
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-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
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second enzyme of arginine biosynthesis
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?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
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?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
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NAGK catalyzes the second step of arginine biosynthesis. In Pseudomonas aeruginosa, this step is rate limiting, and feedback regulated and sigmoidally inhibited by arginine
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?
additional information
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not: ITP
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?
additional information
?
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not: GTP
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?
additional information
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N-propionyl-L-glutamate almost inactive
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?
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ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
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?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
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-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
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NAGK catalyzes the second step of arginine biosynthesis. In Pseudomonas aeruginosa, this step is rate limiting, and feedback regulated and sigmoidally inhibited by arginine
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-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
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enzyme synthesis not repressed by exogenous L-arginine or its precursors
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-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
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second enzyme of arginine biosynthesis
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?
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Ca2+
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Mn2+, Zn2+, Co2+ and Ca2+ in this order can partially replace Mg2+
Co2+
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Mn2+, Zn2+, Co2+ and Ca2+ in this order can partially replace Mg2+
Mn2+
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Mn2+, Zn2+, Co2+ and Ca2+ in decreasing order can partially replace Mg2+
Zn2+
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Mn2+, Zn2+, Co2+ and Ca2+ in this order can partially replace Mg2+
Mg2+
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Mg2+
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30 mM, slight inhibition
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L-arginine
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sigmoidal arginine inhibition kinetics, feedback inhibition, indentification of the N-terminal arginine site, mutational analysis, the mobile alphaH-beta16 loop of the arginine site is the modulatory signal receiver, overview
MgCl2
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30 mM, slight inhibition
arginine
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1 mM, 96% inhibition
arginine
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feedback inhibition is markedly dependent on pH, above pH 9 no inhibition
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2 - 3.1
N-acetyl-L-glutamate
additional information
additional information
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kinetics of enzyme mutants, overview
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3
ATP
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pH 7.2, 37°C
3.1
ATP
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wild-type enzyme
2
N-acetyl-L-glutamate
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pH 7.2, 37°C
3.1
N-acetyl-L-glutamate
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wild-type enzyme
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additional information
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SwissProt
brenda
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29000
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x * 29000, SDS-PAGE
30000
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2 * 30000, SDS-PAGE
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dimer
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2 * 30000, SDS-PAGE
hexamer
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with an extra N-terminal-linked helix interlinking three dimers, the hexameric architecture is not essential for arginine inhibition but is functionally essential for physiologically relevant arginine control of NAGK
additional information
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due to the capacity for self-association the enzyme can exist in different states of aggregation depending on the nature of the ligands and the concentration of phosphate buffer
hexamer
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hexamer
three homodimers are linked to form a ring-like hexamer
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E17A
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site-directed mutagenesis, the mutant shows reduced Vmax, the mutation results in decreased affinity of NAGK for arginine
E17D
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site-directed mutagenesis, the mutant shows reduced Vmax, the mutation results in decreased affinity of NAGK for arginine
E17Q
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site-directed mutagenesis, the mutant shows reduced Vmax, the mutation results in decreased affinity of NAGK for arginine
E284D
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site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates
G290A
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site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates
H271N
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site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates
K213
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site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates
Q10A
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site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates
R24E
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site-directed mutagenesis, the mutant shows reduced Vmax , the mutation results in increased affinity of NAGK for arginine
Y21A
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site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates
additional information
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N-helix N-terminal deletions spanning 16 residues dissociate NAGK to active dimers, those of 20 residues decrease the apparent affinity for arginine, and complete N-helix deletion of 26 residues abolishes arginine inhibition, overview
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70
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30 min, complete inactivation
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loss of activity on repeated freezing and thawing
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-20°C, stable over extended periods
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4°C, 0.1 M phosphate buffer, stable
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Haas, D.; Leisinger, T.
N-acetylglutamate 5-phosphotransferase of Pseudomonas aeruginosa. Purification and ligand-directed association-dissociation
Eur. J. Biochem.
52
365-375
1975
Pseudomonas aeruginosa
brenda
Haas, D.; Leisinger, T.
N-acetylglutamate 5-phosphotransferase of Pseudomonas aeruginosa. Catalytic and regulatory properties
Eur. J. Biochem.
52
377-383
1975
Pseudomonas aeruginosa
brenda
Fernandez-Murga, M.L.; Ramon-Maiques, S.; Gil-Ortiz, F.; Fita, I.; Rubio, V.
Towards structural understanding of feedback control of arginine biosynthesis: cloning and expression of the gene for the arginine-inhibited N-acetyl-L-glutamate kinase from Pseudomonas aeruginosa, purification and crystallization of the recombinant enzyme and preliminary X-ray studies
Acta Crystallogr. Sect. D
58
1045-1047
2002
Pseudomonas aeruginosa
brenda
Fernandez-Murga, M.L.; Gil-Ortiz, F.; Llacer, J.L.; Rubio, V.
Arginine biosynthesis in Thermotoga maritima: characterization of the arginine-sensitive N-acetyl-L-glutamate kinase
J. Bacteriol.
186
6142-6149
2004
Pseudomonas aeruginosa, Thermotoga maritima
brenda
Ramon-Maiques, S.; Fernandez-Murga, M.L.; Gil-Ortiz, F.; Vagin, A.; Fita, I.; Rubio, V.
Structural bases of feed-back control of arginine biosynthesis, revealed by the structures of two hexameric N-acetylglutamate kinases, from Thermotoga maritima and Pseudomonas aeruginosa
J. Mol. Biol.
356
695-713
2006
Pseudomonas aeruginosa (Q9HTN2), Pseudomonas aeruginosa, Thermotoga maritima (Q9X2A4), Thermotoga maritima
brenda
Fernandez-Murga, M.L.; Rubio, V.
Basis of arginine sensitivity of microbial N-acetyl-L-glutamate kinases: mutagenesis and protein engineering study with the Pseudomonas aeruginosa and Escherichia coli enzymes
J. Bacteriol.
190
3018-3025
2008
Pseudomonas aeruginosa
brenda
Min, L.; Jin, Z.; Caldovic, L.; Morizono, H.; Allewell, N.M.; Tuchman, M.; Shi, D.
Mechanism of allosteric inhibition of N-acetyl-L-glutamate synthase by L-arginine
J. Biol. Chem.
284
4873-4880
2009
Arabidopsis thaliana, Pseudomonas aeruginosa (Q9HTN2)
brenda
Yang, X.
Conformational dynamics play important roles upon the function of N-acetylglutamate kinase
Appl. Microbiol. Biotechnol.
101
3485-3492
2017
Escherichia coli (P0A6C8), Corynebacterium glutamicum (Q59281), Pseudomonas aeruginosa (Q9HTN2), Thermotoga maritima (Q9X2A4), Corynebacterium glutamicum ATCC 13032 (Q59281)
brenda