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Literature summary for 2.7.2.8 extracted from

  • 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 (2008), J. Bacteriol., 190, 3018-3025.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
E17A site-directed mutagenesis, the mutant shows reduced Vmax, the mutation results in decreased affinity of NAGK for arginine Pseudomonas aeruginosa
E17D site-directed mutagenesis, the mutant shows reduced Vmax, the mutation results in decreased affinity of NAGK for arginine Pseudomonas aeruginosa
E17Q site-directed mutagenesis, the mutant shows reduced Vmax, the mutation results in decreased affinity of NAGK for arginine Pseudomonas aeruginosa
E284D site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates Pseudomonas aeruginosa
G290A site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates Pseudomonas aeruginosa
H271N site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates Pseudomonas aeruginosa
K213 site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates Pseudomonas aeruginosa
additional information 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 Pseudomonas aeruginosa
Q10A site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates Pseudomonas aeruginosa
R24E site-directed mutagenesis, the mutant shows reduced Vmax , the mutation results in increased affinity of NAGK for arginine Pseudomonas aeruginosa
Y21A site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates Pseudomonas aeruginosa

Inhibitors

Inhibitors Comment Organism Structure
L-arginine 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 Pseudomonas aeruginosa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics of enzyme mutants, overview Pseudomonas aeruginosa
3.1
-
ATP wild-type enzyme Pseudomonas aeruginosa
3.1
-
N-acetyl-L-glutamate wild-type enzyme Pseudomonas aeruginosa

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + N-acetyl-L-glutamate Pseudomonas aeruginosa NAGK catalyzes the second step of arginine biosynthesis. In Pseudomonas aeruginosa, this step is rate limiting, and feedback regulated and sigmoidally inhibited by arginine ADP + N-acetyl-L-glutamyl 5-phosphate
-
?

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + N-acetyl-L-glutamate
-
Pseudomonas aeruginosa ADP + N-acetyl-L-glutamyl 5-phosphate
-
?
ATP + N-acetyl-L-glutamate NAGK catalyzes the second step of arginine biosynthesis. In Pseudomonas aeruginosa, this step is rate limiting, and feedback regulated and sigmoidally inhibited by arginine Pseudomonas aeruginosa ADP + N-acetyl-L-glutamyl 5-phosphate
-
?

Subunits

Subunits Comment Organism
hexamer 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 Pseudomonas aeruginosa

Synonyms

Synonyms Comment Organism
N-acetylglutamate kinase
-
Pseudomonas aeruginosa
NagK
-
Pseudomonas aeruginosa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Pseudomonas aeruginosa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Pseudomonas aeruginosa

Cofactor

Cofactor Comment Organism Structure
ATP
-
Pseudomonas aeruginosa