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Literature summary for 2.7.2.8 extracted from

  • Marco-Marin, C.; Ramon-Maiques, S.; Tavarez, S.; Rubio, V.
    Site-directed mutagenesis of Escherichia coli acetylglutamate kinase and aspartokinase III probes the catalytic and substrate-binding mechanisms of these amino acid kinase family enzymes and allows three-dimensional modelling of aspartokinase (2003), J. Mol. Biol., 334, 459-476.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D162E about 0.1% of wild-type activity Escherichia coli
K8R substantial although diminished activity Escherichia coli
N158K substantial although diminished activity Escherichia coli
R66K substantial although diminished activity Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
ATP
-
Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.2
-
N-acetyl-L-glutamate wild-type, pH 7.0, 25°C Escherichia coli
0.29
-
ATP wild-type, pH 7.0, 25°C Escherichia coli
0.37
-
N-acetyl-L-glutamate mutant D162E, pH 7.0, 25°C Escherichia coli
0.46
-
ATP mutant D162E, pH 7.0, 25°C Escherichia coli
2.3
-
N-acetyl-L-glutamate mutant K8R, pH 7.0, 25°C Escherichia coli
3.3
-
ATP mutant K8R, pH 7.0, 25°C Escherichia coli
5.2
-
ATP mutant R66K, pH 7.0, 25°C Escherichia coli
7.9
-
ATP mutant N158Q, pH 7.0, 25°C Escherichia coli
600
-
N-acetyl-L-glutamate mutant N158Q, pH 7.0, 25°C Escherichia coli
898
-
N-acetyl-L-glutamate mutant R66K, pH 7.0, 25°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6C8
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + N-acetyl-L-glutamate
-
Escherichia coli ADP + N-acetyl-L-glutamate 5-phosphate
-
?

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
30.4
-
ATP wild-type, pH 7.0, 25°C Escherichia coli
41.5
-
ATP mutant N158Q, pH 7.0, 25°C Escherichia coli