2.7.2.8: acetylglutamate kinase
This is an abbreviated version!
For detailed information about acetylglutamate kinase, go to the full flat file.
Reaction
Synonyms
acetylglutamate kinase, acetylglutamate phosphokinase, amino-acid acetyltransferase, argB, CcNAGK, EcNAGK, GRMZM2G132777, kinase, acetylglutamate (phosphorylating), mmNAGS/K, N-acetyl glutamate kinase, N-acetyl-glutamate 5-phosphotransferase, N-acetyl-L-glutamate 5-phosphotransferase, N-acetyl-L-glutamate kinase, N-acetyl-L-glutamate synthase/kinase, N-acetylglutamate 5-phosphotransferase, N-acetylglutamate kinase, N-acetylglutamate phosphokinase, N-acetylglutamate-5-phosphotransferase, N-acetylglutamic 5-phosphotransferase, NagK, NAGK1, NAGS-K, SYPA5-5 N-acetylglutamate kinase, xcNAGS/K, yNAGK
ECTree
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KM Value
KM Value on EC 2.7.2.8 - acetylglutamate kinase
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0.3
ATP
in the absence of protein PII, in 50 mM imidazole, pH 7.5
0.4
ATP
in the absence of protein PII, in 50 mM imidazole, pH 7.5
20.1
ATP
DELTA357-513 (truncated mutant lacking C-terminal 150 amino acids), pH not specified, 37°C
0.85
N-acetyl-L-glutamate
in the absence of protein PII, in 50 mM imidazole, pH 7.5
0.87
N-acetyl-L-glutamate
in the absence of protein PII, in 50 mM imidazole, pH 7.5
3.1
N-acetyl-L-glutamate
-
in the absence of protein PII, in 50 mM imidazole, pH 7.5
3.14
N-acetyl-L-glutamate
-
mutant H26A, pH and temperature not specified in the publication
3.25
N-acetyl-L-glutamate
-
mutant H268N, pH and temperature not specified in the publication
3.32
N-acetyl-L-glutamate
-
mutant G287D, pH and temperature not specified in the publication
3.43
N-acetyl-L-glutamate
-
mutant E19R, pH and temperature not specified in the publication
3.52
N-acetyl-L-glutamate
-
wild-type, pH and temperature not specified in the publication
3.61
N-acetyl-L-glutamate
-
mutant E19A, pH and temperature not specified in the publication
3.72
N-acetyl-L-glutamate
-
mutant R209A, pH and temperature not specified in the publication
3.76
N-acetyl-L-glutamate
-
mutant H268A, pH and temperature not specified in the publication
3.86
N-acetyl-L-glutamate
-
mutant G287A, pH and temperature not specified in the publication
3.89
N-acetyl-L-glutamate
-
mutant W23A, pH and temperature not specified in the publication
3.96
N-acetyl-L-glutamate
-
mutant R209K, pH and temperature not specified in the publication
6.98
N-acetyl-L-glutamate
-
mutant DELTA8, pH and temperature not specified in the publication
7.4
N-acetyl-L-glutamate
-
in the absence of protein PII, in 50 mM imidazole, pH 7.5
7.84
N-acetyl-L-glutamate
-
mutant DELTA2-15, pH and temperature not specified in the publication
8.23
N-acetyl-L-glutamate
-
mutant DELTA2-19, pH and temperature not specified in the publication
8.45
N-acetyl-L-glutamate
-
mutant DELTA2-29, pH and temperature not specified in the publication
9.45
N-acetyl-L-glutamate
in complex with PII protein and 2-ketoglutarate
13.3
N-acetyl-L-glutamate
DELTA357-513 (truncated mutant lacking C-terminal 150 amino acids), pH not specified, 37°C
13.68
N-acetyl-L-glutamate
-
mutant E281A, pH and temperature not specified in the publication
25.74
N-acetyl-L-glutamate
-
mutant DELTA25, pH and temperature not specified in the publication
85
N-acetyl-L-glutamate
in the presence of 1 mM L-arginine, in 50 mM imidazole, pH 7.5
additional information
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formation of complex between enzyme and signal transduction protein PII decreases Km-value by a factor of 10 and increases Vmax 4fold
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additional information
additional information
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kinetics of enzyme mutants, overview
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