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acetyl-CoA + L-glutamate
coenzyme A + N-acetyl-L-glutamate
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
-
at 33% of the activity with N-acetyl-L-glutamate
-
-
?
ATP + N-formyl-L-glutamate
ADP + N-formyl-L-glutamate 5-phosphate
-
at 20% of the activity with N-acetyl-L-glutamate
-
-
?
dATP + N-acetyl-L-glutamate
dADP + N-acetyl-L-glutamate 5-phosphate
-
as effective as ATP
-
-
?
additional information
?
-
acetyl-CoA + L-glutamate
coenzyme A + N-acetyl-L-glutamate
-
ancestral bifunctional N-acetylglutamate synthase and kinase
-
?
acetyl-CoA + L-glutamate
coenzyme A + N-acetyl-L-glutamate
-
-
ancestral bifunctional N-acetylglutamate synthase and kinase
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
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
-
highly specific for ATP and N-acetyl-L-glutamate
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
-
key enzyme in regulation of arginine biosynthesis
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
key enzyme in regulation of arginine biosynthesis
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
highly specific for ATP and N-acetyl-L-glutamate
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
-
key enzyme in regulation of arginine biosynthesis
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
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
-
enzyme synthesis not repressed by exogenous L-arginine or its precursors
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
second enzyme of arginine biosynthesis
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
?
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-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
r
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
r
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
r
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
r
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
NAGK catalyzes the second step of arginine biosynthesis. In Pseudomonas aeruginosa, this step is rate limiting, and feedback regulated and sigmoidally inhibited by arginine
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
r
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
r
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
?
additional information
?
-
-
NAGK strongly interacts with PII protein only in the presence of Mg-ATP, this process is reversed by 2-oxoglutarate
-
-
?
additional information
?
-
-
not: GTP
-
-
?
additional information
?
-
-
not: N-benzoyl-L-glutamate, L-glutamate, D-glutamate
-
-
?
additional information
?
-
-
not: GTP
-
-
?
additional information
?
-
-
not: GTP
-
-
?
additional information
?
-
-
not: N-benzoyl-L-glutamate, L-glutamate, D-glutamate
-
-
?
additional information
?
-
-
not: N-benzoyl-L-glutamate, L-glutamate, D-glutamate
-
-
?
additional information
?
-
-
not: GTP
-
-
?
additional information
?
-
-
not: N-benzoyl-L-glutamate, L-glutamate, D-glutamate
-
-
?
additional information
?
-
-
not: ITP
-
-
?
additional information
?
-
-
not: GTP
-
-
?
additional information
?
-
-
N-propionyl-L-glutamate almost inactive
-
-
?
additional information
?
-
-
NAGK interacts with PII protein
-
-
?
additional information
?
-
residues Lys364, Arg394 and Asn399 in xcNAGS/K are involved in binding of L-glutamate
-
-
?
additional information
?
-
residues Lys364, Arg394 and Asn399 in xcNAGS/K are involved in binding of L-glutamate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
additional information
?
-
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
key enzyme in regulation of arginine biosynthesis
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
key enzyme in regulation of arginine biosynthesis
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
key enzyme in regulation of arginine biosynthesis
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
enzyme synthesis not repressed by exogenous L-arginine or its precursors
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
second enzyme of arginine biosynthesis
-
-
?
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-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
r
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
r
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
r
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
r
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
NAGK catalyzes the second step of arginine biosynthesis. In Pseudomonas aeruginosa, this step is rate limiting, and feedback regulated and sigmoidally inhibited by arginine
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
r
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
r
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
?
additional information
?
-
-
NAGK strongly interacts with PII protein only in the presence of Mg-ATP, this process is reversed by 2-oxoglutarate
-
-
?
additional information
?
-
-
NAGK interacts with PII protein
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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1.3
AcCoA
only for N-acetylglutamate synthase activity
2.8
L-glutamate
only for N-acetylglutamate synthase activity
0.2 - 898
N-acetyl-L-glutamate
additional information
additional information
-
0.29
ATP
wild-type, pH 7.0, 25°C
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
0.46
ATP
mutant D162E, pH 7.0, 25°C
0.6
ATP
-
in the absence of protein PII, in 50 mM imidazole, pH 7.5
1.1
ATP
-
in the absence of protein PII, in 50 mM imidazole, pH 7.5
1.1
ATP
pH 7.5, 37°C, wild-type, Vmax: 72.6
1.74
ATP
without PII protein
2.03
ATP
in complex with PII protein
2.47
ATP
in complex with PII protein and 2-ketoglutarate
3
ATP
-
pH 8.0, 37°C, allosteric
3.1
ATP
-
wild-type enzyme
3.3
ATP
mutant K8R, pH 7.0, 25°C
5.2
ATP
mutant R66K, pH 7.0, 25°C
7.9
ATP
mutant N158Q, pH 7.0, 25°C
13.4
ATP
pH 7.5, 37°C, mutant G11A, Vmax: 11.1
15.3
ATP
wild-type, pH not specified, 37°C
20.1
ATP
DELTA357-513 (truncated mutant lacking C-terminal 150 amino acids), pH not specified, 37°C
0.2
N-acetyl-L-glutamate
wild-type, pH 7.0, 25°C
0.37
N-acetyl-L-glutamate
mutant D162E, pH 7.0, 25°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
1.3
N-acetyl-L-glutamate
pH 7.5, 37°C, wild-type, Vmax: 80
1.9
N-acetyl-L-glutamate
-
two Km-values: 1.9 and 6.2, pH 7.5, 30°C
2
N-acetyl-L-glutamate
-
pH 7.2, 37°C
2.3
N-acetyl-L-glutamate
mutant K8R, pH 7.0, 25°C
2.7
N-acetyl-L-glutamate
-
pH 7.5, complex of enzyme and PII protein
3.1
N-acetyl-L-glutamate
-
wild-type enzyme
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
3.29
N-acetyl-L-glutamate
-
mutant H26E, pH 8.0, 37°C
3.32
N-acetyl-L-glutamate
-
mutant G287D, pH and temperature not specified in the publication
3.33
N-acetyl-L-glutamate
-
mutant E19R, pH 8.0, 37°C
3.36
N-acetyl-L-glutamate
-
mutant H268N/H26E/E19R, pH 8.0, 37°C
3.42
N-acetyl-L-glutamate
-
wild-type, pH 8.0, 37°C
3.42
N-acetyl-L-glutamate
-
mutant H268N/H26E, pH 8.0, 37°C
3.43
N-acetyl-L-glutamate
-
mutant E19R, pH and temperature not specified in the publication
3.45
N-acetyl-L-glutamate
-
mutant H268N, pH 8.0, 37°C
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
4
N-acetyl-L-glutamate
-
pH 8.0, 37°C, allosteric
5.1
N-acetyl-L-glutamate
pH 7.5, 37°C, mutant G11A, Vmax: 9.7
6
N-acetyl-L-glutamate
-
pH 5.5, 37°C
6.2
N-acetyl-L-glutamate
-
2 Km-values: 1.9 and 6.2, pH 7.5, 30°C
6.98
N-acetyl-L-glutamate
-
mutant DELTA8, pH and temperature not specified in the publication
7.08
N-acetyl-L-glutamate
without PII protein
7.4
N-acetyl-L-glutamate
-
in the absence of protein PII, in 50 mM imidazole, pH 7.5
7.55
N-acetyl-L-glutamate
in complex with PII protein
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
10
N-acetyl-L-glutamate
wild-type, pH not specified, 37°C
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
15
N-acetyl-L-glutamate
-
-
15
N-acetyl-L-glutamate
-
pH 5.5, 37°C
25.74
N-acetyl-L-glutamate
-
mutant DELTA25, pH and temperature not specified in the publication
27.4
N-acetyl-L-glutamate
-
pH 7.5, free enzyme
85
N-acetyl-L-glutamate
in the presence of 1 mM L-arginine, in 50 mM imidazole, pH 7.5
600
N-acetyl-L-glutamate
mutant N158Q, pH 7.0, 25°C
898
N-acetyl-L-glutamate
mutant R66K, pH 7.0, 25°C
additional information
additional information
-
formation of complex between enzyme and signal transduction protein PII decreases Km-value by a factor of 10 and increases Vmax 4fold
-
additional information
additional information
-
kinetics of enzyme mutants, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 - 187.5
N-acetyl-L-glutamate
7.7
ATP
wild-type, pH not specified, 37°C
13
ATP
DELTA357-513 (truncated mutant lacking C-terminal 150 amino acids), pH not specified, 37°C
2
N-acetyl-L-glutamate
-
mutant DELTA25, pH and temperature not specified in the publication, with 1 mM L-arginine
3.2
N-acetyl-L-glutamate
-
mutant DELTA25, pH and temperature not specified in the publication
4.2
N-acetyl-L-glutamate
-
mutant DELTA8, pH and temperature not specified in the publication, with 1 mM L-arginine
4.9
N-acetyl-L-glutamate
wild-type, pH not specified, 37°C
6.4
N-acetyl-L-glutamate
-
mutant DELTA8, pH and temperature not specified in the publication
7.2
N-acetyl-L-glutamate
-
mutant DELTA2-29, pH and temperature not specified in the publication, with 1 mM L-arginine
7.9
N-acetyl-L-glutamate
-
mutant DELTA2-29, pH and temperature not specified in the publication
8.4
N-acetyl-L-glutamate
DELTA357-513 (truncated mutant lacking C-terminal 150 amino acids), pH not specified, 37°C
11.5
N-acetyl-L-glutamate
-
mutant DELTA2-19, pH and temperature not specified in the publication, with 1 mM L-arginine
12.4
N-acetyl-L-glutamate
-
mutant DELTA2-19, pH and temperature not specified in the publication
13.1
N-acetyl-L-glutamate
-
in the absence of protein PII, in 50 mM imidazole, pH 7.5
13.8
N-acetyl-L-glutamate
-
mutant DELTA2-15, pH and temperature not specified in the publication, with 1 mM L-arginine
15.2
N-acetyl-L-glutamate
-
mutant DELTA2-15, pH and temperature not specified in the publication
31.4
N-acetyl-L-glutamate
-
wild-type, pH 8.0, 37°C, with 1 mM L-arginine
31.4
N-acetyl-L-glutamate
-
wild-type, pH and temperature not specified in the publication, with 1 mM L-arginine
32.8
N-acetyl-L-glutamate
-
mutant W23A, pH and temperature not specified in the publication, with 1 mM L-arginine
34.9
N-acetyl-L-glutamate
-
mutant E281A, pH and temperature not specified in the publication, with 1 mM L-arginine
36.1
N-acetyl-L-glutamate
-
mutant G287A, pH and temperature not specified in the publication, with 1 mM L-arginine
36.7
N-acetyl-L-glutamate
-
mutant G287A, pH and temperature not specified in the publication
37.4
N-acetyl-L-glutamate
-
mutant R209K, pH and temperature not specified in the publication, with 1 mM L-arginine
38.3
N-acetyl-L-glutamate
-
mutant G287D, pH and temperature not specified in the publication, with 1 mM L-arginine
38.5
N-acetyl-L-glutamate
-
mutant E19A, pH and temperature not specified in the publication, with 1 mM L-arginine
39.7
N-acetyl-L-glutamate
-
mutant R209A, pH and temperature not specified in the publication, with 1 mM L-arginine
39.7
N-acetyl-L-glutamate
-
mutant W23A, pH and temperature not specified in the publication
40.4
N-acetyl-L-glutamate
-
in the presence of protein PII, in 50 mM imidazole, pH 7.5
41
N-acetyl-L-glutamate
-
mutant E281A, pH and temperature not specified in the publication
41
N-acetyl-L-glutamate
-
mutant H26E, pH 8.0, 37°C, with 1 mM L-arginine
41.1
N-acetyl-L-glutamate
-
mutant H268A, pH and temperature not specified in the publication, with 1 mM L-arginine
41.1
N-acetyl-L-glutamate
-
mutant H268N, pH 8.0, 37°C, with 1 mM L-arginine
41.3
N-acetyl-L-glutamate
-
mutant G287D, pH and temperature not specified in the publication
41.9
N-acetyl-L-glutamate
-
mutant R209A, pH and temperature not specified in the publication
42
N-acetyl-L-glutamate
-
mutant E19R, pH 8.0, 37°C, with 1 mM L-arginine
42.1
N-acetyl-L-glutamate
-
mutant E19R, pH and temperature not specified in the publication, with 1 mM L-arginine
42.1
N-acetyl-L-glutamate
-
mutant R209K, pH and temperature not specified in the publication
43
N-acetyl-L-glutamate
-
mutant H26A, pH and temperature not specified in the publication, with 1 mM L-arginine
43.3
N-acetyl-L-glutamate
-
mutant H268N, pH and temperature not specified in the publication
43.4
N-acetyl-L-glutamate
-
mutant H26A, pH and temperature not specified in the publication
43.8
N-acetyl-L-glutamate
-
mutant H268N, pH and temperature not specified in the publication, with 1 mM L-arginine
44.1
N-acetyl-L-glutamate
-
mutant E19A, pH and temperature not specified in the publication
44.4
N-acetyl-L-glutamate
-
mutant H26E, pH 8.0, 37°C
44.5
N-acetyl-L-glutamate
-
mutant H268A, pH and temperature not specified in the publication
44.8
N-acetyl-L-glutamate
-
mutant E19R, pH and temperature not specified in the publication
45.1
N-acetyl-L-glutamate
-
wild-type, pH 8.0, 37°C
45.1
N-acetyl-L-glutamate
-
wild-type, pH and temperature not specified in the publication
45.3
N-acetyl-L-glutamate
-
mutant H268N, pH 8.0, 37°C
45.6
N-acetyl-L-glutamate
-
mutant H268N/H26E, pH 8.0, 37°C, with 1 mM L-arginine
45.8
N-acetyl-L-glutamate
-
mutant E19R, pH 8.0, 37°C
46
N-acetyl-L-glutamate
-
mutant H268N/H26E/E19R, pH 8.0, 37°C, with 1 mM L-arginine
46.1
N-acetyl-L-glutamate
-
mutant H268N/H26E, pH 8.0, 37°C
46.5
N-acetyl-L-glutamate
-
mutant H268N/H26E/E19R, pH 8.0, 37°C
115
N-acetyl-L-glutamate
in the presence of 1 mM L-arginine, in 50 mM imidazole, pH 7.5
126.1
N-acetyl-L-glutamate
in the absence of protein PII, in 50 mM imidazole, pH 7.5
187.5
N-acetyl-L-glutamate
in the presence of protein PII, in 50 mM imidazole, pH 7.5
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0.02
L-arginine
Synechococcus elongatus
-
in the absence of protein PII, in 50 mM imidazole, pH 7.5
0.19
L-arginine
Synechococcus elongatus
-
in the presence of protein PII, in 50 mM imidazole, pH 7.5
0.4
L-arginine
Corynebacterium crenatum
-
wild-type, pH 8.0, 37°C
0.4
L-arginine
Corynebacterium glutamicum
-
wild-type, pH and temperature not specified in the publication
0.44
L-arginine
Saccharomyces cerevisiae
DELTA357-513 (truncated mutant lacking C-terminal 150 amino acids), pH not specified, 37°C
0.97
L-arginine
Saccharomyces cerevisiae
wild-type, pH not specified, 37°C
1
L-arginine
Arabidopsis thaliana
in the absence of protein PII, in 50 mM imidazole, pH 7.5
1.8
L-arginine
Corynebacterium glutamicum
-
mutant W23A, pH and temperature not specified in the publication
5.9
L-arginine
Arabidopsis thaliana
in the presence of protein PII, in 50 mM imidazole, pH 7.5
6.4
L-arginine
Corynebacterium glutamicum
-
mutant DELTA8, pH and temperature not specified in the publication
6.8
L-arginine
Corynebacterium glutamicum
-
mutant DELTA25, pH and temperature not specified in the publication
8.6
L-arginine
Corynebacterium glutamicum
-
mutant E281A, pH and temperature not specified in the publication
14.8
L-arginine
Corynebacterium glutamicum
-
mutant R209K, pH and temperature not specified in the publication
14.9
L-arginine
Corynebacterium glutamicum
-
mutant G287A, pH and temperature not specified in the publication
15.7
L-arginine
Corynebacterium glutamicum
-
mutant H268A, pH and temperature not specified in the publication
16.1
L-arginine
Corynebacterium glutamicum
-
mutant E19A, pH and temperature not specified in the publication
16.2
L-arginine
Corynebacterium glutamicum
-
mutant G287D, pH and temperature not specified in the publication
18.5
L-arginine
Corynebacterium glutamicum
-
mutant R209A, pH and temperature not specified in the publication
21
L-arginine
Corynebacterium crenatum
-
mutant H26E, pH 8.0, 37°C
21.7
L-arginine
Corynebacterium glutamicum
-
mutant H26A, pH and temperature not specified in the publication
22
L-arginine
Corynebacterium crenatum
-
mutant H268N, pH 8.0, 37°C
22.3
L-arginine
Corynebacterium glutamicum
-
mutant H268N, pH and temperature not specified in the publication
24
L-arginine
Corynebacterium crenatum
-
mutant E19R, pH 8.0, 37°C
24.4
L-arginine
Corynebacterium glutamicum
-
mutant E19R, pH and temperature not specified in the publication
28.4
L-arginine
Corynebacterium glutamicum
-
mutant DELTA2-15, pH and temperature not specified in the publication
59.2
L-arginine
Corynebacterium glutamicum
-
mutant DELTA2-19, pH and temperature not specified in the publication
65.2
L-arginine
Corynebacterium glutamicum
-
mutant DELTA2-29, pH and temperature not specified in the publication
350
L-arginine
Corynebacterium crenatum
-
mutant H268N/H26E, pH 8.0, 37°C
784
L-arginine
Corynebacterium crenatum
-
mutant H268N/H26E/E19R, pH 8.0, 37°C
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A26V
site-directed mutagenesis, the mutation deregulates the feedback inhibition of the enzyme
G287D
site-directed mutagenesis, the mutation increases the 50% inhibitoryL--arginine concentration significantly in vitro, which deregulates the feedback inhibition of CcNAGK by L-arginine in SYPA5-5 during the fermentation
H268N/H26E
-
Km and kcat (N-acetyl-L-glutamate) similar to wild-type, IC50 (L-arginine) 875fold increased compared to wild-type
H268N/H26E/E19R
-
Km and kcat (N-acetyl-L-glutamate) similar to wild-type, IC50 (L-arginine) 1960fold increased compared to wild-type
M31V
site-directed mutagenesis, the mutation deregulates the feedback inhibition of the enzyme
DELTA2-15
-
Km (N-acetyl-L-glutamate) increased compared to wild-type, kcat decreased compared to wild-type, IC50 (L-arginine) 71fold increased compared to wild-type
DELTA2-19
-
Km (N-acetyl-L-glutamate) increased compared to wild-type, kcat decreased compared to wild-type, IC50 (L-arginine) 148fold increased compared to wild-type
DELTA2-29
-
Km (N-acetyl-L-glutamate) increased compared to wild-type, kcat decreased compared to wild-type, IC50 (L-arginine) 163fold increased compared to wild-type
DELTA25
-
Km (N-acetyl-L-glutamate) highly increased compared to wild-type, kcat highly decreased compared to wild-type, IC50 (L-arginine) 17fold increased compared to wild-type
DELTA8
-
Km (N-acetyl-L-glutamate) increased compared to wild-type, kcat highly decreased compared to wild-type, IC50 (L-arginine) 16fold increased compared to wild-type
E19A
-
Km (N-acetyl-L-glutamate) similar to wild-type, kcat similar to wild-type, IC50 (L-arginine) 40fold increased compared to wild-type
E19R
-
Km (N-acetyl-L-glutamate) similar to wild-type, kcat similar to wild-type, IC50 (L-arginine) 61fold increased compared to wild-type
E281A
-
Km (N-acetyl-L-glutamate) highly increased compared to wild-type, kcat similar to wild-type, IC50 (L-arginine) 21fold increased compared to wild-type
G287A
-
Km (N-acetyl-L-glutamate) similar to wild-type, kcat decreased compared to wild-type, IC50 (L-arginine) 37fold increased compared to wild-type
G287D
-
Km (N-acetyl-L-glutamate) similar to wild-type, kcat similar to wild-type, IC50 (L-arginine) 40fold increased compared to wild-type
H268A
-
Km (N-acetyl-L-glutamate) similar to wild-type, kcat similar to wild-type, IC50 (L-arginine) 39fold increased compared to wild-type
H268N
-
Km (N-acetyl-L-glutamate) similar to wild-type, kcat similar to wild-type, IC50 (L-arginine) 58fold increased compared to wild-type
H26A
-
Km (N-acetyl-L-glutamate) similar to wild-type, kcat similar to wild-type, IC50 (L-arginine) 54fold increased compared to wild-type
R209A
-
Km (N-acetyl-L-glutamate) similar to wild-type, kcat similar to wild-type, IC50 (L-arginine) 46fold increased compared to wild-type
R209K
-
Km (N-acetyl-L-glutamate) similar to wild-type, kcat similar to wild-type, IC50 (L-arginine) 37fold increased compared to wild-type
W23A
-
Km (N-acetyl-L-glutamate) similar to wild-type, kcat similar to wild-type, IC50 (L-arginine) 4.5fold increased compared to wild-type
D162E
about 0.1% of wild-type activity
G11A
G11A does not hamper recombinant enzyme expression or purification. Mutant shows a 10fold decrease in Vmax values and it selectively increases 8fold the Km for ATP, affecting much less (3fold increase) the apparent Km for N-acetyl-L-glutamate
K8R
substantial although diminished activity
N158K
substantial although diminished activity
R66K
substantial although diminished activity
I106M
-
to increase phasing power, three additional amino acids codons are mutated to methionine (I106M, I294M and L367M). Crystals from this mutant protein are diffracted to 2.7 A
I294M
-
to increase phasing power, three additional amino acids codons are mutated to methionine (I106M, I294M and L367M). Crystals from this mutant protein are diffracted to 2.7 A
K356H
site-directed mutagenesis, inactive mutant
L367M
-
to increase phasing power, three additional amino acids codons are mutated to methionine (I106M, I294M and L367M). Crystals from this mutant protein are diffracted to 2.7 A
N391Q
site-directed mutagenesis, inactive mutant
R386K
site-directed mutagenesis, inactive mutant
S387A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y397F
site-directed mutagenesis, inactive mutant
E17A
-
site-directed mutagenesis, the mutant shows reduced Vmax, the mutation results in decreased affinity of NAGK for arginine
E17D
-
site-directed mutagenesis, the mutant shows reduced Vmax, the mutation results in decreased affinity of NAGK for arginine
E17Q
-
site-directed mutagenesis, the mutant shows reduced Vmax, the mutation results in decreased affinity of NAGK for arginine
E284D
-
site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates
G290A
-
site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates
H271N
-
site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates
K213
-
site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates
Q10A
-
site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates
R24E
-
site-directed mutagenesis, the mutant shows reduced Vmax , the mutation results in increased affinity of NAGK for arginine
Y21A
-
site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates
DELTA357-513
truncated mutant lacking C-terminal 150 amino acids (spanning residues 38-356), belonging to the DUF619 domain family, shows that is it stabilizes yNAGK, slows catalysis and modulates feed-back inhibition by arginine. Truncated yNAGK shows doubled kcat compared to wild-type, Km is almost not affected. IC50 (L-arginine) is lowered compared to wild-type. Truncated mutand shows lower thermal stability compared to wild-type
R233A
-
mutant does not interact in vitro with PII protein of wild-type sequence in yeast two-hybrid analysis. Mutant interacts with PII variants containing I86N or I86T mutation
E186A/E387A
to improve resolution in crystallization
E416A/K417A
to improve resolution in crystallization
E94A/K95A
to improve resolution in crystallization
K26A/E27A
to improve resolution in crystallization
K279A/E280A
to improve resolution in crystallization
K364H
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
K419A
to improve resolution in crystallization
N399Q
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R394K
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
S395A
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
Y405F
site-directed mutagenesis, inactive mutant
K364H
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
N399Q
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
R394K
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
S395A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
-
Y405F
-
site-directed mutagenesis, inactive mutant
-
E19R
-
Km and kcat (N-acetyl-L-glutamate) similar to wild-type, IC50 (L-arginine) approximately 55fold increased compared to wild-type
E19R
site-directed mutagenesis, the mutation increases the 50% inhibitoryL--arginine concentration significantly in vitro, which deregulates the feedback inhibition of CcNAGK by L-arginine in SYPA5-5 during the fermentation
H268N
-
Km and kcat (N-acetyl-L-glutamate) similar to wild-type, IC50 (L-arginine) approximately 55fold increased compared to wild-type
H268N
site-directed mutagenesis, the mutant strain shows accumulation of large amounts of pathway intermediates L-citrulline and L-ornithine and decreased production of L-arginine. Transcription levels of argGH decrease accompanied with the reduction of argininosuccinate synthase activity, which leads to the metabolic obstacle from L-citrulline to L-arginine
H268N
site-directed mutagenesis, the mutation increases the 50% inhibitoryL--arginine concentration significantly in vitro, which deregulates the feedback inhibition of CcNAGK by L-arginine in SYPA5-5 during the fermentation
H268N
-
the mutation significantly decreases the sensitivity of the enzyme to L-arginine and keeps the specific activity as compared to the wild type enzyme
H26E
-
Km and kcat (N-acetyl-L-glutamate) similar to wild-type, IC50 (L-arginine) approximately 55fold increased compared to wild-type
H26E
site-directed mutagenesis, the mutation increases the 50% inhibitoryL--arginine concentration significantly in vitro, which deregulates the feedback inhibition of CcNAGK by L-arginine in SYPA5-5 during the fermentation
R209A
site-directed mutagenesis, the mutant strain shows accumulation of large amounts of pathway intermediates L-citrulline and L-ornithine and decreased production of L-arginine. Transcription levels of argGH decrease accompanied with the reduction of argininosuccinase activity, which leads to the metabolic obstacle from L-citrulline to L-arginine
R209A
site-directed mutagenesis, the mutation increases the 50% inhibitoryL--arginine concentration significantly in vitro, which deregulates the feedback inhibition of CcNAGK by L-arginine in SYPA5-5 during the fermentation
R209A
-
the mutation significantly decreases the sensitivity of the enzyme to L-arginine and keeps the specific activity as compared to the wild type enzyme
H268N
-
the mutation significantly decreases the sensitivity of the enzyme to L-arginine and keeps the specific activity as compared to the wild type enzyme
-
H268N
-
site-directed mutagenesis, the mutant strain shows accumulation of large amounts of pathway intermediates L-citrulline and L-ornithine and decreased production of L-arginine. Transcription levels of argGH decrease accompanied with the reduction of argininosuccinate synthase activity, which leads to the metabolic obstacle from L-citrulline to L-arginine
-
H268N
-
site-directed mutagenesis, the mutation increases the 50% inhibitoryL--arginine concentration significantly in vitro, which deregulates the feedback inhibition of CcNAGK by L-arginine in SYPA5-5 during the fermentation
-
R209A
-
the mutation significantly decreases the sensitivity of the enzyme to L-arginine and keeps the specific activity as compared to the wild type enzyme
-
R209A
-
site-directed mutagenesis, the mutant strain shows accumulation of large amounts of pathway intermediates L-citrulline and L-ornithine and decreased production of L-arginine. Transcription levels of argGH decrease accompanied with the reduction of argininosuccinase activity, which leads to the metabolic obstacle from L-citrulline to L-arginine
-
R209A
-
site-directed mutagenesis, the mutation increases the 50% inhibitoryL--arginine concentration significantly in vitro, which deregulates the feedback inhibition of CcNAGK by L-arginine in SYPA5-5 during the fermentation
-
additional information
construction of feedback inhibition deregulated Corynebacterium crenatum mutant strains, phenotypes, overview
additional information
-
construction of feedback inhibition deregulated Corynebacterium crenatum mutant strains, phenotypes, overview
additional information
-
construction of feedback inhibition deregulated Corynebacterium crenatum mutant strains, phenotypes, overview
-
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
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Baich, A.; Vogel, H.J.
N-acetyl-gamma-glutamokinase and N-acetylglutamic gamma-semialdehyde dehydrogenase: Repressible enzymes of arginine synthesis in Escherichia coli
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N-Acetylglutamate-5-phosphotransferase
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Acetylglutamate kinase. A mitochondrial feedback-sensitive enzyme of arginine biosynthesis in Neurospora crassa
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Purification and characterization of N-acetylglutamate 5-phosphotransferase from pea (Pisum sativum) cotyledons
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331
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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
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2002
Pseudomonas aeruginosa
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Structure of acetylglutamate kinase, a key enzyme for arginine biosynthesis and a prototype for the amino acid kinase enzyme family, during catalysis
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10
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Escherichia coli
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Arginine biosynthesis in Thermotoga maritima: characterization of the arginine-sensitive N-acetyl-L-glutamate kinase
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Complex formation and catalytic activation by the PII signaling protein of N-acetyl-L-glutamate kinase from Synechococcus elongatus strain PCC 7942
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Arabidopsis thaliana, Arabidopsis thaliana (Q9SCL7)
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Ramon-Maiques, S.; Fernandez-Murga, M.L.; Gil-Ortiz, F.; Vagin, A.; Fita, I.; Rubio, V.
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Pseudomonas aeruginosa (Q9HTN2), Pseudomonas aeruginosa, Thermotoga maritima (Q9X2A4), Thermotoga maritima
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The crystal structure of the complex of PII and acetylglutamate kinase reveals how PII controls the storage of nitrogen as arginine
Proc. Natl. Acad. Sci. USA
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Synechococcus elongatus (Q6V1L5), Synechococcus elongatus
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Wu, C.W.; Li, L.F.; Liu, X.; Gao, X.Z.; Lei, J.; Su, X.D.; Zhao, X.; Liang, Y.H.
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Streptococcus mutans
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Fernandez-Murga, M.L.; Rubio, V.
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Feria Bourrellier, A.; Ferrario-Mry, S.; Vidal, J.; Hodges, M.
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Arabidopsis thaliana
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Min, L.; Jin, Z.; Caldovic, L.; Morizono, H.; Allewell, N.M.; Tuchman, M.; Shi, D.
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Arabidopsis thaliana, Pseudomonas aeruginosa (Q9HTN2)
brenda
Beez, S.; Fokina, O.; Herrmann, C.; Forchhammer, K.
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Synechococcus elongatus, Arabidopsis thaliana (Q9SCL7), Arabidopsis thaliana
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Shi, D.; Li, Y.; Cabrera-Luque, J.; Jin, Z.; Yu, X.; Zhao, G.; Haskins, N.; Allewell, N.M.; Tuchman, M.
A novel N-acetylglutamate synthase architecture revealed by the crystal structure of the bifunctional enzyme from Maricaulis maris
PLoS ONE
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Maricaulis maris
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Xu, M.; Rao, Z.; Dou, W.; Yang, J.; Jin, J.; Xu, Z.
Site-directed mutagenesis and feedback-resistant N-acetyl-L-glutamate kinase (NAGK) increase Corynebacterium crenatum L-arginine production
Amino Acids
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2012
Corynebacterium crenatum
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Xu, M.; Rao, Z.; Dou, W.; Jin, J.; Xu, Z.
Site-directed mutagenesis studies on the L-arginine-binding sites of feedback inhibition in N-acetyl-L-glutamate kinase (NAGK) from Corynebacterium glutamicum
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Corynebacterium glutamicum
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Fokina, O.; Chellamuthu, V.R.; Zeth, K.; Forchhammer, K.
A novel signal transduction protein P(II) variant from Synechococcus elongatus PCC 7942 indicates a two-step process for NAGK-P(II) complex formation
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Synechococcus elongatus
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Gil-Ortiz, F.; Ramon-Maiques, S.; Fernandez-Murga, M.L.; Fita, I.; Rubio, V.
Two crystal structures of Escherichia coli N-acetyl-L-glutamate kinase demonstrate the cycling between open and closed conformations
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Escherichia coli (A0A140NEG9), Escherichia coli
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Marcos, E.; Crehuet, R.; Bahar, I.
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Escherichia coli
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de Cima, S.; Gil-Ortiz, F.; Crabeel, M.; Fita, I.; Rubio, V.
Insight on an arginine synthesis metabolon from the tetrameric structure of yeast acetylglutamate kinase
PLoS ONE
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Saccharomyces cerevisiae (Q01217), Saccharomyces cerevisiae
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Van de Casteele, M.; Demarez, M.; Legrain, C.; Glansdorff, N.; Pierard, A.
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Saccharolobus solfataricus, Saccharolobus solfataricus P1
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Zhao, G.; Haskins, N.; Jin, Z.; M Allewell, N.; Tuchman, M.; Shi, D.
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Maricaulis maris (Q0ASS9), Maricaulis maris, Maricaulis maris MCS10 (Q0ASS9), Xanthomonas campestris (A0A0H2X8L7), Xanthomonas campestris 8004 (A0A0H2X8L7)
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Zhao, Q.; Luo, Y.; Dou, W.; Zhang, X.; Zhang, X.; Zhang, W.; Xu, M.; Geng, Y.; Rao, Z.; Xu, Z.
Controlling the transcription levels of argGH redistributed L-arginine metabolic flux in N-acetylglutamate kinase and ArgR-deregulated Corynebacterium crenatum
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Corynebacterium crenatum (Q6R6P5), Corynebacterium crenatum, Corynebacterium crenatum SYPA5-5 (Q6R6P5), Corynebacterium crenatum SYPA5-5
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Yang, X.
Conformational dynamics play important roles upon the function of N-acetylglutamate kinase
Appl. Microbiol. Biotechnol.
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3485-3492
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Escherichia coli (P0A6C8), Corynebacterium glutamicum (Q59281), Pseudomonas aeruginosa (Q9HTN2), Thermotoga maritima (Q9X2A4), Corynebacterium glutamicum ATCC 13032 (Q59281)
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Liu, W.; Xiang, Y.; Zhang, X.; Han, G.; Sun, X.; Sheng, Y.; Yan, J.; Scheller, H.V.; Zhang, A.
Over-expression of a maize N-acetylglutamate kinase gene (ZmNAGK) improves drought tolerance in tobacco
Front. Plant Sci.
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1902
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Zea mays (A0A1D6E3W6), Zea mays
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Zhao, Q.; Luo, Y.; Dou, W.; Zhang, X.; Zhang, X.; Zhang, W.; Xu, M.; Geng, Y.; Rao, Z.; Xu, Z.
Controlling the transcription levels of argGH redistributed L-arginine metabolic flux in N-acetylglutamate kinase and ArgR-deregulated Corynebacterium crenatum
J. Ind. Microbiol. Biotechnol.
43
55-66
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Corynebacterium crenatum, Corynebacterium crenatum SYPA5-5
brenda
Huang, J.; Chen, D.; Yan, H.; Xie, F.; Yu, Y.; Zhang, L.; Sun, M.; Peng, X.
Acetylglutamate kinase is required for both gametophyte function and embryo development in Arabidopsis thaliana
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642-656
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Arabidopsis thaliana (Q9SCL7), Arabidopsis thaliana
brenda
Ohashi, M.; Nasuno, R.; Isogai, S.; Takagi, H.
High-level production of ornithine by expression of the feedback inhibition-insensitive N-acetyl glutamate kinase in the sake yeast Saccharomyces cerevisiae
Metab. Eng.
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1-9
2020
Saccharomyces cerevisiae, Saccharomyces cerevisiae K901
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