Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
175
3-aminopentanedioate
-
pH 7.0, 37°C
0.35 - 62.5
hydroxylamine
2.8
NH4Cl
-
second value 8.9 mM, biphasic plot
additional information
hydroxylamine
0.0000597
ADP
-
gamma-glutamyl transferase assay
0.00091
ADP
pH 6.0, 35°C, recombinant mutant R64G
0.00461
ADP
pH 6.0, 35°C, recombinant mutant E60A
0.00865
ADP
pH 6.0, 35°C, recombinant wild-type enzyme
0.01
ADP
-
transferase activity
0.0113
ADP
pH 6.0, 35°C, recombinant mutant E60A/R64G
0.09
ADP
pH 6.4, 37°C, wild-type enzyme
0.05
ATP
D51A mutant, pH 7.0, 30°C
0.06
ATP
-
isozyme GSIII-1, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity
0.07
ATP
D51S mutant, pH 7.0, 30°C
0.07
ATP
-
isozyme GSIII-2, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity
0.1
ATP
-
enzyme from strain SA0, pH 6.8
0.12
ATP
D51N mutant, pH 7.0, 30°C
0.13
ATP
-
enzyme from strain SA0, pH 7.5
0.17
ATP
-
enzyme from strain SA1, pH 6.8
0.2
ATP
-
wild-type enzyme
0.2
ATP
-
in the presence of Mg2+
0.21
ATP
-
enzyme from strain SA1, pH 7.5
0.21
ATP
wild type enzyme, pH 7.0, 30°C
0.22
ATP
-
biosynthetic assay
0.25
ATP
-
oxidized mutant enzyme E165C
0.26
ATP
-
reduced mutant enzyme E165C
0.3
ATP
-
wild type enzyme, pH 7.5, 37°C
0.3
ATP
-
wild-type and mutant enzyme, pH 7.5, 37°C
0.3
ATP
pH 7.8, 30°C, isoenzyme GLN1,1
0.38
ATP
recombinant enzyme, coupled reactions assay, pH and temperature not specified in the publication
0.39
ATP
recombinant enzyme, Malachite green assay, pH and temperature not specified in the publication
0.43
ATP
-
enzyme form GSIII
0.45
ATP
30°C, isoenzyme OsGLN1,1
0.45
ATP
-
isozyme GSI, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity
0.53
ATP
-
biosynthetic assay, Mg2+-activated, enzyme form EII
0.53
ATP
30°C, isoenzyme OsGLN1,2
0.56
ATP
pH 7.8, 30°C, isoenzyme GLN1,4
0.85
ATP
pH 7.8, 30°C, isoenzyme GLN1,3
1
ATP
-
D56E mutant enzyme, pH 7.5, 37°C
1.1
ATP
pH 7.8, 30°C, isoenzyme GLN1,2
1.2
ATP
-
mutant E304H, 25°C, pH not specified in the publication
1.2
ATP
pH 7.0, temperature not specified in the publication, mutant E304A
1.3
ATP
-
short isoform, pH 7.2, 37°C
1.3
ATP
-
pH 11.0, 30 mM Mg2+
1.4
ATP
-
pH 8.0, 3 mM Mn2+
1.4
ATP
-
pH 8.5, 30 mM Mg2+
1.5
ATP
-
Mg2+-stimulated
1.5
ATP
-
ATP, biosynthetic assay, Mn2+-activated, enzyme form EII
1.5
ATP
-
pH 7.5, 3 mM MN2+
1.5
ATP
-
pH 8.5, 3 mM Mn2+
1.6
ATP
-
D56A mutant enzyme, pH 7.5, 37°C
1.7
ATP
-
Mg2+-stimulated
1.8
ATP
-
synthetase assay
1.83
ATP
pH not specified in the publication, 30°C, wild-type mature enzyme
1.9
ATP
-
long isoform, pH 7.2, 37°C
1.91
ATP
-
isozyme GSIII-1, pH 7.5, 37°C, glutamine synthetase activity
1.95
ATP
pH not specified in the publication, 30°C, mutant mature enzyme lacking the C-terminal peptide
2
ATP
-
Mg2+-stimulated or Mn2+-stimulated
2
ATP
-
pH 8.0, 30 mM Mg2+
2.3
ATP
-
Mn2+-stimulated
2.3
ATP
-
ATP, Mg2+-stimulated
2.3
ATP
pH 7.0, temperature not specified in the publication, mutant R62A
2.4
ATP
-
wild-type enzyme
2.4
ATP
-
wild-type, 25°C, pH not specified in the publication
2.4
ATP
pH 7.0, temperature not specified in the publication, wild-type enzyme
2.5
ATP
-
L-Glu, Mg2+-stimulated
2.5
ATP
-
Mn2+-stimulated
2.5
ATP
-
mutant enzyme S186F
2.65
ATP
-
isozyme GSIII-2, pH 7.5, 37°C, glutamine synthetase activity
2.9
ATP
-
biosynthetic assay, Mg2+-activated, enzyme form EI
2.9
ATP
-
phosphorylated GS1a, in the presence of 0.0005 mM microcystin
3
ATP
-
chloroplast enzyme
3
ATP
-
non-phosphorylated GS1a, in the presence of 0.0005 mM microcystin
4.5
ATP
pH 6.4, 37°C, wild-type enzyme
5.3
ATP
-
mutant G302A, 25°C, pH not specified in the publication
6.45
ATP
pH 6.4, 37°C, mutant enzyme E380A
9.4
ATP
-
mutant Y303H, 25°C, pH not specified in the publication
10.6
ATP
D51E mutant, pH 7.0, 30°C
11
ATP
-
mutant E304D, 25°C, pH not specified in the publication
500
ethylamine
-
pH 8.5, 3 mM Mn2+
700
ethylamine
-
pH 11.0, 30 mM Mg2+
4.9
Gln
-
-
11.6
Gln
-
glutamyl transferase reaction
37.6
Gln
-
transferase assay
48.6
Gln
-
gamma-glutamyl transferase assay
0.9
Glu
-
enzyme form GSIII
3
Glu
-
ATP, biosynthetic assay, Mn2+-activated, enzyme form EI
6.3
Glu
-
biosynthetic assay
6.7
Glu
-
synthetase assay
8.58
Glu
-
biosynthetic assay
13.3
Glu
-
enzyme form GSIII
14
Glu
-
hydroxylamine, glutamyl transferase assay
1.4
glutamate
-
enzyme from strain SA0, pH 6.8
1.7
glutamate
-
enzyme from strain SA0, pH 7.5
5.71
glutamate
-
pH 7.4, 35°C
9.2
glutamate
-
enzyme from strain SA1, pH 6.8
16.8
glutamate
-
enzyme from strain SA1, pH 7.5
0.35
hydroxylamine
-
Mn2+-activated, enzyme form EII
0.4
hydroxylamine
-
Mn2+-activated, enzyme form EI
0.68
hydroxylamine
-
mutant E304H, 25°C, pH not specified in the publication
0.68
hydroxylamine
pH 7.0, temperature not specified in the publication, mutant E304A
0.74
hydroxylamine
-
mutant E304D, 25°C, pH not specified in the publication
0.83
hydroxylamine
-
wild-type, 25°C, pH not specified in the publication
0.83
hydroxylamine
pH 7.0, temperature not specified in the publication, wild-type enzyme
0.85
hydroxylamine
pH not specified in the publication, 30°C, mutant mature enzyme lacking the C-terminal peptide
0.92
hydroxylamine
pH not specified in the publication, 30°C, wild-type mature enzyme
1.04
hydroxylamine
-
isozyme GSIII-1, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity
1.4
hydroxylamine
pH 7.0, temperature not specified in the publication, mutant R62A
1.5
hydroxylamine
pH 6.4, 37°C, mutant enzyme E380A
1.92
hydroxylamine
-
isozyme GSIII-2, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity
2.6
hydroxylamine
-
glutamyltransferase reaction
2.7
hydroxylamine
-
isozyme GSI, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity
2.9
hydroxylamine
-
wild-type enzyme
3.37
hydroxylamine
-
gamma-glutamyl transferase assay
3.4
hydroxylamine
-
mutant enzyme S186F
4.1
hydroxylamine
-
transferase reaction
4.7
hydroxylamine
pH 6.4, 37°C, wild-type enzyme
5.3
hydroxylamine
-
enzyme form GSIII
6
hydroxylamine
-
transferase activity
8.3
hydroxylamine
-
pH 7.0
10.5
hydroxylamine
-
at 45°C
11.1
L-Gln
-
glutamyl transferase reaction
12
L-Gln
-
transferase activity
12.6
L-Gln
-
biosynthetic reaction
22.2
L-Gln
-
transferase reaction
0.0025
L-Glu
-
in the presence of Mg2+
0.67
L-Glu
isoenzyme GLN1,4
0.83
L-Glu
mutant A174S of isoenzyme GLN1,4
1.1
L-Glu
-
Mg2+-stimulated
1.14
L-Glu
mutant K49Q of isoenzyme GLN1,4
1.3
L-Glu
-
Mn2+-stimulated
1.43
L-Glu
mutant K49Q/A174S of isoenzyme GLN1,4
1.8
L-Glu
-
phosphorylated GS1a, in the presence of 0.0005 mM microcystin
2.1
L-Glu
-
Mn2+-stimulated
2.1
L-Glu
-
Gln, transferase reaction
2.1
L-Glu
30°C, isoenzyme OsGLN1,2
2.4
L-Glu
mutant K49Q/A174S of isoenzyme GLN1,3
2.8
L-Glu
-
non-phosphorylated GS1a, in the presence of 0.0005 mM microcystin
3.2
L-Glu
mutant A174S of isoenzyme GLN1,3
3.2
L-Glu
mutant K49Q of isoenzyme GLN1,3
3.3
L-Glu
-
wild-type enzyme
3.4
L-Glu
-
synthetase reaction
4.17
L-Glu
isoenzyme GLN1,3
6
L-Glu
-
oxidized mutant enzyme E165C
7
L-Glu
-
reduced mutant enzyme E165C
17
L-Glu
-
biosynthetic assay, Mg2+-activated, enzyme form I or Mn2+-activated, enzyme form EII.
18
L-Glu
-
Mg2+-stimulated
18
L-Glu
-
L-Glu, biosynthetic assay, Mg2+-activated, enzyme form EII
21
L-Glu
-
Mg2+-stimulated
25
L-Glu
-
Mg2+-stimulated
0.32
L-glutamate
D51A mutant, pH 7.0, 30°C
0.37
L-glutamate
D51S mutant, pH 7.0, 30°C
0.44
L-glutamate
recombinant enzyme, coupled reactions assay, pH and temperature not specified in the publication
0.47
L-glutamate
recombinant enzyme, Malachite green assay, pH and temperature not specified in the publication
0.6
L-glutamate
pH 7.8, 30°C, isoenzyme GLN1,4
0.85
L-glutamate
D51N mutant, pH 7.0, 30°C
1 - 4
L-glutamate
pH 7.0, temperature not specified in the publication, mutant R62A
1.1
L-glutamate
-
short isoform, pH 7.2, 37°C
1.1
L-glutamate
pH 7.8, 30°C, isoenzyme GLN1,1
1.3
L-glutamate
-
long isoform, pH 7.2, 37°C
1.5
L-glutamate
wild type enzyme, pH 7.0, 30°C
1.7 - 2
L-glutamate
-
isozyme GSIII-2, pH 7.5, 37°C, glutamine synthetase activity
1.9
L-glutamate
30°C, isoenzyme OsGLN1,1
2
L-glutamate
-
mutant enzyme, pH 7.5, 37°C
3.4
L-glutamate
-
mutant E304H, 25°C, pH not specified in the publication
3.4
L-glutamate
pH 7.0, temperature not specified in the publication, mutant E304A
3.8
L-glutamate
pH 7.8, 30°C, isoenzyme GLN1,2
3.9
L-glutamate
pH 7.8, 30°C, isoenzyme GLN1,3
5.7
L-glutamate
pH not specified in the publication, 30°C, wild-type mature enzyme
7
L-glutamate
-
wild-type enzyme, pH 7.5, 37°C
7
L-glutamate
-
wild type enzyme, pH 7.5, 37°C
8.58
L-glutamate
-
isozyme GSIII-1, pH 7.5, 37°C, glutamine synthetase activity
10
L-glutamate
-
mutant E304D, 25°C, pH not specified in the publication
11.52
L-glutamate
pH not specified in the publication, 30°C, mutant mature enzyme lacking the C-terminal peptide
16
L-glutamate
D51E mutant, pH 7.0, 30°C
18
L-glutamate
-
D56E mutant enzyme, pH 7.5, 37°C
22
L-glutamate
-
chloroplast enzyme
23.5
L-glutamate
60°C, pH 7.8
26.3
L-glutamate
recombinant enzyme, pH 7.8, 37°C
27
L-glutamate
-
wild-type enzyme
27
L-glutamate
-
wild-type, 25°C, pH not specified in the publication
27
L-glutamate
pH 7.0, temperature not specified in the publication, wild-type enzyme
29
L-glutamate
-
mutant enzyme S186F
38
L-glutamate
-
D56A mutant enzyme, pH 7.5, 37°C
58
L-glutamate
pH 7.0, 60°C
59
L-glutamate
-
mutant Y303H, 25°C, pH not specified in the publication
84
L-glutamate
-
mutant G302A, 25°C, pH not specified in the publication
104
L-glutamate
-
pH 7.0, 37°C
0.00673
L-glutamine
pH 6.0, 35°C, recombinant mutant E60A/R64G
0.00888
L-glutamine
pH 6.0, 35°C, recombinant mutant E60A
0.00982
L-glutamine
pH 6.0, 35°C, recombinant mutant R64G
0.012
L-glutamine
pH 6.0, 35°C, recombinant wild-type enzyme
0.62
L-glutamine
-
isozyme GSIII-2, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity
1.3
L-glutamine
-
isozyme GSIII-1, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity
1.93
L-glutamine
-
isozyme GSI, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity
6.8
L-glutamine
pH 6.4, 37°C, wild-type enzyme
13
L-glutamine
-
wild-type enzyme
14
L-glutamine
-
mutant enzyme S186F
20
methylamine
-
pH 8.0, 3 mM Mn2+
100
methylamine
-
pH 8.5, 30 mM Mg2+
0.18
NH3
-
wild-type, 25°C, pH not specified in the publication
0.18
NH3
pH 7.0, temperature not specified in the publication, wild-type enzyme
0.34
NH3
pH 7.0, temperature not specified in the publication, mutant R62A
0.43
NH3
-
isozyme GSIII-2, pH 7.5, 37°C, glutamine synthetase activity
0.48
NH3
-
isozyme GSIII-1, pH 7.5, 37°C, glutamine synthetase activity
32
NH3
-
mutant E304H, 25°C, pH not specified in the publication
32
NH3
pH 7.0, temperature not specified in the publication, mutant E304A
120
NH3
-
mutant E304D, 25°C, pH not specified in the publication
0.004
NH4+
-
enzyme from strain SA0, pH 6.8
0.01
NH4+
pH 7.8, 30°C, below, isoenzyme GLN1,1
0.0125
NH4+
-
biosynthetic assay
0.013
NH4+
-
D56E mutant enzyme, pH 7.5, 37°C
0.015
NH4+
-
enzyme from strain SA0, pH 7.5
0.02
NH4+
-
D56A mutant enzyme, pH 7.5, 37°C
0.02 - 0.05
NH4+
-
isoforms GSI and GSII
0.025
NH4+
-
wild type enzyme, pH 7.5, 37°C
0.027
NH4+
30°C, isoenzyme OsGLN1,1
0.028
NH4+
-
pH 7.4, 35°C
0.042
NH4+
-
in the presence of Mg2+
0.05
NH4+
wild type enzyme, pH 7.0, 30°C
0.073
NH4+
30°C, isoenzyme OsGLN1,2
0.119
NH4+
mutant A174S of isoenzyme GLN1,4
0.12
NH4+
isoenzyme GLN1,4
0.18
NH4+
-
Mg2+-stimulated
0.19
NH4+
-
enzyme form GSIII
0.2
NH4+
-
biosynthetic assay
0.2
NH4+
-
NH4+, biosynthetic assay, Mg2+-activated, enzyme form EII
0.334
NH4+
mutant A174S of isoenzyme GLN1,3
0.4
NH4+
-
chloroplast enzyme
0.45
NH4+
mutant K49Q of isoenzyme GLN1,3
0.453
NH4+
mutant K49Q of isoenzyme GLN1,4
0.456
NH4+
mutant K49Q/A174S of isoenzyme GLN1,3
0.48
NH4+
-
biosynthetic assay, Mn2+-stimulated, enzyme form EI
0.55
NH4+
D51E mutant, pH 7.0, 30°C
0.56
NH4+
-
Mg2+-stimulated
0.56
NH4+
-
hydroxylamine, Mg2+-activated, enzyme form EII
0.56
NH4+
-
pH 8.0, 30 mM Mg2+
0.58
NH4+
pH 7.8, 30°C, below, isoenzyme GLN1,4
0.59
NH4+
-
Mg2+-stimulated
0.59
NH4+
-
pH 7.5, 3 mM MN2+
0.69
NH4+
-
Mn2+-stimulated
0.69
NH4+
-
NH4+, Mg2+-stimulated
0.71
NH4+
-
Mn2+-stimulated
0.736
NH4+
mutant K49Q/A174S of isoenzyme GLN1,4
0.77
NH4+
-
Mn2+-stimulated
0.78
NH4+
recombinant enzyme, Malachite green assay, pH and temperature not specified in the publication
0.79
NH4+
recombinant enzyme, coupled reactions assay, pH and temperature not specified in the publication
0.92
NH4+
D51N mutant, pH 7.0, 30°C
1.21
NH4+
pH 7.8, 30°C, below, isoenzyme GLN1,3
1.33
NH4+
isoenzyme GLN1,3
1.4
NH4+
-
enzyme from strain SA1, pH 7.5
2.45
NH4+
pH 7.8, 30°C, below, isoenzyme GLN1,2
5.95
NH4+
D51S mutant, pH 7.0, 30°C
12.4
NH4+
-
enzyme from strain SA1, pH 6.8
12.45
NH4+
D51A mutant, pH 7.0, 30°C
33
NH4+
-
enzyme form GSIII
additional information
hydroxylamine
the Km value of GlnA for hydroxylamine is higher when a high concentration was used (5 to 30mM), 60°C, pH 7.8
additional information
hydroxylamine
-
the Km value of GlnA for hydroxylamine is higher when a high concentration was used (5 to 30mM), 60°C, pH 7.8
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
ADP-ribosylation of glutamine synthetase could be an alternative modification to adenylylation to regulate glutamine synthetase activity
-
additional information
additional information
-
Km-values of wild-type and mutant enzymes D50A, D50E, E327A
-
additional information
additional information
-
the enzyme is modulated by a closed bicyclic covalent interconvertible cascade. It consists of two protein nucleotidylation cycles. One involves the cyclic adenylylation and deadenylylation of glutamine synthetase, the other involves the uridylylation and deuridylylation of Shapiro´s regulatory protein PII
-
additional information
additional information
-
the site of ADP-ribosylation is Arg172
-
additional information
additional information
-
enzyme activity is controlled by adenylylation
-
additional information
additional information
-
enzyme activity is controlled by adenylylation
-
additional information
additional information
-
Km for Gln and Glu increases after adenylylation
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
the enzymatic rate of GS enzymes shows a hyperbolic curve typical of the enzymes that follow the Michaelis-Menten equation regarding the ATP and glutamate and a sigmoidal curve relative to the hydroxylamine concentration
-
additional information
additional information
-
the enzymatic rate of GS enzymes shows a hyperbolic curve typical of the enzymes that follow the Michaelis-Menten equation regarding the ATP and glutamate and a sigmoidal curve relative to the hydroxylamine concentration
-