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0.0003
-
mutant D165N overexpressed at 8°C
0.012
-
2-oxoglutarate, mutant M101K
0.014
-
2-oxoglutarate, mutant K80R
0.019
-
2-oxoglutarate, mutant G82R and M101S
0.026
-
2-oxoglutarate, mutant G82K
0.034
-
mutant D165N overexpressed at 37°C
0.047
-
mutant D165N overexpressed at 23°C
0.0495 - 0.133
-
pH 8.2, 30°C
0.077
NADP-linked GDH activity
0.21
-
on L-aspartate, mutant M101S
0.29
-
mutant enzyme W244S, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
0.32
-
wild type enzyme, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
0.34
-
mutant enzyme W244S, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
0.39
-
on L-aspartate, mutant G82K
0.49
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH using NAD+
0.5
-
mutant enzyme W244S, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
0.51
-
mutant enzyme W244S, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
0.62
recombinant enzyme from crude cell extract, at 25°C
0.73
-
wild type enzyme, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
0.77
NAD-linked GDH activity
0.84
-
with alkalized extract from the tuber of Corydalis ternata
0.87
-
mutant enzyme D245K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
0.9
-
mutant enzyme E243R, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
0.97
in the presence of antibiotics and ammonia
1.12
-
mutant enzyme D245K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
1.14
-
mutant enzyme D245K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
1.23
-
wild type enzyme, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
1.32
-
wild type enzyme, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
1.53
-
mutant enzyme D245K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
1.83
-
mutant enzyme E243R, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
101.8
-
mutant enzyme D245K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
102
-
mutant enzyme E243D, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
11
-
mutant enzyme E243R, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
119.5
-
in the presence of 0.1 mM Hg
12
-
mutant enzyme E243R, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
12.5
-
mutant enzyme D245K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
15
-
mutant enzyme E243D, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
155
-
wild type enzyme, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
17.6
-
mutant enzyme E243K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
170.6
-
in the presence of 0.1 mM Hg and in the presence of 5 mM glutamine
171.4
-
in the presence of 0.1 mM Hg and in the presence of 0.1 mM AlCl3
174
-
wild type enzyme, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
19
-
mutant enzyme E243K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
19.7
-
in the absence of Hg and in the presence of 0.1 mM AlCl3
2.16
-
mutant enzyme D245K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
2.26
-
mutant enzyme E243R, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
2.3
-
mutant enzyme E243R, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
2.98
-
mutant enzyme E243D, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
20
-
mutant enzyme W244S, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
20.1
-
mutant enzyme E243K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
20.6
-
wild type enzyme, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
243.4
-
in the presence of 0.1 mM Hg and in the presence of NH4NO3
25
-
in the presence of 0.001 mM Hg and in the presence of NH4NO3
25.3
-
mutant enzyme E243K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
26.7
-
in the presence of 0.001 mM Hg
3
-
mutant enzyme E243R, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
3.05
-
mutant enzyme E243R, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
3.1
purified recombinant enzyme, at 25°C
3.27
-
mutant enzyme E243K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
3.41
-
mutant enzyme E243R, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
3.54
-
recombinant, urea-activated enzyme
3.65
-
recombinant, heat-activated enzyme
3.82
-
mutant enzyme W244S, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
30
-
mutant enzyme D245K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
328.2
-
in the presence of 0.1 mM Hg and in the presence of 5 mM sucrose
34
-
mutant enzyme E243D, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
34.2
-
in the absence of Hg
35
recombinant enzyme purified from Haloferax volcanii, pH 8.5, 40°C
4.1
-
mutant enzyme E243R, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
4.93
-
mutant enzyme E243D, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
440
-
2-oxoglutarate, wild-type
5
-
mutant enzyme E243D, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
5.2
-
mutant enzyme E243K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
5.8
-
mutant enzyme D245K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
50
-
wild type enzyme, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
52.9
-
in the absence of Hg and in the presence of 5 mM sucrose
54.6
-
in the presence of 0.01 mM Hg
56
-
mutant enzyme E243K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
56.5
-
mutant enzyme W244S, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
58
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH using NADP+
58.6
-
in the absence of Hg and in the presence of 5 mM glutathione
59.4
-
in the absence of Hg and in the presence of 5 mM glutamine
6.52
recombinant enzyme in Haloferax volcanii, pH 8.5, 40°C
6.78
-
mutant enzyme W244S, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
62
-
mutant enzyme W244S, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
65.8
-
in the absence of Hg and in the presence of NH4NO3
68
-
mutant enzyme D245K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
7.2
-
mutant enzyme E243D, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
70.94
-
in the presence of 0.1 mM Hg and in the presence of 5 mM glutathione
72
-
in the presence of 0.01 mM Hg and in the presence of NH4NO3
89.3
purified recombinant enzyme
9.01
-
mutant enzyme E243K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
9.6
-
mutant enzyme E243K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
9.8
-
wild type enzyme, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
90
-
mutant enzyme E243D, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
0.33
-
mutant enzyme W244S, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
0.33
-
wild type enzyme, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
1.47
-
mutant enzyme E243D, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
1.47
-
mutant enzyme E243D, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
104
-
GDH II
104
purified native enzyme
248
-
-
248
-
NAD+-dependent enzyme
54
-
GDH-II
54
-
mutant enzyme E243K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
additional information
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additional information
Apodachlya sp.
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additional information
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additional information
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additional information
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additional information
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additional information
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additional information
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glucose withdrawal stimulates GDH activity
additional information
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additional information
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additional information
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additional information
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additional information
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additional information
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additional information
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additional information
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additional information
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GDH activity is markedly increased in Pseudomonas fluorescens cultures exposed to menadione-containing media containing Arg, Glu and Pro. When NH4+ is utilized as the nitrogen source, both alpha-ketoglutarate dehydrogenase and GDH levels are diminished. These enzymatic profiles are reversed when control cells are incubated in menadione media
additional information
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additional information
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additional information
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additional information
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additional information
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