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0.0008 - 606
2-oxoglutarate
0.000011 - 1349
L-glutamate
additional information
additional information
-
0.0008
2-oxoglutarate
pH 8.5, 40°C, recombinant enzyme in presence of DMSO
0.00111
2-oxoglutarate
-
animals treated with alkalized extract from the tuber of Corydalis ternata
0.00131
2-oxoglutarate
-
animals treated with protopine
0.00138
2-oxoglutarate
-
control group
0.0034
2-oxoglutarate
pH 8.5, 40°C, recombinant enzyme
0.041
2-oxoglutarate
pH 6.5, 25°C, recombinant enzyme, in presence of 10 mM L-aspartate
0.0862
2-oxoglutarate
-
mutant D165N
0.103
2-oxoglutarate
-
pH 7, 25°C
0.125
2-oxoglutarate
-
wild-type
0.65
2-oxoglutarate
-
wild-type
0.65
2-oxoglutarate
wild-type
0.75
2-oxoglutarate
-
activated NAD-GDH
0.92
2-oxoglutarate
-
pH 9.5, 50°C, recombinant enzyme
0.92
2-oxoglutarate
pH 9.5, 50°C
0.93
2-oxoglutarate
mutant E27F
1.22
2-oxoglutarate
mutant Q144R
1.9
2-oxoglutarate
-
non-activated NAD-GDH
2.36
2-oxoglutarate
-
NAD+-dependent enzyme
2.36
2-oxoglutarate
-
pH 8.0, 20°C
2.85
2-oxoglutarate
-
wild-type CsGDH, Vmax: 546 micromol/min/mg, pH 8.0, 25°C
3.12
2-oxoglutarate
-
pH 8.0, 23°C
5.6
2-oxoglutarate
-
pH 8.0
100
2-oxoglutarate
-
mutant M101S
285
2-oxoglutarate
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, 781 mM NH4Cl, Vmax: 2260 micromol/min/mg, pH 8.0, 25°C
606
2-oxoglutarate
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, 1800 mM NH4Cl, Vmax: 200 micromol/min/mg, pH 8.0, 25°C
5.82
glutamate
-
pH 7, 25°C
0.000011
L-glutamate
pH 9.0, 40°C, recombinant enzyme
0.000025
L-glutamate
pH 9.0, 40°C, recombinant enzyme in presence of DMSO
0.00299
L-glutamate
-
animals treated with protopine
0.00302
L-glutamate
-
animals treated with alkalized extract from the tuber of Corydalis ternata
0.00321
L-glutamate
-
control group
0.16
L-glutamate
-
native enzyme
0.16
L-glutamate
-
recombinant, heat-activated enzyme
0.18
L-glutamate
-
recombinant, urea-activated enzyme
0.34
L-glutamate
wild-type
0.39
L-glutamate
0.009 mM inhibitor biothionol, Vmax: 0.05, pH 7.5
1.06
L-glutamate
0.005 mM inhibitor biothionol, Vmax: 0.1, pH 7.5
1.17
L-glutamate
0.003 mM inhibitor biothionol, Vmax: 0.14, pH 7.5
1.27
L-glutamate
0.008 mM inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.05, pH 7.5
1.38
L-glutamate
0.0015 mM inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.13, pH 7.5
1.38
L-glutamate
without inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.17, pH 7.5
1.39
L-glutamate
-
wild-type CsGDH, Vmax: 47.1 micromol/min/mg, pH 8.0, 25°C
1.53
L-glutamate
0.004 mM inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.09, pH 7.5
1.62
L-glutamate
without inhibitor biothionol, Vmax: 0.18, pH 7.5
2.5 - 5
L-glutamate
pH 7.5, 25°C
2.5 - 5
L-glutamate
with NAD+, recombinant enzyme, pH and temperature not specified in the publication
2.66
L-glutamate
-
mutant D165N
3.25
L-glutamate
-
mutant enzyme W393F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C
3.25
L-glutamate
-
wild type enzyme, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C
3.3
L-glutamate
-
mutant enzyme W449F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C
3.41
L-glutamate
-
mutant enzyme W64F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C
3.7 - 5
L-glutamate
-
mutant enzyme W310F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C
3.97
L-glutamate
-
wild-type
5.1
L-glutamate
mutant C872R, pH 9.0, 25°C
5.2
L-glutamate
mutant C1141T, pH 9.0, 25°C
5.3
L-glutamate
-
pH 10.5, 50°C, recombinant enzyme
5.3
L-glutamate
pH 10.5, 50°C
5.4
L-glutamate
mutant C825G, pH 9.0, 25°C
6.1
L-glutamate
wild-type, pH 9.0, 25°C
6.8
L-glutamate
mutant D869A, pH 9.0, 25°C
7.1
L-glutamate
in the presence of 5 mM NAD+, in 100 mM glycine/NaOH (pH 9.5), at 25°C
7.2
L-glutamate
mutant V1139A, pH 9.0, 25°C
18.2
L-glutamate
-
mutant enzyme W243F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C
28.6
L-glutamate
-
NAD+-dependent enzyme
28.6
L-glutamate
-
pH 8.0, 20°C
33.33
L-glutamate
-
pH 8.0, 23°C
1349
L-glutamate
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 121.9 micromol/min/mg, pH 8.0, 25°C
0.018
NAD+
-
recombinant, urea-activated enzyme
0.019
NAD+
-
native enzyme
0.021
NAD+
-
recombinant, heat-activated enzyme
0.028
NAD+
-
pH 10.5, 50°C, recombinant enzyme
0.076
NAD+
-
mutant D165N
0.112
NAD+
pH 9.0, 40°C, recombinant enzyme in presence of DMSO
0.118
NAD+
pH 9.0, 40°C, recombinant enzyme
0.125
NAD+
-
wild type enzyme, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C
0.138
NAD+
-
mutant enzyme W393F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C
0.14
NAD+
0.008 mM inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.04, pH 7.5
0.168
NAD+
-
wild-type CsGDH, Vmax: 40.6 micromol/min/mg, pH 8.0, 25°C
0.22
NAD+
-
mutant enzyme W449F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C
0.23
NAD+
-
mutant enzyme W64F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C
0.23
NAD+
0.0015 mM inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.13, pH 7.5
0.26
NAD+
0.004 mM inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.09, pH 7.5
0.26
NAD+
0.009 mM inhibitor biothionol, Vmax: 0.05, pH 7.5
0.31
NAD+
without inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.24, pH 7.5
0.31
NAD+
without inhibitor biothionol, Vmax: 0.24, pH 7.5
0.35
NAD+
-
mutant enzyme W310F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C
0.36
NAD+
0.005 mM inhibitor biothionol, Vmax: 0.13, pH 7.5
0.4
NAD+
-
mutant enzyme W243F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C
0.43
NAD+
0.003 mM inhibitor biothionol, Vmax: 0.22, pH 7.5
0.5
NAD+
-
NAD+-dependent enzyme
1.2
NAD+
mutant C825G, pH 9.0, 25°C
1.2
NAD+
mutant V1139A, pH 9.0, 25°C
1.3
NAD+
wild-type, pH 9.0, 25°C
1.3
NAD+
mutant C872R, pH 9.0, 25°C
1.5
NAD+
mutant D869A, pH 9.0, 25°C
2.1
NAD+
in the presence of 20 mM L-glutamate, in 100 mM glycine/NaOH (pH 9.5), at 25°C
2.1
NAD+
mutant C1141T, pH 9.0, 25°C
0.001
NADH
-
pH 9.5, 50°C, recombinant enzyme
0.0044
NADH
-
wild type enzyme, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.0056
NADH
-
mutant D165N
0.0076
NADH
-
mutant enzyme W244S, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.009
NADH
pH 8.5, 40°C, recombinant enzyme in presence of DMSO
0.0123
NADH
-
mutant enzyme E243D, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.014
NADH
pH 8.5, 40°C, recombinant enzyme
0.018
NADH
-
mutant enzyme D245K, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.018
NADH
-
pH 6.0, 25°C, mutant P262S
0.02
NADH
-
pH 7.0, 25°C, recombinant wild-type enzyme
0.022
NADH
-
pH 6.0, 25°C, mutant D263K
0.023
NADH
-
pH 7.0, 25°C, mutant D263K
0.025
NADH
-
pH 7.0, 25°C, mutant A242G
0.028
NADH
-
pH 6.0, 25°C, mutant F238S
0.034
NADH
-
pH 6.0, 25°C, mutant A242G
0.035
NADH
-
pH 7.0, 25°C, mutant F238S/P262S
0.036
NADH
-
mutant enzyme E243K, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.036
NADH
-
pH 6.0, 25°C, recombinant wild-type enzyme
0.03609
NADH
-
control group
0.037
NADH
-
non-activated NAD-GDH
0.03785
NADH
-
animals treated with protopine
0.03833
NADH
-
animals treated with alkalized extract from the tuber of Corydalis ternata
0.0385
NADH
-
mutant enzyme E243R, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.04
NADH
-
pH 7.0, 25°C, mutant F238S
0.047
NADH
-
pH 7.0, 25°C, mutant P262S
0.048
NADH
-
pH 6.0, 25°C, mutant F238S/P262S
0.055
NADH
-
wild-type CsGDH, Vmax: 285 micromol/min/mg, pH 8.0, 25°C
0.078
NADH
-
pH 8.0, 25°C, recombinant wild-type enzyme
0.085
NADH
-
pH 8.0, 25°C, mutant A242G
0.09
NADH
-
activated NAD-GDH
0.091
NADH
-
mutant M101S
0.091
NADH
-
pH 8.0, 25°C, mutant D263K
0.142
NADH
-
pH 8.0, 25°C, mutant P262S
0.204
NADH
-
pH 8.0, 25°C, mutant F238S/P262S
0.23
NADH
-
pH 8.0, 25°C, mutant F238S
0.163
NADP+
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 80.8 micromol/min/mg, pH 8.0, 25°C
0.0384
NADPH
-
mutant enzyme E243R, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.053
NADPH
-
mutant enzyme E243K, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.238
NADPH
-
mutant enzyme D245K, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.431
NADPH
-
mutant enzyme W244S, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.476
NADPH
-
mutant enzyme E243D, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.51
NADPH
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 2180 micromol/min/mg, pH 8.0, 25°C
1.64
NADPH
-
wild type enzyme, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.00013
NH3
pH 8.5, 40°C, recombinant enzyme in presence of DMSO
0.00035
NH3
pH 8.5, 40°C, recombinant enzyme
9.8
NH3
-
pH 9.5, 50°C, recombinant enzyme
33.9
NH3
as NH4+, pH 6.5, 25°C, recombinant enzyme, in absence of L-aspartate
0.00528
NH4+
-
animals treated with alkalized extract from the tuber of Corydalis ternata
0.0054
NH4+
-
animals treated with protopine
0.00613
NH4+
-
control group
0.033
NH4+
-
for 200 mM NH4+
12.9
NH4+
-
wild-type CsGDH, Vmax: 307 micromol/min/mg, pH 8.0, 25°C
22.8
NH4+
-
non-activated NAD-GDH
24.6
NH4+
-
NAD+-dependent enzyme
25.6
NH4+
-
activated NAD-GDH
96
NH4+
-
from double-reciprocal plots for concentrations between 5 mM and 200 mM
304
NH4+
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 1960 micromol/min/mg, pH 8.0, 25°C
2.27
oxaloacetate
-
mutant M101S
4.16
oxaloacetate
-
mutant G82K
additional information
additional information
-
no significant changes in Km values between groups treated with alkalized extract from the tuber of Corydalis ternata or protopine and control groups
-
additional information
additional information
-
wild-type Vmax: 23.71 (pH 7), 35.16 (pH 9)
-
additional information
additional information
dissociation constants of wild-type and mutant enzymes for different coenzymes, overview
-
additional information
additional information
the enzyme shows positive cooperativity towards 2-oxoglutarate and NADH, and Michaelis-Menten type kinetics with ammonium chloride in the absence of catalytic activator L-aspartate. L-aspartate effect on enzyme kinetics, overview
-
additional information
additional information
-
the enzyme shows positive cooperativity towards 2-oxoglutarate and NADH, and Michaelis-Menten type kinetics with ammonium chloride in the absence of catalytic activator L-aspartate. L-aspartate effect on enzyme kinetics, overview
-
additional information
additional information
-
cofactor kinetics, overview
-
additional information
additional information
-
cofactor kinetics, overview
-
additional information
additional information
-
cofactor kinetics, overview. Even without the heterotropic antenna responsible for allosteric regulation in mammalian enzymes, the GDH is emphatically still allosteric. The Eadie-Hofstee plot for NAD+ is strongly non-linear.Att pH 9.0 there is almost total positive co-operativity with glutamate, with a Hill coefficient close to the theoretical maximum of 6 for a hexamer
-
additional information
additional information
-
enzyme kinetics of wild-tyype and mutant enzymes with NADPH, overview
-
additional information
additional information
-
kinetics of recombinant wild-type and mutant enzymes with NADH/NAD+ and NADPH/NADP+, overview
-