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0.00076
-
activity in liver nuclei, cofactor NADH
0.0028
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activity in liver mitochondria, cofactor NADH
0.168
-
NADH dependent activity in cells grown on medium containing 1 mM NH4Cl
0.257
-
NADH dependent activity in cells grown on medium containing 1 mM NH4Cl
0.336
-
NADH dependent activity in cells grown on medium containing 1 mM NH4Cl
0.858
-
NADPH dependent activity in cells grown on medium containing 1 mM NH4Cl
1.07
-
NADH dependent activity in cells grown on medium containing 1 mM NH4Cl
1.2
-
glutamate dehydrogenase 2
1.8
-
glutamate dehydrogenase 1
1.93
-
after 3rd crystallization
1.96
-
NADPH dependent activity in cells grown on medium containing 1 mM NH4Cl
100
-
recombinant R463A mutant enzyme, maximal activity in the presence of 6 mM leucine
140
-
recombinant H454Y mutant enzyme, maximal activity in the presence of 0.2 mM ADP
145.7
-
purified mutant enzyme R443S/G456A
159.1
-
purified isozyme GDH2
161.9
-
purified isozyme GDH1
19
-
recombinant S448P mutant enzyme, basal activity
190
-
enzyme from euthermic animals
2.22
-
NADPH dependent activity in cells grown on medium containing 1 mM NH4Cl
201
-
enzyme from hibernating animals
32.3
-
high-activity form of the enzyme, NADP+-dependent deamination
4.6
-
membrane-bound liver enzyme
4.8
-
enzyme purified from liver nuclei
411
-
native enzyme at 100°C
419
-
recombinant enzyme at 75°C
5.18
-
NADPH dependent activity in cells grown on medium containing 1 mM NH4Cl
5.9
-
low-activity form of the enzyme, NADP+ dependent deamination
55
-
recombinant S448P mutant enzyme, maximal activity in the presence of 6 mM leucine
69
-
recombinant S448P mutant enzyme, maximal activity in the presence of 0.2 mM ADP
73
-
recombinant R463A mutant enzyme, basal activity
74
-
recombinant H454Y mutant enzyme, basal activity
79.4
-
purified enzyme, pH 8.0, 70°C
84
-
recombinant wild-type enzyme, basal activity
130
-
recombinant wild-type enzyme, maximal activity in the presence of 0.2 mM ADP or 6 mM leucine
130
-
recombinant S448P mutant enzyme, maximal activity in the presence of 6 mM leucine
423
-
recombinant enzyme at 90°C
additional information
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hGDH1 displays a high basal activity of 40% of its maximal activity. Regulation of the hGDH1 activity is achieved by interplay of GTP and ADP/L-leucine
additional information
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hGDH2 displays a basal activity less than 10% of its maximal activity. Control of the hGDH2 activity depends on the level of its basal activity and on changing ADP/L-leucine concentrations. For hGDH2 enzyme protein concentration and basal activity show a linear pattern of dependence. Lowering the temperature of the reaction mixture from 25°C to 20°C has a stabilizing effect on hGDH2, as under these conditions, the specific basal activities of the enzyme increases. Increasing the concentration of the TrisHCl buffer from 50 mM to 125 mM or to 250 mM (pH 8.0) raises basal activity levels, but the maximal activity declines
additional information
enzyme activity in wild-type and transgenic overexpressing brain cell fractions, overview
additional information
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enzyme activity in wild-type and transgenic overexpressing brain cell fractions, overview
additional information
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1.44 DELTA absorbance/min/mg, cofactor NAD+
additional information
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0.263 DELTA absorbance/min/mg, cofactor NADP+
additional information
-
-
additional information
the specific activity of the hexameric form of the recombinant enzyme is much lower than that of the natural enzyme. The structure of the hexameric form of the recombinant enzyme with low specific activity (Type I) is different from that of the natural enzyme with high specific activity (Type II). Upon heat treatment (80°C, 15 min), the Type I structure is effectively converted to Type II structure and the specific activity of the enzyme is increased by 2.6fold