EC Number   |
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Reference |
|---|
   1.4.1.3 | -999 |
- |
- |
655623 |
| 1.4.1.3 | -999 |
- |
0.263 DELTA absorbance/min/mg, cofactor NADP+ |
391594 |
| 1.4.1.3 | -999 |
- |
1.44 DELTA absorbance/min/mg, cofactor NAD+ |
391594 |
| 1.4.1.3 | -999 |
- |
enzyme activity in wild-type and transgenic overexpressing brain cell fractions, overview |
712827 |
| 1.4.1.3 | -999 |
- |
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 |
700428 |
| 1.4.1.3 | -999 |
- |
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 Tris–HCl buffer from 50 mM to 125 mM or to 250 mM (pH 8.0) raises basal activity levels, but the maximal activity declines |
700428 |
| 1.4.1.3 | -999 |
- |
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 |
724160 |
| 1.4.1.3 | 0.00076 |
- |
activity in liver nuclei, cofactor NADH |
391596 |
| 1.4.1.3 | 0.0028 |
- |
activity in liver mitochondria, cofactor NADH |
391596 |
| 1.4.1.3 | 0.168 |
- |
NADH dependent activity in cells grown on medium containing 1 mM NH4Cl |
391619 |
