EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    1.2.1.105 | -999 |
- |
more |
- |
349022 |
| 1.2.1.105 | -999 |
- |
more |
kinetic study, reaction of 2-oxoglutarate dehydrogenase complex |
656580 |
| 1.2.1.105 | -999 |
- |
more |
the Hill coefficient for 2-oxoglutarate and NAD at 0.2 M ionic strength is 1.0, whereas at 0.05 M ionic strength it is 0.85 and 1.2 for 2-oxoglutarate and NAD, respectively, pH 7.8, 30°C |
758868 |
| 1.2.1.105 | -999 |
- |
more |
two substrate-binding modes are revealed at different degrees of saturation of the enzyme with 2-oxoglutarate. At low substrate concentrations, 0.001-0.01 mM, the binding mainly depends on the interaction of the enzyme with the substrate carbonyl groups. At 0.1-1 mM the relative contribution of the 2-oxo group in the binding increases |
349044 |
| 1.2.1.105 | 0.0025 |
- |
2-oxoglutarate |
mutant H298T, pH not specified in the publication, temperature not specified in the publication |
758781 |
| 1.2.1.105 | 0.00261 |
- |
2-oxoglutarate |
wild-type, pH not specified in the publication, temperature not specified in the publication |
758781 |
| 1.2.1.105 | 0.00273 |
- |
2-oxoglutarate |
mutant H260E/H298N, pH not specified in the publication, temperature not specified in the publication |
758781 |
| 1.2.1.105 | 0.0032 |
- |
CoA |
S0.5 value, 0.15 M ionic strength, pH 7.8, 30°C |
758868 |
| 1.2.1.105 | 0.00341 |
- |
2-oxoglutarate |
mutant H298L, pH not specified in the publication, temperature not specified in the publication |
758781 |
| 1.2.1.105 | 0.0035 |
- |
CoA |
S0.5 value, 0.10 M ionic strength, pH 7.8, 30°C |
758868 |
