EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    1.1.1.37 | -999 |
- |
more |
- |
669660 |
| 1.1.1.37 | -999 |
- |
more |
activity kinetics of the native and recombinant proteins are identical |
686623 |
| 1.1.1.37 | -999 |
- |
more |
kinetics |
685420 |
| 1.1.1.37 | -999 |
- |
more |
Michaelis-Menten and allosteric sigmoidal kinetics |
761765 |
| 1.1.1.37 | -999 |
- |
more |
Michaelis-Menten kinetics |
740198, 740926, 740975 |
| 1.1.1.37 | -999 |
- |
more |
pH-dependent kinetic mechanism for cMDH, and kinetic modelling for cMDH-catalyzed oxidation of L-malate, detailed overview |
740166 |
| 1.1.1.37 | -999 |
- |
more |
pH-dependent kinetic mechanism for mMDH, and kinetic modelling for mMDH-catalyzed oxidation of L-malate, detailed overview |
740165 |
| 1.1.1.37 | -999 |
- |
more |
recombinant L-MDH displays a typical Michaelis-Menten kinetic profile for both substrates |
748018 |
| 1.1.1.37 | -999 |
- |
more |
the enzyme displays a strong KCl-concentration dependent variation in KM-value for oxaloacetate, but not for NADH |
654906 |
| 1.1.1.37 | 0.0001 |
- |
oxaloacetate |
pH and temperature not specified in the publication with NAD+ |
740926 |
