EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    1.1.1.87 | -999 |
- |
more |
Michaelis-Menten kinetics, the enzyme shows a steady-state random kinetic mechanism with a preferred order of addition of Mg2+ prior to NAD+. The same step(s) limit the reaction at limiting and saturating Mg2+ concentrations. Solvent kinetic deuterium isotope effects and viscosity effects are consistent with a rate-limiting pre-catalytic conformational change at saturating reactant concentrations |
739958 |
| 1.1.1.87 | -999 |
- |
more |
mutant enzymes kinetic analysis and pH-dependencies, overview |
696350 |
| 1.1.1.87 | -999 |
- |
more |
substitution of potassium acetate for KCl changes the kinetic mechanism of HIcDH from a steady state random to a fully ordered mechanism with the binding of Mg-HIc followed by K+ and NAD+, increase in the affinity of enzyme for Mg-HIc as a result of elimination of the inhibitory effect of Cl-, kinetic analysis, overview |
696220 |
| 1.1.1.87 | 0.0042 |
- |
homoisocitrate |
oxidate decarboxylation of homoisocitrate |
685232 |
| 1.1.1.87 | 0.0073 |
- |
homoisocitrate |
wild type enzyme, with NAD+ as cosubstrate, at pH 8.0 and 60°C |
760522 |
| 1.1.1.87 | 0.01 |
- |
homoisocitrate |
value below |
644539 |
| 1.1.1.87 | 0.014 |
- |
isocitrate |
wild type enzyme, with NAD+ as cosubstrate, at pH 8.0 and 60°C |
760522 |
| 1.1.1.87 | 0.0164 |
- |
isocitrate |
pH 7.8, 70°C, recombinant enzyme |
660907 |
| 1.1.1.87 | 0.018 |
- |
homoisocitrate |
- |
685539 |
| 1.1.1.87 | 0.018 |
- |
homoisocitrate |
pH 7.8, 36°C, recombinant enzyme |
667934 |
