EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    1.1.1.169 | -999 |
- |
more |
kinetics and thermodynamics, overview |
669806 |
| 1.1.1.169 | -999 |
- |
more |
kinetics and thermodynamics, wild-type enzyme, overview |
667687 |
| 1.1.1.169 | -999 |
- |
more |
kinetics of recombinant wild-type and mutant enzymes, overview |
687675 |
| 1.1.1.169 | -999 |
- |
more |
Michaelis-Menten kinetics in both reaction directions |
736827 |
| 1.1.1.169 | -999 |
- |
more |
steady-state kinetics, pH-dependence of kinetics with different substrates, overview |
654677 |
| 1.1.1.169 | -999 |
- |
more |
the enzyme shows strong positive cooperativity in kinetics. The enzyme follows a random addition mechanism in which the initial binding of NADPH is the kinetically preferred path, with a small degree of cooperativity between subunits. The mechanism of Staphylococcus aureus KPR is distinct from those of previously described members of the family of 2-hydroxyacid dehydrogenases |
740065 |
| 1.1.1.169 | 0.00135 |
- |
NADPH |
recombinant enzyme, pH 6.4, 70°C |
736827 |
| 1.1.1.169 | 0.002 |
- |
NADPH |
+/-0.0003, mutant E256A |
286109 |
| 1.1.1.169 | 0.0029 |
- |
NADPH |
+/-0.0006, mutant E256D |
286109 |
| 1.1.1.169 | 0.003 |
- |
NADH |
recombinant enzyme, pH 6.4, 70°C |
736827 |
