EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
  1.14.13.114 | -999 |
- |
more |
kinetic analysis |
744353 |
| 1.14.13.114 | -999 |
- |
more |
Michaelis-Menten kinetics, comparative steady-state kinetic analysis with different substrates, 13C kinetic isotope effects, wild-type enzyme and mutants, overview. Comparison of the initial steady-state rates of product (2,5-DHP and NAD+) formation measured by HPLC and equilibrium dissociation constants for the NicC-FAD-6HNA complex |
764159 |
| 1.14.13.114 | 0.0028 |
- |
NADH |
pH 7.5, 25°C, recombinant mutant Y225F |
764159 |
| 1.14.13.114 | 0.003 |
- |
NADH |
pH 7.5, 25°C |
744353 |
| 1.14.13.114 | 0.0039 |
- |
5-chloro-6-hydroxynicotinate |
pH 7.5, 25°C, recombinant wild-type enzyme |
764159 |
| 1.14.13.114 | 0.006 |
- |
NADH |
pH 7.5, 25°C |
744353 |
| 1.14.13.114 | 0.0063 |
- |
NADH |
pH 7.5, 25°C, recombinant mutant C202A |
764159 |
| 1.14.13.114 | 0.0081 |
- |
NADH |
pH 7.5, 25°C, recombinant wild-type enzyme |
764159 |
| 1.14.13.114 | 0.019 |
- |
NADH |
pH 7.5, 25°C, recombinant mutant H302A |
764159 |
| 1.14.13.114 | 0.02 |
- |
6-Hydroxynicotinate |
pH 7.5, 25°C, recombinant mutant H302A |
764159 |
