EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
   1.5.1.39 | -999 |
- |
more |
Michaelis-Menten steady-state kinetics. The kinetic parameters show that the Km values of mutants T29A, T29G, and T29D are similar to that of wild-type enzyme with 0.0882 mM but the Km of mutants are increased. Also, the Vmax of mutant T29C and T29S are increased compared to wild-type, while the T29R mutant shows a significant decrease in Vmax |
764601 |
| 1.5.1.39 | -999 |
- |
more |
steady-state kinetics, relative binding affinities for oxidized and reduced flavin, overview. Steady-state kinetic analysis of the oxidase activity of the Pden_5119 protein and substrate kinetic isotope effect (KIE) |
765399 |
| 1.5.1.39 | 0.0028 |
- |
FMN |
pH 7.0, 30°C, recombinant wild-type |
765399 |
| 1.5.1.39 | 0.05 |
- |
NADH |
pH 7.0, 30°C, recombinant wild-type |
765399 |
| 1.5.1.39 | 0.057 |
- |
NADH |
pH 7.5, 25°C, recombinant wild-type enzyme |
765724 |
| 1.5.1.39 | 0.08 |
- |
NADPH |
pH 7.5, 25°C, recombinant wild-type enzyme |
765724 |
| 1.5.1.39 | 0.0882 |
- |
NADH |
recombinant wild-type enzyme, pH 5.5, 35°C |
764601 |
| 1.5.1.39 | 0.1394 |
- |
NADH |
recombinant mutant T29Y, pH 5.5, 35°C |
764601 |
| 1.5.1.39 | 0.141 |
- |
NADPH |
pH 7.5, 25°C |
763966 |
| 1.5.1.39 | 0.179 |
- |
NADH |
recombinant mutant T29N, pH 5.5, 35°C |
764601 |
