EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
  1.5.1.38 | -999 |
- |
more |
steady-state kinetic analysis of wild-type and mutant enzymes, kinetics of FMN binding, overview |
741937 |
| 1.5.1.38 | -999 |
- |
more |
steady-state Michaelis-Menten kinetics, and rapid-reaction kinetic analyses of Y118A, DELTAY118 SsuE, and wild-type SsuE, as well as stopped-flow kinetics, overview |
764152 |
| 1.5.1.38 | -999 |
- |
more |
the kinetic mechanism of FRP is changed to a sequential pattern with a Km(FMN) of 0.003 mM and a Km(NADPH) of 0.02 mM in a luciferase-coupled assay measuring light emission |
392200 |
| 1.5.1.38 | 0.000054 |
- |
FMN |
pH 7.9, 30°C |
438770 |
| 1.5.1.38 | 0.0005 |
- |
FMN |
pH 6.8, 23°C |
392179 |
| 1.5.1.38 | 0.0027 |
- |
FAD |
pH 7.9, 30°C |
438770 |
| 1.5.1.38 | 0.003 |
- |
NADPH |
pH 7.0, 23°C, enzyme derivative reconstituted from apoenzyme and 2-thioFMN |
392300 |
| 1.5.1.38 | 0.005 |
- |
FMN |
pH 7.0, 23°C, native enzyme |
392300 |
| 1.5.1.38 | 0.007 |
- |
2-thioFMN |
pH 7.0, 23°C, enzyme derivative reconstituted from apoenzyme and 2-thioFMN |
392300 |
| 1.5.1.38 | 0.008 |
- |
FMN |
pH 7.0, 23°C, single-enzyme spectrophotometric assay monitoring the NADPH oxidation |
392200 |
