EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
   1.7.1.B3 | -999 |
- |
more |
enzyme kinetic analysis, overview |
742109 |
| 1.7.1.B3 | -999 |
- |
more |
Michaelis-Menten steady-state kinetics |
742167 |
| 1.7.1.B3 | -999 |
- |
more |
Michaelis-Menten steady-state kinetics of recombinant His6-tagged enzyme |
743709 |
| 1.7.1.B3 | -999 |
- |
more |
Michaelis-Menten steady-state kinetics. For NfsA the oxidative half-reaction (i.e., the reoxidation of FMNH by the oxidant substrate) is a rate-limiting step, because the values of kcat at infinite concentrations of tetryl or 2,4,6-trinitrotoluene are substantially lower than the lowest rate of the reductive half reaction (the reduction of FMN by NADPH) measured in the preliminary rapid reaction experiments. Stopped-flow and single-turnover measurements |
741786 |
| 1.7.1.B3 | 0.00085 |
- |
NADPH |
pH 7.0, 23°C, recombinant enzyme, with nitrofurazone |
742109 |
| 1.7.1.B3 | 0.011 |
- |
tetryl |
pH 7.0, 25°C |
741786 |
| 1.7.1.B3 | 0.012 |
- |
nitrofurazone |
recombinant wild-type enzyme, pH 7.0, 22°C |
742167 |
| 1.7.1.B3 | 0.013 |
- |
2,4,6-trinitrotoluene |
recombinant mutant F46Y, pH 7.0, 22°C |
742167 |
| 1.7.1.B3 | 0.0163 |
- |
nitrofurazone |
pH 7.0, 23°C, recombinant enzyme |
742109 |
| 1.7.1.B3 | 0.018 |
- |
o-dinitrobenzene |
pH 7.0, 25°C |
741786 |
