EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
   1.7.3.1 | -999 |
- |
more |
kinetic competency of the cationic imine enzyme intermediate |
655799 |
| 1.7.3.1 | -999 |
- |
more |
kinetics and thermodynamics of the deprotonation step with substrate nitroethane, effects of tunneling |
655793 |
| 1.7.3.1 | -999 |
- |
more |
steady-state and rapid reaction kinetics of wild-type and mutant enzymes |
654710 |
| 1.7.3.1 | -999 |
- |
more |
thermodynamics, kinetic mechanism with nitroethane and 1-nitrobutane, isotopic effects, monotonic increase with each additional methylene group from nitroethane to 1-nitrobutane increasing kcat/Km value by 20fold, no further increase with 1-nitropentane and 1-nitrohexane |
654373 |
| 1.7.3.1 | 0.011 |
- |
O2 |
mutant enzyme S171T, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C |
711373 |
| 1.7.3.1 | 0.019 |
- |
O2 |
pH 8.0, 30°C, mutant enzyme D402E |
685114 |
| 1.7.3.1 | 0.023 |
- |
O2 |
- |
639230 |
| 1.7.3.1 | 0.028 |
- |
O2 |
mutant enzyme Y398F, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C |
711373 |
| 1.7.3.1 | 0.029 |
- |
O2 |
mutant enzyme S171A, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C |
711373 |
| 1.7.3.1 | 0.03 |
- |
1-nitrobutane |
recombinant wild-type enzyme, pH 8.0, 30°C |
654710 |
