EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
   1.6.5.5 | -999 |
- |
more |
Michaelis-Menten steady-state kinetics. For NfsA the oxidative half-reaction (i.e., the reoxidation of FMNHby 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. The flavoenzymes reducing quinones in a two-electron way possess a highly unstable semiquinone state, i.e., the redox potential of flavin semiquinone/dihydroflavin couple is more positive than the potential of flavin/semiquinone couple, thermodynamics, overview |
741786 |
| 1.6.5.5 | -999 |
- |
more |
stopped-flow and laser-flash photolysis kinetic analyses, steady-state kinetics |
724333 |
| 1.6.5.5 | 0.00065 |
- |
9,10-phenanthrenequinone |
pH 7.5 |
697701 |
| 1.6.5.5 | 0.0009 |
- |
5,8-Dihydroxy-1,4-naphthoquinone |
pH 7.0, 25°C |
741786 |
| 1.6.5.5 | 0.0012 |
- |
dibromothymoquinone |
pH 7.5, 10°C |
724333 |
| 1.6.5.5 | 0.0013 |
- |
2,5-dimethyl-4-benzoquinone |
pH 7.5, 10°C |
724333 |
| 1.6.5.5 | 0.0015 |
- |
9,10-phenanthrenequinone |
pH 7.5 |
697208 |
| 1.6.5.5 | 0.0016 |
- |
5-hydroxy-1,4-naphthoquinone |
pH 7.0, 25°C |
741786 |
| 1.6.5.5 | 0.0024 |
- |
1,2-naphthoquinone |
- |
14088 |
| 1.6.5.5 | 0.0025 |
- |
NADPH |
pH 7.5, cosubstrate: 9,10-phenanthrenequinone |
697701 |
