EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
   1.16.1.8 | -999 |
- |
more |
isothermal titration calorimetry reveals a binding constant of 0.037 and 0.002 mM for binding of NADP+ and 2',5'-ADP, respectively, for the ligand-protein complex formed with full-length MSR or the isolated FNR module |
685093 |
| 1.16.1.8 | -999 |
- |
more |
lack of control on the thermodynamics and kinetics of electron transfer in MSR, overview |
685164 |
| 1.16.1.8 | -999 |
- |
more |
steady-state kinetics analysis of wild-type and mutant enzymes with cytochrome c3+ and NADPH as substrates, overview |
726959, 727476 |
| 1.16.1.8 | -999 |
- |
more |
stopped-flow and steady-state kinetic analysis |
741764 |
| 1.16.1.8 | -999 |
- |
more |
stopped-flow spectroscopy, single turnover methods and a kinetic model relating electron flux through the enzyme to its conformational setpoint and its rates of conformational switching, kinetic model for electron flux through a dual-flavin enzyme, overview |
744874 |
| 1.16.1.8 | 0.0023 |
- |
2,6-dichlorophenolindophenol |
variant I22/S175 |
657920 |
| 1.16.1.8 | 0.0024 |
- |
NADPH |
pH 7.5, 25°C, recombinant wild-type enzyme |
741764 |
| 1.16.1.8 | 0.00264 |
- |
NADPH |
- |
659159 |
| 1.16.1.8 | 0.00289 |
- |
NADPH |
pH 7.5, 25°C |
685093 |
| 1.16.1.8 | 0.0038 |
- |
2,6-dichlorophenolindophenol |
variant I22/S175 |
657920 |
