EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
   1.14.13.39 | -999 |
- |
more |
biochemical pathway model, kinetic modeling, isozymes NOS1 and NOS3 |
673804 |
| 1.14.13.39 | -999 |
- |
more |
kinetic analysis of the interaction between peroxynitrite and the oxygenase domain of inducible NOS at three different pH values, overview |
687548 |
| 1.14.13.39 | -999 |
- |
more |
kinetics |
685120 |
| 1.14.13.39 | -999 |
- |
more |
kinetics and kinetic modelling, stopped-flow measurements |
687572 |
| 1.14.13.39 | -999 |
- |
more |
kinetics modeling and single-turnover reactions, kinetics of heme transitions during Arg oxidation, product stoichiometry analysis, detailed overview |
685094 |
| 1.14.13.39 | -999 |
- |
more |
kinetics of cytcochrome c reduction and of reaction with FMN and cytochrome c, overview, eNOS and nNOS differ slightly in their NADP(H) interaction and flavin thermodynamics, and show distinct electron transfer activities, two-state conformational equilibrium of the FMN subdomain, overview |
687734 |
| 1.14.13.39 | -999 |
- |
more |
kinetics of flavin reduction of the recombinant enzyme, overview |
685095 |
| 1.14.13.39 | -999 |
- |
more |
kinetics of heme-NO complex formation in the stopped-flow reaction |
687579 |
| 1.14.13.39 | -999 |
- |
more |
kinetics of NO and substrate binding, recombinant enzyme |
684957 |
| 1.14.13.39 | -999 |
- |
more |
kinetics, rapid-freeze method, overview |
687697 |
