EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    1.14.15.1 | -999 |
- |
more |
combined quantum mechanical/molecular mechanical study, molecular dynamics, overview |
674197 |
| 1.14.15.1 | -999 |
- |
more |
detailed comparative pre-steady-state kinetic and steady-state analysis of enzyme mutant SeP450cam C357U/R365L/E366Q and its the cysteine-containing wild-type, overview |
744343 |
| 1.14.15.1 | -999 |
- |
more |
development of a global data fitting kinetic model that describes the time-varying concentrations of substrate and products, Michaelis-Menten kinetics |
672760 |
| 1.14.15.1 | -999 |
- |
more |
enzyme-cofactor interaction kinetics of wild-type and mutant enzymes, steady-state and stopped-flow reaction kinetics, overview |
744698 |
| 1.14.15.1 | -999 |
- |
more |
EPR/ENDOR studies of wild-type and mutant T252A enzymes |
674152 |
| 1.14.15.1 | -999 |
- |
more |
equilibrium isotope effect on O2 binding, isotope effects and transient-state kinetics, electron transfer kinetics, steady-state kinetics, recombinant His6-tagged enzyme, overview |
672115 |
| 1.14.15.1 | -999 |
- |
more |
interaction thermodynamics between Pdx and various states of P450cam constrained in different conformations, overview |
744192 |
| 1.14.15.1 | -999 |
- |
more |
kinetics of wild-type and mutant enzymes |
746282 |
| 1.14.15.1 | -999 |
- |
more |
Km-value of putidaredoxin, 0.0038 mM, steady-state kinetics of enzyme interaction with redox partners |
658056 |
| 1.14.15.1 | -999 |
- |
more |
single turnover kinetics |
674516 |
