EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    1.14.18.1 | -999 |
- |
more |
4.3% O2 |
636382 |
| 1.14.18.1 | -999 |
- |
more |
detailed kinetics, overview |
675458 |
| 1.14.18.1 | -999 |
- |
more |
enzyme kinetic analysis at different pH values, overview |
746343 |
| 1.14.18.1 | -999 |
- |
more |
enzyme kinetics |
745475 |
| 1.14.18.1 | -999 |
- |
more |
kinetic mechanism, general kinetic model |
674108 |
| 1.14.18.1 | -999 |
- |
more |
kinetic parameters for free and immobilized enzymes, determined according to the Michaelis-Menten equation, show a lower Km value for PPO-MAC400 than for the free enzyme, indicating higher affinity towards substrate, while PPO-MAC200 exhibits a higher Km value |
686097 |
| 1.14.18.1 | -999 |
- |
more |
kinetics measurement and simulation of in vitro kinetics of the tyrosinase reaction |
744483 |
| 1.14.18.1 | -999 |
- |
more |
kinetics, the activation free energy is dominated by the enthalpic term, the value of which lies in the relatively narrow range of 61 kJmol-1 irrespective of substrate or reaction type as monophenolase, EC 1.14.18.1, or diphenolase |
673090 |
| 1.14.18.1 | -999 |
- |
more |
Michaeli-Menten kinetics |
745474 |
| 1.14.18.1 | -999 |
- |
more |
Michaelis-Menten kinetics |
744490, 744758, 745130, 745131, 745557 |
