EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
   1.1.3.17 | -999 |
- |
more |
analysis of steady-state kinetic mechanism, activation of alcohol substrate, hydride ion transfer |
696242 |
| 1.1.3.17 | -999 |
- |
more |
analysis of substrate kinetic isotope effects |
698905 |
| 1.1.3.17 | -999 |
- |
more |
kinetics and redox potentiometric analysis of liganded and unliganded wild-type and mutant enzymes, comparison of spectral parameters of wild-type and mutant enzymes, overview |
672136 |
| 1.1.3.17 | -999 |
- |
more |
kinetics and thermodynamics, steady state kinetic mechanism |
671605 |
| 1.1.3.17 | -999 |
- |
more |
kinetics, recombinant enzyme, NMR-determination of hydration ratio of betaine aldehyde, overview |
672121 |
| 1.1.3.17 | -999 |
- |
more |
kinetics, recombinant enzyme, overview |
674159 |
| 1.1.3.17 | -999 |
- |
more |
minimal kinetic mechanism for reductive half-reaction of the V464A and V464T mutant enzymes, oxidative half-reactions' steady-state kinetic mechanisms, overview |
724284 |
| 1.1.3.17 | -999 |
- |
more |
similar level of catalytic activity than free enzyme in solution |
686373 |
| 1.1.3.17 | -999 |
- |
more |
steady-state kinetics and thermodynamics, effect of pH on the hysteretic behavior of the enzyme at 25°C, kinetic parameters of enzyme stored at pH 6.0 and -20°C, overview |
677058 |
| 1.1.3.17 | -999 |
- |
more |
steady-state kinetics of wild-type and mutant enzymes at different pH and in presence or absence of imidazole, kinetic isotope effects |
654773 |
