EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
   1.5.1.42 | -999 |
- |
more |
Gibbs activation and reaction free energies obtained for the hydride transfer by wild-type enzyme |
764492 |
| 1.5.1.42 | -999 |
- |
more |
steady-state kinetic analysis, the initial rates of NADH oxidation follow typical Michaelis-Menten kinetics, and Lineweaver-Burk plots show parallel patterns for a ping-pong mechanism |
765260 |
| 1.5.1.42 | -999 |
- |
more |
the kinetics of binding of FMNH- to PlLuxAB and VcLuxAB and the subsequent reactions with oxygen are the same with either free FMNH- or FMNH- generated in situ by LuxG. No complexes between LuxG and the various species are necessary to transfer FMNH- to the acceptors. Single-mixing and double-mixing stopped-flow spectrophotometry. Anaerobic transient reaction kinetic analysis, overview |
741888 |
| 1.5.1.42 | 0.001 |
- |
FMN |
pH 5.6, 23°C, spectrometric assay |
392180 |
| 1.5.1.42 | 0.001 |
- |
FMN |
pH 8.5, 23°C, spectrometric assay |
392180 |
| 1.5.1.42 | 0.0011 |
- |
FMN |
pH 6.8, 23°C |
392179 |
| 1.5.1.42 | 0.0013 |
- |
FMN |
pH 7.8, 25°C |
715329 |
| 1.5.1.42 | 0.0036 |
- |
FMN |
pH 7.5, 25°C |
746821 |
| 1.5.1.42 | 0.00443 |
- |
FMN |
recombinant enzyme HcbA3, pH 7.5, 20°C |
765260 |
| 1.5.1.42 | 0.012 |
- |
NADH |
pH 8.5, 23°C, spectrometric assay |
392180 |
