EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    1.5.1.30 | -999 |
- |
more |
enzyme kinetic analysis, overview |
742109 |
| 1.5.1.30 | -999 |
- |
more |
Km-value of both NADPH and FMN gradually decreases at increasing concentrations of oxygen, with 0.000104 and 0.000019 mM as the upper limits for Km of FMN and NADPH, resp. |
671610 |
| 1.5.1.30 | -999 |
- |
more |
substrate and cofactor binding, reaction kinetics |
658108 |
| 1.5.1.30 | 0.000016 |
- |
FMN |
25°C, single-enzyme assay |
657786 |
| 1.5.1.30 | 0.000019 |
- |
NADPH |
presence of 1.05 mM O2 |
671610 |
| 1.5.1.30 | 0.00007 |
- |
NADPH |
mutant enzyme E99K, in 50 mM phosphate buffer, at pH 7.0, at 23°C |
684711 |
| 1.5.1.30 | 0.00013 |
- |
FMN |
25°C, enzyme in complex with monooxygenase SsuD, presence of octanesulfonate |
657786 |
| 1.5.1.30 | 0.00013 |
- |
FMN |
presence of 1.05 mM O2 |
671610 |
| 1.5.1.30 | 0.00085 |
- |
NADPH |
nitrofurazone as electron acceptor |
392302 |
| 1.5.1.30 | 0.0009 |
- |
FMN |
coupled oxidoreductase-luciferase assay, kcat/Km = 73/(M*min), in 100 mM Na+/K+ phosphate buffer with 100 mM NaCl, pH 7.0, 1 microM Fre oxidoreductase, 10 microM decanal, 10 microM NADPH, 5 microM luciferase |
698992 |
