EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    1.13.11.52 | -999 |
- |
more |
bimolecular CO association rate coefficients, 22°C |
742005 |
| 1.13.11.52 | -999 |
- |
more |
kinetics of IDO-catalyzed indole oxidation as supported by H2O2, overview. The rate of disappearance of indole as a function of [H2O2] in the IDOFe3+-catalyzed reaction exhibits Michaelis-Menten behavior, with Km of about 1.1 mM for peroxide [indole] |
726383 |
| 1.13.11.52 | -999 |
- |
more |
Michaelis-Menten kinetics |
741581, 743654 |
| 1.13.11.52 | -999 |
- |
more |
steadystate, pre-steady-state and stopped-flow kinetics |
742885 |
| 1.13.11.52 | -999 |
- |
more |
stopped-flow and Michaelis-Menten steady-state kinetic measurements, kinetic model for catalytic dioxygenation of L-Trp by hIDO1, detailed overview. At low O2, the reversibility of the first step is essential for accurate reproduction of experimental O2 kcat/KM ratios |
741770 |
| 1.13.11.52 | 0.00072 |
- |
L-tryptophan |
NADPH-cytochrome P450 reductase-supported oxidation, in the absence of methylene blue and cytochrome b5, in PBS buffer (pH 7.4), at 37°C |
711229 |
| 1.13.11.52 | 0.0015 |
- |
L-tryptophan |
NADPH-cytochrome P450 reductase-supported oxidation, in the absence of methylene blue and in the presence of 250 nM cytochrome b5, in PBS buffer (pH 7.4), at 37°C |
711229 |
| 1.13.11.52 | 0.0017 |
- |
L-tryptophan |
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.0001 mM methylene blue and in the absence of cytochrome b5, in PBS buffer (pH 7.4), at 37°C |
711229 |
| 1.13.11.52 | 0.0019 |
- |
D-tryptophan |
H303A mutant, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.3 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37°C, 10-60 min |
659233 |
| 1.13.11.52 | 0.0019 |
- |
L-tryptophan |
NADPH-cytochrome P450 reductase-supported oxidation, in the presence of 0.0001 mM methylene blue and 250 nM cytochrome b5, in PBS buffer (pH 7.4), at 37°C |
711229 |
