EC Number   |
Natural Substrates |
|---|
    1.13.11.52 | 5-hydroxy-L-tryptophan + O2 |
- |
| 1.13.11.52 | D-tryptophan + O2 |
- |
| 1.13.11.52 | D-tryptophan + O2 |
IDO displays a similar kcat for D- and L-tryptophan, but D-tryptophan has 173folds higher Km |
| 1.13.11.52 | D-tryptophan + O2 |
L-Trp is a better substrate for IDO than D-Trp |
| 1.13.11.52 | D-tryptophan + O2 |
while L and D-tryptophan have similar affinities (Km values), the kcat is 10times lower for D-tryptophan |
| 1.13.11.52 | D-tryptophan + O2 |
IDO1 |
| 1.13.11.52 | L-Trp + O2 |
regulation of enzyme activity |
| 1.13.11.52 | L-Trp + O2 |
lipopolysaccharide and muramyl tripeptide upregulate enzyme induction through a mechanism independent of interleukin 1alpha |
| 1.13.11.52 | L-Trp + O2 |
interleukin-4 inhibits expression of the enzyme in monocytes |
| 1.13.11.52 | L-Trp + O2 |
initial enzyme of tryptophan degradation pathway |
