CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.58 | Methane Monooxygenase Hydroxylase; Chain G, domain 1 |
|
1.20.58.480 |
Domain Context
CATH Clusters
| Superfamily | 1.20.58.480 |
| Functional Family |
Enzyme Information
| 1.13.11.52 |
Indoleamine 2,3-dioxygenase.
based on mapping to UniProt P14902
(1) D-tryptophan + O(2) = N-formyl-D-kynurenine. (2) L-tryptophan + O(2) = N-formyl-L-kynurenine.
-!- Requires ascorbic acid and methylene blue for activity. -!- Has broader substrate specificity than EC 1.13.11.11. -!- Is induced in response to pathological conditions and host-defense mechanisms. -!- While the enzyme is more active with D-tryptophan than L-tryptophan, its only known function to date is in the metabolism of L-tryptophan. -!- Superoxide radicals can replace O(2) as oxygen donor.
|
UniProtKB Entries (1)
| P14902 |
I23O1_HUMAN
Homo sapiens
Indoleamine 2,3-dioxygenase 1
|
PDB Structure
| PDB | 2D0T |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase.
Proc.Natl.Acad.Sci.Usa
|
