indoleamine 2,3-dioxygenase EC#: 1.13.11.52; ChemWhat Code: 1374976
| Product Name | indoleamine 2,3-dioxygenase |
| Example Structure |  |
| Synonyms | 31854, BRAFLDRAFT_126354, CG5163, EC 1.11.1.4, EC 1.13.1.12, hIDO, hIDO1, hTDO, IDO, IDO-1, IDO-2, IDO1, IDO2, INDO, INDOL1, indolamine 2,3-dioxygenase, indole 2,3-dioxygenase, indoleamine 2, 3-dioxygenase, indoleamine 2,3 dioxygenase, indoleamine 2,3-dioxygenase, indoleamine 2,3-dioxygenase 1, indoleamine 2,3-dioxygenase 2, indoleamine 2,3-dioxygenase-1, indoleamine 2,3-dioxygenase-2, indoleamine 2,3-dioxygenase-like protein, indoleamine-2,3-dioxygenase, Indoleamine-pyrrole 2,3-dioxygenase, L-tryptophan 2,3-dioxygenase, L-tryptophan pyrrolase, mIDO, oxygenase, tryptophan 2,3-di-, proto-IDO, proto-indoleamine 2,3-dioxygenase, superoxygenase, TDO, TDO2, TioF, TO, TRPO, Tryptamin 2,3-dioxygenase, tryptamine 2,3-dioxygenase, tryptophan 2,3-dioxygenase, tryptophan dioxygenase, tryptophan oxygenase, tryptophan peroxidase, tryptophan pyrrolase, tryptophan-2,3-dioxygenase, tryptophanase, v1g244579, Vermilion protein |
| EC Number | 1.13.11.52 |
| CAS Registry Number | |
| Comments | A protohemoprotein. Requires ascorbic acid and methylene blue for activity. This enzyme has broader substrate specificity than EC 1.13.11.11, tryptophan 2,3-dioxygenase [1]. It is induced in response to pathological conditions and host-defense mechanisms and its distribution in mammals is not confined to the liver [2]. 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 [2,6]. Superoxide radicals can replace O2 as oxygen donor [4,7]. |
| Cofactor | heme |
| History | |
| Reactions | (1) D-tryptophan + O(2) = N-formyl-D-kynurenine. (2) L-tryptophan + O(2) = N-formyl-L-kynurenine. |
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