EC Number   |
General Information |
Reference |
|---|
    1.13.11.11 | drug target |
conversion of tryptophan to N-formylkynurenine is the first and rate-limiting step of the tryptophan metabolic pathway (i.e., the kynurenine pathway). This conversion is catalyzed by three enzyme isoforms: indoleamine 2,3-dioxygenase 1 (IDO1), indoleamine 2,3-dioxygenase 2 (IDO2), and tryptophan-2,3-dioxygenase (TDO). As this pathway generates numerous metabolites that are involved in various pathological conditions, IDOs and TDO represent important targets for therapeutic intervention. Despite their poor sequence similarities, their active sites are highly conserved, and therefore allow the design of inhibitors with multiple activities that can target at least two isoforms |
765516 |
| 1.13.11.11 | drug target |
human indoleamine 2,3-dioxygenase 1 (hIDO1) and tryptophan 2,3-dioxygenase (hTDO) are closely linked to the pathogenesis of Parkinson's disease |
765226 |
| 1.13.11.11 | drug target |
Indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase (TDO) are promising drug development targets due to their implications in pathologies such as cancer and neurodegenerative diseases. IDO1/TDO dual inhibitors and provides chemical molecules for potential development into drugs |
764295 |
| 1.13.11.11 | drug target |
the enzyme (TDO2) catalyzes the conversion of tryptophan to the immunosuppressive metabolite kynurenine. TDO2 overexpression has been observed in a number of cancers. Therefore, TDO inhibition may be a useful therapeutic intervention for cancers |
763817 |
| 1.13.11.11 | drug target |
tryptophan 2,3-dioxygenase is a therapeutic target for Parkinson's disease |
764645 |
| 1.13.11.11 | evolution |
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) are heme-containing enzymes that catalyze the O2-dependent oxidation of L-tryptophan (L-Trp) in biological systems following different reaction mechanisms, the rate-limiting step in the IDO and TDO mechanisms is not the same |
-, 741938 |
| 1.13.11.11 | evolution |
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview |
743005 |
| 1.13.11.11 | malfunction |
alterations in the activity of tryptophan 2,3-dioxygenase cause imbalances in the levels of serotonin and other neuroactive metabolites which can contribute to motor, psychiatric, gastrointestinal, and other dysfunctions often seen in Parkinson's disease |
764645 |
| 1.13.11.11 | malfunction |
pharmacological inhibition or knockdown of the enzyme (TDO2) in adjuvant-induced arthritis-fibroblast-like synoviocytes results in a reduced proliferation, secretion, migration and invasion |
764385 |
| 1.13.11.11 | malfunction |
TDO knockout mice require a minimum of 0.06% dietary L-Trp, which value is about 2 mg/d/mouse |
-, 742114 |
