EC Number   |
General Information |
Reference |
|---|
    1.13.11.52 | drug target |
as an immunosuppressive enzyme, indoleamine 2,3-dioxygenase 1 is considered a promising target for oncology immunotherapy |
765415 |
| 1.13.11.52 | drug target |
combined treatment of cancer cells in vitro with indoleamine 2,3-dioxygenase 1-specific antisense oligonucleotides and small molecule inhibitors can reduce the production of kynurenine by cancer cells in a synergistic manner |
764396 |
| 1.13.11.52 | 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 |
| 1.13.11.52 | 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 |
| 1.13.11.52 | 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 |
| 1.13.11.52 | drug target |
the enzyme is a promising target for cancer immunotherapy |
764463 |
| 1.13.11.52 | drug target |
the enzyme is a tumour cell survival factor that causes immune escape in several types of cancer |
765149 |
| 1.13.11.52 | drug target |
the enzyme is an anti-cancer drug target |
764273 |
| 1.13.11.52 | drug target |
the enzyme is an attractive target for cancer immunotherapy |
764291 |
| 1.13.11.52 | evolution |
indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO, EC 1.13.11.11) 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. Some lineages have independently generated multiple IDO paralogues through gene duplications. Only mammalian IDO1s and fungal typical IDOs have high affinity and catalytic efficiency for L-Trp catabolism, comparable to TDOs. Invertebrate IDO enzymes have low affinity and catalytic efficiency for L-Trp catabolism. Phylogenetic analysis. the phylogenetic distribution of low catalytic-efficiency IDOs indicates the ancestral IDO also had low affinity and catalytic efficiency for L-Trp catabolism. IDOs with high catalytic-efficiency for L-Trp catabolism may have evolved in certain lineages to fulfill particular biological roles. The low catalytic efficiency IDOs have been well conserved in a number of lineages throughout their evolution, although it is not clear that the enzymes contribute significantly to L-Trp catabolism in these species |
743005 |
