PROSITE documentation PDOC00684Indoleamine 2,3-dioxygenase signatures
Indoleamine 2,3-dioxygenase (EC 1.13.11.42) (IDO) [1] is an enzyme responsible for the conversion of tryptophan and other indole derivatives to kynurenines. In mammals, IDO is induced by interferon-γ (IFN-γ) and responsible for some of its anti-proliferative effects. The degradative action of IDO on tryptophan leads to cell death by starvation of this essential and relatively scarce amino acid. IDO is a heme-containing enzyme of about 400 amino acids.
Other proteins that are evolutionarily related to IDO are:
- Myoglobin from the red muscle of the gastropods Nordotis madaka and Sulculus diversicolor [2]. These unusual globins lack enzymatic activity but have kept the heme group.
- Yeast hypothetical protein YJR078w.
As a signature for the IDO family, we selected two conserved regions. The first is located in the central section and is rich in glycine and serine residues; the second is located in the second third of the sequence and contains a conserved histidine that could serve as a proximal ligand to the heme iron.
Last update:May 2004 / Text revised.
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PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Taylor M.W. Feng G.S. |
| Title | Relationship between interferon-gamma, indoleamine 2,3-dioxygenase, and tryptophan catabolism. | |
| Source | FASEB J. 5:2516-2522(1991). | |
| PubMed ID | 1907934 |
| 2 | Authors | Suzuki T. |
| Title | Abalone myoglobins evolved from indoleamine dioxygenase: the cDNA-derived amino acid sequence of myoglobin from Nordotis madaka. | |
| Source | J. Protein Chem. 13:9-13(1994). | |
| PubMed ID | 8011076 |
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