|PROSITE documentation PDOC00684|
Indoleamine 2,3-dioxygenase (EC 22.214.171.124) (IDO)  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:
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.
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).|
|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).|