IDO1 dioxygenates L-Trp to NFK

Stable Identifier
R-HSA-198563
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
tryptophan + O2 => N-formylkynurenine [IDO]
Locations in the PathwayBrowser
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Cytosolic indoleamine 2,3-dioxygenase (IDO) catalyzes the conversion of L-tryptophan and oxygen to formylkynurenine. The structure and catalytic properties of the human enzyme have been analyzed directly (Sugimoto et al. 2006); the subcellular location and monomeric state of the active form of the enzyme are inferred from the properties of its rabbit ortholog (Shimizu et al. 1976). In the body, IDO is ubiquitously expressed and is induced by interferon. These properties, together with IDO's broad substrate specificity, are consistent with the hypothesis that the enzyme functions functions in anti bacterial and inflammatory processes (Taylor and Feng 1991).

Literature References
PubMed ID Title Journal Year
16477023 Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase

Sugimoto, H, Oda, SI, Otsuki, T, Hino, T, Yoshida, T, Shiro, Y

Proc Natl Acad Sci USA 2006
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
tryptophan 2,3-dioxygenase activity of IDO1 [cytosol]
Physical Entity
Activity
Orthologous Events
Authored
Created