IDO2 dioxygenates L-Trp to NFK

Stable Identifier
Reaction [transition]
Homo sapiens
tryptophan + O2 => N-formylkynurenine [IDO2]
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Cytosolic indoleamine 2,3-dioxygenase 2 (IDO2) catalyzes the conversion of L-tryptophan and oxygen to formylkynurenine. The catalytic properties of the human enzyme have been analyzed directly; the subcellular location and monomeric state of the active form of the enzyme are inferred from the properties of its rabbit ortholog. In the body, IDO2 mRNA can be detected in a variety of cells, including dendritic cells, consistent with a normal role in immune function and a pathological one in tumor progression. Two IDO2 variants common in human populations encode enzymatically inactive protiens, suggesting that absence of IDO2 activity may be common in humans (Metz et al. 2007).

Literature References
PubMed ID Title Journal Year
17671174 Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan

Metz, R, DuHadaway, JB, Kamasani, U, Laury-Kleintop, L, Muller, AJ, Prendergast, GC

Cancer Res 2007
Participant Of
Catalyst Activity
Catalyst Activity
tryptophan 2,3-dioxygenase activity of IDO2 [cytosol]
Physical Entity
Orthologous Events
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