Evolution of Vertebrate Indoleamine 2,3-Dioxygenases
✍ Scribed by Hajime Julie Yuasa; Miwa Takubo; Ayumi Takahashi; Tetsuo Hasegawa; Hiroshi Noma; Tomohiko Suzuki
- Publisher
- Springer
- Year
- 2007
- Tongue
- English
- Weight
- 439 KB
- Volume
- 65
- Category
- Article
- ISSN
- 0022-2844
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## Abstract The first and rate‐limiting step of the kynurenine pathway, in which tryptophan (Trp) is converted to __N__‐formylkynurenine is catalyzed by two heme‐containing proteins, Indoleamine 2,3‐dioxygenase (IDO), and Tryptophan 2,3‐dioxygenase (TDO). In mammals, TDO is found exclusively in liv
## Abstract Human indoleamine 2,3‐dioxygenase (hIDO), a monomeric heme enzyme, catalyzes the oxidative degradation of L‐tryptophan (L‐Trp) and other indoleamine derivatives. Its activity follows typical Michaelis–Menten behavior only for L‐Trp concentrations up to 50 μM; a further increase in the c
Indoleamine 2,3-dioxygenase (IDO) is a tryptophan catabolizing enzyme that has a number of immunoregulatory effects. It is expressed at high levels in the gastrointestinal tract, particularly in the small intestine, and has been implicated in the control of intestinal inflammation. However, its prec