Author pages are created from data sourced from our academic publisher partnerships and public sources.
Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase.
- H. Sugimoto, S. Oda, T. Otsuki, T. Hino, T. Yoshida, Y. Shiro
- Medicine, Chemistry
- Proceedings of the National Academy of Sciences…
- 21 February 2006
Human indoleamine 2,3-dioxygenase (IDO) catalyzes the cleavage of the pyrrol ring of L-Trp and incorporates both atoms of a molecule of oxygen (O2). Here we report on the x-ray crystal structure of… Expand
Crystal structure of human indoleamine 2,3-dioxygenase
Crystallization and preliminary crystallographic studies of human indoleamine 2,3-dioxygenase.
- S. Oda, H. Sugimoto, T. Yoshida, Y. Shiro
- Chemistry, Medicine
- Acta crystallographica. Section F, Structural…
- 1 March 2006
Indoleamine 2,3-dioxygenase (IDO) is a haem-containing dioxygenase that catalyzes the oxidative cleavage of the pyrrole ring of indoleamines by the insertion of molecular oxygen. This reaction is the… Expand
X-ray structure and reaction mechanism of human indoleamine 2,3-dioxygenase
Abstract The oxidative cleavage of the pyrrole ring of indoleamines by the insertion of molecular oxygen is catalyzed by indoleamine 2,3-dioxygenase (IDO). The reaction involves the addition of both… Expand
Crystal structure of 4-phenylimidazole bound form of human indoleamine 2,3-dioxygenase
Structure of poxvirus K7 protein in complex with RNA helicase DDX3
Crystal Structure of Marburg virus VP40 Dimer
Crystal structure of cyanide bound form of human indoleamine 2,3-dioxygenase