Oxidation of L-tryptophan in biology: a comparison between tryptophan 2,3-dioxygenase and indoleamine 2,3-dioxygenase.
Article Details
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Rafice SA, Chauhan N, Efimov I, Basran J, Raven EL
Oxidation of L-tryptophan in biology: a comparison between tryptophan 2,3-dioxygenase and indoleamine 2,3-dioxygenase.
Biochem Soc Trans. 2009 Apr;37(Pt 2):408-12. doi: 10.1042/BST0370408.
- PubMed ID
- 19290871 [ View in PubMed]
- Abstract
The family of haem dioxygenases catalyse the initial oxidative cleavage of L-tryptophan to N-formylkynurenine, which is the first, rate-limiting, step in the L-kynurenine pathway. In the present paper, we discuss and compare structure and function across the family of haem dioxygenases by focusing on TDO (tryptophan 2,3-dioxygenase) and IDO (indoleamine 2,3-dioxygenase), including a review of recent structural information for both enzymes. The present paper describes how the recent development of recombinant expression systems has informed our more detailed understanding of the substrate binding, catalytic activity and mechanistic properties of these haem dioxygenases.
DrugBank Data that Cites this Article
- Drug Enzymes
Drug Enzyme Kind Organism Pharmacological Action Actions Tryptophan Indoleamine 2,3-dioxygenase 1 Protein Humans UnknownSubstrateDetails Tryptophan Tryptophan 2,3-dioxygenase Protein Humans UnknownSubstrateDetails