Oxidation of L-tryptophan in biology: A comparison between tryptophan 2,3-dioxygenase and indoleamine 2,3-dioxygenase

Sara A. Rafice, Nishma Chauhan, Igor Efimov, Jaswir Basran, Emma Lloyd Raven*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

59 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)408-412
Number of pages5
JournalBiochemical Society Transactions
Volume37
Issue number2
DOIs
Publication statusPublished - 3 Aug 2009

Keywords

  • Dioxygenase
  • Haem
  • Indoleamine 2,3-dioxygenase
  • Tryptophan
  • Tryptophan 2,3-dioxygenase

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