Exploring the mechanism of tryptophan 2,3-dioxygenase

Sarah J Thackray, Christopher G Mowat, Stephen K Chapman

    Research output: Contribution to journalArticle

    62 Citations (Scopus)

    Abstract

    The haem proteins TDO (tryptophan 2,3-dioxygenase) and IDO (indoleamine 2,3-dioxygenase) are specific and powerful oxidation catalysts that insert one molecule of dioxygen into L-tryptophan in the first and rate-limiting step in the kynurenine pathway. Recent crystallographic and biochemical analyses of TDO and IDO have greatly aided our understanding of the mechanisms employed by these enzymes in the binding and activation of dioxygen and tryptophan. In the present paper, we briefly discuss the function, structure and possible catalytic mechanism of these enzymes.

    Original languageEnglish
    Pages (from-to)1120-1123
    Number of pages4
    JournalBiochemical Society Transactions
    Volume36
    Issue number6
    DOIs
    Publication statusPublished - Dec 2008

    Keywords

    • REDOX
    • CATALYSIS
    • oxygen
    • ENZYMES
    • haem
    • indoleamine 2,3-dioxygenase
    • tryptophan 2,3-dioxygenase
    • kynurenine
    • HUMAN INDOLEAMINE 2,3-DIOXYGENASE
    • CATABOLISM
    • CRYSTAL-STRUCTURE

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