Journal
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 37, Issue -, Pages 408-412Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BST0370408
Keywords
dioxygenase; haem; indoleamine 2,3-dioxygenase; tryptophan; tryptophan 2,3-dioxygenase
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Funding
- Engineering and Physical Sciences Research Council
- Wellcome Trust [WT083636]
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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.
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