Back to Search Start Over

Exploring the mechanism of tryptophan 2,3-dioxygenase.

Authors :
Sarah J. Thackray
Christopher G. Mowat
Stephen K. Chapman
Source :
Biochemical Society Transactions; 2008, Vol. 36 Issue 6, p1120-1123, 4p
Publication Year :
2008

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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
03005127
Volume :
36
Issue :
6
Database :
Complementary Index
Journal :
Biochemical Society Transactions
Publication Type :
Academic Journal
Accession number :
44637337
Full Text :
https://doi.org/10.1042/BST0361120