Please use this identifier to cite or link to this item:
Title: Substrate Oxidation by Indoleamine 2,3-Dioxygenase : EVIDENCE FOR A COMMON REACTION MECHANISM
Authors: Booth, E. S.
Basran, J.
Lee, M.
Handa, S.
Raven, Emma L.
First Published: 25-Dec-2015
Publisher: American Society for Biochemistry and Molecular Biology
Citation: Journal of Biological Chemistry, 2015, 290 (52), pp. 30924-30930
Abstract: The kynurenine pathway is the major route of l-tryptophan (l-Trp) catabolism in biology, leading ultimately to the formation of NAD(+). The initial and rate-limiting step of the kynurenine pathway involves oxidation of l-Trp to N-formylkynurenine. This is an O2-dependent process and catalyzed by indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase. More than 60 years after these dioxygenase enzymes were first isolated (Kotake, Y., and Masayama, I. (1936) Z. Physiol. Chem. 243, 237-244), the mechanism of the reaction is not established. We examined the mechanism of substrate oxidation for a series of substituted tryptophan analogues by indoleamine 2,3-dioxygenase. We observed formation of a transient intermediate, assigned as a Compound II (ferryl) species, during oxidation of l-Trp, 1-methyl-l-Trp, and a number of other substrate analogues. The data are consistent with a common reaction mechanism for indoleamine 2,3-dioxygenase-catalyzed oxidation of tryptophan and other tryptophan analogues.
DOI Link: 10.1074/jbc.M115.695684
ISSN: 0021-9258
eISSN: 1083-351X
Version: Publisher Version
Status: Peer-reviewed
Type: Journal Article
Rights: Copyright © 2015 by The American Society for Biochemistry and Molecular Biology, Inc. Final version free via Creative Commons CC-BY license ( ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Appears in Collections:Published Articles, Dept. of Chemistry

Files in This Item:
File Description SizeFormat 
J. Biol. Chem.-2015-Booth-30924-30.pdfPublished (publisher PDF)674.74 kBAdobe PDFView/Open

Items in LRA are protected by copyright, with all rights reserved, unless otherwise indicated.