Contributions of tryptophan 2,3-dioxygenase and indoleamine 2,3-dioxygenase to the conversion of d-tryptophan to nicotinamide analyzed by using tryptophan 2,3-dioxygenase-knockout mice-Reference-Cited by-同舟云学术

Contributions of tryptophan 2,3-dioxygenase and indoleamine 2,3-dioxygenase to the conversion of d-tryptophan to nicotinamide analyzed by using tryptophan 2,3-dioxygenase-knockout mice

Published:2014-05-04 Issue:5 Volume:78 Page:878-881
ISSN:0916-8451
Container-title:Bioscience, Biotechnology, and Biochemistry
language:en
Short-container-title:

Author:

Maeta Akihiro¹,Sano Mitsue¹,Fukuwatari Tsutomu¹,Funakoshi Hiroshi²,Nakamura Toshikazu³,Shibata Katsumi¹

Affiliation:

1. Department of Nutrition, School of Human Cultures, The University of Shiga Prefecture, Hikone, Japan

2. Division of Molecular Regenerative Medicine, Department of Biochemistry and Molecular Biology, Asahikawa Medical University, Asahikawa, Japan

3. Kringle Pharma Joint Research Division for Regenerative Drug Discovery, Center for Advanced Science and Innovation, Osaka University, Osaka, Japan

Abstract

Abstract We investigated the contribution percentage of tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) to the conversion of d-tryptophan to nicotinamide in TDO-knockout mice. The calculated percentage conversions indicated that TDO and IDO oxidized 70 and 30%, respectively, of the dietary l-tryptophan. These results indicate that both TDO and IDO biosynthesize nicotinamide from d-tryptophan and l-tryptophan in mice.

Publisher

Oxford University Press (OUP)

Subject

Organic Chemistry,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Biochemistry,Analytical Chemistry,Biotechnology

Link

http://academic.oup.com/bbb/article-pdf/78/5/878/36800988/bbb0878.pdf

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