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 |
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Authors: | Akihiro Maeta Mitsue Sano Tsutomu Fukuwatari Hiroshi Funakoshi Toshikazu Nakamura |
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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 |
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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. |
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Keywords: | smallcaps smallerCapital" >d-tryptophan biosynthesis tryptophan 2,3-dioxygenase indoleamine 2,3-dioxygenase nicotinamide |
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