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