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2014•Bioscience Biotechnology and BiochemistryOpen access

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

Akihiro Maeta, Mitsue Sano, Tsutomu Fukuwatari, Hiroshi Funakoshi, Toshikazu Nakamura, Katsumi Shibata

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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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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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Available 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.

Key concepts: Indoleamine 2,3-dioxygenase, Tryptophan, Nicotinamide, Dioxygenase, Chemistry, Tryptophan Metabolism, Biochemistry, Amino acid

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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 — Research Paper | ScholarLens