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

Biosci Biotechnol Biochem. 2014;78(5):878-81. doi: 10.1080/09168451.2014.905185. Epub 2014 May 15.

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: biosynthesis; d-tryptophan; indoleamine 2,3-dioxygenase; nicotinamide; tryptophan 2,3-dioxygenase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Body Weight / drug effects
  • Diet
  • Eating / drug effects
  • Female
  • Indoleamine-Pyrrole 2,3,-Dioxygenase / metabolism*
  • Mice
  • Mice, Knockout
  • Niacinamide / biosynthesis
  • Niacinamide / metabolism*
  • Stereoisomerism
  • Tryptophan / chemistry
  • Tryptophan / metabolism*
  • Tryptophan / pharmacology
  • Tryptophan Oxygenase / deficiency
  • Tryptophan Oxygenase / genetics
  • Tryptophan Oxygenase / metabolism*

Substances

  • Indoleamine-Pyrrole 2,3,-Dioxygenase
  • Niacinamide
  • Tryptophan
  • Tryptophan Oxygenase