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
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Body Weight / drug effects
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Diet
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Eating / drug effects
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Female
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Indoleamine-Pyrrole 2,3,-Dioxygenase / metabolism*
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Mice
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Mice, Knockout
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Niacinamide / biosynthesis
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Niacinamide / metabolism*
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Stereoisomerism
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Tryptophan / chemistry
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Tryptophan / metabolism*
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Tryptophan / pharmacology
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Tryptophan Oxygenase / deficiency
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Tryptophan Oxygenase / genetics
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Tryptophan Oxygenase / metabolism*
Substances
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Indoleamine-Pyrrole 2,3,-Dioxygenase
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Niacinamide
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Tryptophan
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Tryptophan Oxygenase