Estimated Conversion Efficiency of Tryptophan-Nicotinamide Using an Activity Ratio of 3-Hydroxyanthranilate 3,4-dioxygenase to Aminocarboxymuconate-semialdehyde Decarboxylase in Fishes

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  • FUKUWATARI Tsutomu
    Laboratories of Food Science and Nutrition, Department of Life Style Studies, School of Human Cultures, The University of Shiga Prefecture
  • MATO Kozue
    Laboratories of Food Science and Nutrition, Department of Life Style Studies, School of Human Cultures, The University of Shiga Prefecture
  • OHTA Mari
    Laboratories of Food Science and Nutrition, Department of Life Style Studies, School of Human Cultures, The University of Shiga Prefecture
  • SASAKI Ryuzo
    Laboratories of Food Science and Nutrition, Department of Life Style Studies, School of Human Cultures, The University of Shiga Prefecture
  • SHIBATA Katsumi
    Laboratories of Food Science and Nutrition, Department of Life Style Studies, School of Human Cultures, The University of Shiga Prefecture

Bibliographic Information

Other Title
  • 魚類における3-ヒドロキシアンスラニル酸オキシゲナーゼ/アミノカルボキシムコン酸セミアルデヒド脱炭酸酵素活性比からのトリプトファン-ニコチンアミド変換率の推定
  • ギョルイ ニ オケル 3 ヒドロキシアンスラニルサン オキシゲナーゼ アミノカルボキシムコンサン セミアルデヒド ダツタンサン コウソ カッセイヒ カラ ノ トリプトファン ニコチンアミド ヘンカンリツ ノ スイテイ

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Abstract

In order to estimate the conversion efficiency of tryptophan-nicotinamide in freshwater fishes, carp and crucian, the liver 3-hydroxyanthranilate 3,4-dioxygenase (3-HAO) and aminocarboxymuconate-semialdehyde decarboxylase (ACMSD) activities were measured. The activity ratios of 3-HAO/ACMSD in carp and crucian were both around 5. These values were extremely low compared with that of rat (650), which can synsthesize a significant amount of nicotinamide from tryptophan. The activities of quinolinate phosphoribosyltransferase in carp and crucian were below the limit of detection. From these results, it was suggested that fishes cannot biosynthesize nicotinamide from tryptophan.

Journal

  • VITAMINS

    VITAMINS 78 (8), 409-411, 2004

    THE VITAMIN SOCIETY OF JAPAN

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