Covalent binding of N-hydroxy-Trp-P-2 to DNA by cytosolic proline-dependent system

Yasushi Yamazoe, Miki Shimada, Tetsuya Kamataki, Ryuichi Kato

    研究成果: Article査読

    40 被引用数 (Scopus)

    抄録

    A new enzymatic activation system for the covalent binding of a mutagenic metabolite of a tryptophan pyrolysate, N-hydroxy-Trp-P-2, is described. The system exists in hepatic cytosolic fraction of rats, requiring ATP and some amino acids as the cofactor. Proline was the most effective among amino acids examined. These results suggest that N-hydroxy-Trp-P-2 formed by microsomal cytochrome P-450 is activated by prolyl-tRNA synthetase or related enzyme(s). Possible roles of sulfation and acetylation in the formation of the covalent adducts were also discussed.

    本文言語English
    ページ(範囲)165-172
    ページ数8
    ジャーナルBiochemical and biophysical research communications
    107
    1
    DOI
    出版ステータスPublished - 1982 7 16

    ASJC Scopus subject areas

    • 生物理学
    • 生化学
    • 分子生物学
    • 細胞生物学

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