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

Yasushi Yamazoe, Miki Shimada, Tetsuya Kamataki, Ryuichi Kato

    Research output: Contribution to journalArticlepeer-review

    40 Citations (Scopus)

    Abstract

    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.

    Original languageEnglish
    Pages (from-to)165-172
    Number of pages8
    JournalBiochemical and biophysical research communications
    Volume107
    Issue number1
    DOIs
    Publication statusPublished - 1982 Jul 16

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology
    • Cell Biology

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