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

Yasushi Yamazoe; Miki Shimada; Tetsuya Kamataki; Ryuichi Kato

doi:10.1016/0006-291X(82)91684-9

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 journal › Article › peer-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 language	English
Pages (from-to)	165-172
Number of pages	8
Journal	Biochemical and biophysical research communications
Volume	107
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(82)91684-9
Publication status	Published - 1982 Jul 16

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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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.",

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AU - Kato, Ryuichi

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