TY - JOUR
T1 - Covalent binding of N-hydroxy-Trp-P-2 to DNA by cytosolic proline-dependent system
AU - Yamazoe, Yasushi
AU - Shimada, Miki
AU - Kamataki, Tetsuya
AU - Kato, Ryuichi
PY - 1982/7/16
Y1 - 1982/7/16
N2 - 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.
AB - 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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U2 - 10.1016/0006-291X(82)91684-9
DO - 10.1016/0006-291X(82)91684-9
M3 - Article
C2 - 7126201
AN - SCOPUS:0020485166
VL - 107
SP - 165
EP - 172
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -