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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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