Participation of a medium chain acyl-CoA synthetase in glycine conjugation of the benzoic acid derivatives with the electron-donating groups

Biochemical Pharmacology
F KasuyaM Fukui

Abstract

Glycine conjugation of a series of benzoic acid derivatives was investigated in bovine liver mitochondria. Benzoic acids with chlorine, methyl, methoxy or ethoxy substituents in the para-or meta-positions of the benzene ring showed a high degree of glycine conjugation. In contrast, the acids with cyano, nitro, amino, or acetylamino groups were conjugated to a small extent with glycine. A medium chain acyl-CoA synthetase that activates carboxylic acids was purified from bovine liver mitochondria. The purified medium chain acyl-CoA synthetase accepted not only medium chain fatty acids but also aromatic and arylacetic acids as substrates. There was a good correlation between the activity of the purified medium chain acyl-CoA synthetase and glycine conjugation of ten benzoic acids with electron-donating substituents. These findings indicate that the purified medium chain acyl-CoA synthetase is a major enzyme for glycine conjugation of benzoic acids with electron-donating groups in bovine live mitochondria.

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Citations

Oct 30, 2013·Journal of Agricultural and Food Chemistry·Guangmang LiuJiayong Tang
Jun 30, 2006·Toxicology and Applied Pharmacology·Wolfgang VölkelWolfgang Dekant
Jan 25, 2006·Toxicology and Applied Pharmacology·Toshiro YamaguchiYutaka Nakamura
Apr 13, 2007·Expert Opinion on Drug Metabolism & Toxicology·Kathleen M KnightsJohn O Miners
Mar 21, 2000·Chemico-biological Interactions·F KasuyaM Fukui

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