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

1996; Elsevier BV; Volume: 51; Issue: 6 Linguagem: Inglês

10.1016/0006-2952(95)02399-2

1873-2968

Fumiyo Kasuya, Kazuo Igarashi, Miyoshi Fukui,

Biochemical Acid Research Studies

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.