Methylation of Xenobiotic Thiols by Euglena gracilis : Characterization of a Cytoplasmic Thiol Methyltransferase
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概要
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The green alga Euglena gracilis contains a thiol methyltransferase that catalyzes the S-adenosylmethionine-dependent methylation of pentachlorobenzenethiol. The enzyme was localized in the cytoplasm and partially purified. The pH optimum for the enzyme was 6.5. The enzyme methylated a number of foreign thiols, but not the cellular thiols, glutathione or cysteine. Phenols and anilines were not substrates. When pentachlorobenzenethiol was the methyl acceptor the K_m was found to be 82μM and the corresponding K_m for S-adenosylmethionine was 140μM. The molecular weight of the enzyme was 21.000, as determined by gel filtration. A role for this enzyme in detoxifying xenobiotic thiols is proposed.
- 日本植物生理学会の論文
著者
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Fall Ray
Department Of Chemistry And Cooperative Institute For Research In Environmental Sciences University
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Drotar AnnaMarie
Department of Chemistry, and Cooperative Institute for Research in Environmental Sciences, Universit
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Drotar Annamarie
Department Of Chemistry And Cooperative Institute For Research In Environmental Sciences University
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Fall Ray
Department Of Chemistry And Biochemistry University Of Colorado
関連論文
- Methylation of Xenobiotic Thiols by Euglena gracilis : Characterization of a Cytoplasmic Thiol Methyltransferase
- Evidence of Isoprenoid Precursor Toxicity in Bacillus subtilis