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Plant and Cell Physiology, 1985, Vol. 26, No. 5 847-854
© 1985


Article

Methylation of Xenobiotic Thiols by Euglena gracilis: Characterization of a Cytoplasmic Thiol Methyltransferase

AnnaMarie Drotar and Ray Fall

Department of Chemistry, and Cooperative Institute for Research in Environmental Sciences, University of Colorado Boulder, CO 80309 U.S.A.

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 pentachloro-benzenethiol was the methyl acceptor the Km was found to be 82 µM and the corresponding Km for S-adenosylmethionine was 140 µM. 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.

(Received September 28, 1984; Accepted April 25, 1985)
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