Abstract
A methyltransferase(s) that catalyzes the transfer of the methyl group from S-adenosylmethionine to a sterol acceptor was solubilized with Triton X-100 and partially purified from bean rust uredospores ( Uromyces phaseoli). Zymosterol was the most active substrate tested while desmosterol and lanosterol exhibited good activity. The products were sterols with either a methylene or ethylidene group at the C-24 position. Direct evidence for the synthesis of the ethylidene group was obtained by using 24-methylenecholesterol as a substrate.
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