A sterol methyltransferase from bean rust uredospores, Uromyces phaseoli☆

Autor: Hung-Kuang Lin, Herman W. Knoche
Rok vydání: 1976
Předmět:
Zdroj: Phytochemistry. 15:683-687
ISSN: 0031-9422
DOI: 10.1016/s0031-9422(00)94421-2
Popis: 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.
Databáze: OpenAIRE