Biosynthesis of yeast sterols Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/7h149s741

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  • An enzyme system from cell-free yeast homogenates mediating the transfer of the methyl group from S-adenosylmethionine-methyl-C¹⁴ or methionine-methyl-C¹⁴ to C-28 of ergosterol has been studied. The effects of divalent cations, suithydryl inhibitors and reducing substances on the activity of the enzyme system have been investigated. It was established that for maximal activity, the system requires adenosine triphosphate, glucose-6-phosphate, ascorbic acid, potassium acetate, and Mn⁺⁺ sterol synthesis was inhibited by N-ethylmalimide and p-chloromecurabenzoate. Aging of the enzyme preparation is accompanied by a rapid loss of enzymic activity. The reaction has been shown to occur in whole cells as well as cell-free homogenates. The reaction, therefore, appears to be physiologically important in the biosynthesis of ergosterol in yeast. Data obtained by separation of the labeled sterols isolated from cell-free and whole cell experiments indicate that transmethylation occurs at least two steps prior to the formation of ergosterol in the biosynthetic pathway.
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