Mechanism-based active site modification of sterol methyl transferase by tritium-labeled 26-homocholesta-8,14,24-trien-26-yn-3β-ol

W. David Nes, Julie A. Marshall, Wen Zhou, Ling He, Allen L. Dennis

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

The title compound (26-HC, 5) was synthesized and tested as a mechanism- based inhibitor of the sterol methyl transferase (SMT) enzyme from Saccharomyces cerevisiae. Enzyme assays were performed with SMT enzyme using zymosterol as substrate and AdoMet as coenzyme. The inhibition of SMT enzyme by 26-HC showed an apparent k(i) of 72.5 μM and k(inact) of 2.4 min-1. Covalent modification of the active site of a SMT enzyme was demonstrated for the first time using [3-3H]26-HC.

Original languageEnglish
Pages (from-to)8575-8578
Number of pages4
JournalTetrahedron Letters
Volume39
Issue number47
DOIs
StatePublished - Nov 19 1998

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