Inactivation of soybean sterol 24-C-methyltransferase by elongated sterol side chains at C26

Zhihong Song, W. David Nes

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

The enzymatic C-methylation reaction catalyzed by the Glycine max sterol 24-C-methyltransferase was studied with substrate analogs containing a cycloartenol nucleus (CA) and a double bond (8) or triple bond (14) attached to C26. The production of the corresponding C24(28)-methylene olefin and time-dependent inhibition kinetics of kinact 0.24 min-1 (CA-8) or 0.06 min-1 (CA-14) indicates an active-site directed process and partitioning to produce novel products.

Original languageEnglish
Pages (from-to)5902-5906
Number of pages5
JournalBioorganic and Medicinal Chemistry Letters
Volume17
Issue number21
DOIs
StatePublished - Nov 1 2007

Keywords

  • Cycloartenol
  • Mechanism-based inhibitor
  • Phytosterol
  • Sterol methylation
  • Sterol methyltransferase

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