S-Farnesylcysteine methyltransferase in bovine brain

Craig Volker, Raymond A. Miller, Jeffry Benton Stock

Research output: Contribution to journalArticle

24 Scopus citations

Abstract

Members of the ras family of GTP binding proteins, nuclear lamin B, the γ subunit of transducin, and specific yeast mating pheromones are subject to a set of post-translational modifications that culminate in methylation of the α-carboxyl group of a carboxyl-terminal S-farnesylcysteine residue. N-Acetyl-S-trans,trans-farnesyl-l-cysteine (AFC), a small molecule analog of this carboxyl-terminal amino acid, is a substrate of the carboxyl methyltransferase (KM= ∼20 μm). Here we report the synthesis and characterization of AFC and demonstrate how we have exploited its distinctive properties to develop a rapid assay for carboxyl methyltransferase activity.

Original languageEnglish (US)
Pages (from-to)283-287
Number of pages5
JournalMethods
Volume1
Issue number3
DOIs
StatePublished - Jan 1 1990

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)

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