Yeast protein farnesyltransferase. Binding of S-alkyl peptides and related analogues

David B. Rozema, Scott T. Phillips, C. Dale Poulter

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

Formula presented Protein farnesyltransferase (PFTase) catalyzes alkylation of cysteine residues by farnesyl diphosphate (FPP). The dissociation constants for the PFTase-peptide analogue complexes for the series of analogues fl-RTRC(X)VIA (X = H, methyl, dodecyl, farnesyl) were measured by fluorescence anisotropy. The results indicate that an ionizable sulfhydryl moiety is important for substrate binding and the farnesyl group in the product facilitates binding.

Original languageEnglish (US)
Pages (from-to)815-817
Number of pages3
JournalOrganic Letters
Volume1
Issue number5
DOIs
StatePublished - Sep 9 1999

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Physical and Theoretical Chemistry
  • Organic Chemistry

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