Expansion of protein farnesyltransferase specificity using "tunable" active site interactions: Development of bioengineered prenylation pathways

James L. Hougland, Soumyashree A. Gangopadhyay, Carol A. Fierke

Research output: Contribution to journalArticle

12 Scopus citations

Abstract

Background: FTase recognizes and modifies many proteins with C-terminal CA1A2X sequences. Results: Mutating active site residues Trp-102β and Trp-106β significantly alters FTase peptide selectivity both in vitro and in vivo. Conclusion: FTase substrate selectivity includes negative discrimination that can be relaxed/altered without losing activity. Significance: Deciphering FTase peptide recognition allows creation of bioengineered prenylation pathways and provides a model for other multispecific enzymes.

Original languageEnglish (US)
Pages (from-to)38090-38100
Number of pages11
JournalJournal of Biological Chemistry
Volume287
Issue number45
DOIs
StatePublished - Nov 2 2012

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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