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

11 Citations (Scopus)

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

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Prenylation
Catalytic Domain
Peptides
Protein C
Substrates
Enzymes
Proteins
p21(ras) farnesyl-protein transferase
In Vitro Techniques

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Expansion of protein farnesyltransferase specificity using "tunable" active site interactions : Development of bioengineered prenylation pathways. / Hougland, James L; Gangopadhyay, Soumyashree A.; Fierke, Carol A.

In: Journal of Biological Chemistry, Vol. 287, No. 45, 02.11.2012, p. 38090-38100.

Research output: Contribution to journalArticle

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