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Computational design and selections for an engineered, thermostable terpene synthase

  • Author(s): Diaz, JE
  • Lin, CS
  • Kunishiro, K
  • Feld, BK
  • Avrantinis, SK
  • Bronson, J
  • Greaves, J
  • Saven, JG
  • Weiss, GA
  • et al.
Abstract

Terpenoids include structurally diverse antibiotics, flavorings, and fragrances. Engineering terpene synthases for control over the synthesis of such compounds represents a long sought goal. We report computational design, selections, and assays of a thermostable mutant of tobacco 5-epi-aristolochene synthase (TEAS) for the catalysis of carbocation cyclization reactions at elevated temperatures. Selection for thermostability included proteolytic digestion followed by capture of intact proteins. Unlike the wild-type enzyme, the mutant TEAS retains enzymatic activity at 65°C. The thermostable terpene synthase variant denatures above 80°C, approximately twice the temperature of the wild-type enzyme. Published by Wiley-Blackwell. © 2011 The Protein Society.

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