Computational design and selections for an engineered, thermostable terpene synthase

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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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CITATION STYLE

APA

Diaz, J. E., Lin, C. S., Kunishiro, K., Feld, B. K., Avrantinis, S. K., Bronson, J., … Weiss, G. A. (2011). Computational design and selections for an engineered, thermostable terpene synthase. Protein Science, 20(9), 1597–1606. https://doi.org/10.1002/pro.691

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