Year: 2011
Type: article
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.
Source: Protein Science
DOI: 10.1002/pro.691
Authors: Juan E. Diaz, Chun‐Shi Lin, Kazuyoshi Kunishiro, Birte K. Feld, Sara K. Avrantinis, Jonathan Bronson, John Greaves, Jeffery G. Saven, Gregory A. Weiss
Institutions: University of California, Irvine, University of Pennsylvania
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: bronze
OpenAlex ID: W2107844301