Journal
PROTEIN SCIENCE
Volume 20, Issue 9, Pages 1597-1606Publisher
WILEY-BLACKWELL
DOI: 10.1002/pro.691
Keywords
terpene synthases; protein-engineering; phage display; thermostability
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Funding
- Arnold and Mabel Beckman Foundation
- National Institutes of Health [GM61267]
- National Institute of General Medical Sciences [1 R01 GM078528-01]
- Petroleum Research Fund [40902-G4]
- NSF [DMR 05-20020]
- Kyoto Pharmaceuticals
- American Chemical Society Division of Organic Chemistry
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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 degrees C. The thermostable terpene synthase variant denatures above 80 degrees C, approximately twice the temperature of the wild-type enzyme.
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