1. Current understanding and biotechnological application of the bacterial diterpene synthase CotB2
- Author
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Norbert Mehlmer, Keren Raz, Ronja Driller, Bernhard Loll, Monika Fuchs, Thomas Brück, Dan Thomas Major, and Daniel Garbe
- Subjects
crystal structure ,Streptomyces melanosporofaciens ,Reaction mechanism ,cyclooctatin ,Mutagenesis (molecular biology technique) ,terpene synthase ,Review ,010402 general chemistry ,01 natural sciences ,diterpene ,lcsh:QD241-441 ,chemistry.chemical_compound ,lcsh:Organic chemistry ,Biosynthesis ,Cyclooctatin ,lcsh:Science ,chemistry.chemical_classification ,biology ,ATP synthase ,010405 organic chemistry ,Crystal structure ,Organic Chemistry ,Terpene synthase ,Combinatorial chemistry ,ddc ,0104 chemical sciences ,Chemistry ,Enzyme ,chemistry ,Committed step ,biology.protein ,lcsh:Q ,cotb2 ,reaction mechanism ,Diterpene ,CotB2 ,biotechnology ,Biotechnology - Abstract
CotB2 catalyzes the first committed step in cyclooctatin biosynthesis of the soil bacterium Streptomyces melanosporofaciens. To date, CotB2 represents the best studied bacterial diterpene synthase. Its reaction mechanism has been addressed by isoptope labeling, targeted mutagenesis and theoretical computations in the gas phase, as well as full enzyme molecular dynamic simulations. By X-ray crystallography different snapshots of CotB2 from the open, inactive, to the closed, active conformation have been obtained in great detail, allowing us to draw detailed conclusions regarding the catalytic mechanism at the molecular level. Moreover, numerous alternative geranylgeranyl diphosphate cyclization products obtained by CotB2 mutagenesis have exciting applications for the sustainable production of high value bioactive substances.
- Published
- 2019
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