Current understanding and biotechnological application of the bacterial diterpene synthase CotB2

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DOI

  • Ronja Driller
  • Daniel Garbe, Technical University of Munich (TUM)
  • ,
  • Norbert Mehlmer, Technical University of Munich (TUM)
  • ,
  • Monika Fuchs, Technical University of Munich (TUM)
  • ,
  • Keren Raz, Bar-Ilan University
  • ,
  • Dan Thomas Major, Bar-Ilan University
  • ,
  • Thomas Brück, Technical University of Munich (TUM)
  • ,
  • Bernhard Loll, Free University of Berlin

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.

Original languageEnglish
JournalBeilstein Journal of Organic Chemistry
Volume15
Pages (from-to)2355-2368
Number of pages14
ISSN2195-951X
DOIs
Publication statusPublished - 2019

    Research areas

  • Biotechnology, CotB2, Crystal structure, Cyclooctatin, Diterpene, Reaction mechanism, Terpene synthase

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