Mechanistic Characterisation of the Bacterial Sesterviridene Synthase from Kitasatospora viridis

Abstract: A gene coding for a terpene synthase homolog from Kitasatospora viridis was cloned and expressed in Escherichia coli. The purified recombinant protein possessed sesterterpene synthase activity and efficiently converted geranylfarnesyl diphosphate (GFPP) with 19 % yield into the sesterterpene hydrocarbon sesterviridene A. Large scale enzymatic conversions also allowed for the isolation of two side products that are generated with very low yields of ca. 0.1 %. Several derivatives of sesterviridene A were obtained by chemical transformations, securing the NMR‐based structural assignments. The absolute configuration of sesterviridene A was determined by chemical correlation using stereoselectively deuterated precursors and by anomalous dispersion X‐ray crystallography. The cyclisation mechanism from GFPP to sesterviridene A was extensively studied through isotopic labelling experiments and DFT calculations.

Location
Deutsche Nationalbibliothek Frankfurt am Main
Extent
Online-Ressource
Language
Englisch

Bibliographic citation
Mechanistic Characterisation of the Bacterial Sesterviridene Synthase from Kitasatospora viridis ; day:23 ; month:06 ; year:2023 ; extent:6
Angewandte Chemie / International edition. International edition ; (23.06.2023) (gesamt 6)

Creator
Xu, Houchao
Schnakenburg, Gregor
Goldfuss, Bernd
Dickschat, Jeroen S.

DOI
10.1002/anie.202306429
URN
urn:nbn:de:101:1-2023062315425709383195
Rights
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
Last update
14.08.2025, 10:52 AM CEST

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Associated

  • Xu, Houchao
  • Schnakenburg, Gregor
  • Goldfuss, Bernd
  • Dickschat, Jeroen S.

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