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
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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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
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Xu, Houchao
Schnakenburg, Gregor
Goldfuss, Bernd
Dickschat, Jeroen S.
- DOI
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10.1002/anie.202306429
- URN
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urn:nbn:de:101:1-2023062315425709383195
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 10:52 AM CEST
Data provider
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Xu, Houchao
- Schnakenburg, Gregor
- Goldfuss, Bernd
- Dickschat, Jeroen S.