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Mechanistic Characterisation and Engineering of Sesterviolene Synthase from Streptomyces violens
The sesterviolene synthase from Streptomyces violens was identified and represents the second known sesterterpene synthase from bacteria. Isotopic labelling experiments in conjunction with DFT calculations were performed that provided detailed insight into its complex cyclisation mechanism. Enzyme e...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10107272/ https://www.ncbi.nlm.nih.gov/pubmed/36350768 http://dx.doi.org/10.1002/anie.202215688 |
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author | Gu, Binbin Goldfuss, Bernd Dickschat, Jeroen S. |
author_facet | Gu, Binbin Goldfuss, Bernd Dickschat, Jeroen S. |
author_sort | Gu, Binbin |
collection | PubMed |
description | The sesterviolene synthase from Streptomyces violens was identified and represents the second known sesterterpene synthase from bacteria. Isotopic labelling experiments in conjunction with DFT calculations were performed that provided detailed insight into its complex cyclisation mechanism. Enzyme engineering through site‐directed mutagenesis gave access to a high‐yielding enzyme variant that provided six additional minor products and the main product in sufficient quantities to study its chemistry. |
format | Online Article Text |
id | pubmed-10107272 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-101072722023-04-18 Mechanistic Characterisation and Engineering of Sesterviolene Synthase from Streptomyces violens Gu, Binbin Goldfuss, Bernd Dickschat, Jeroen S. Angew Chem Int Ed Engl Communications The sesterviolene synthase from Streptomyces violens was identified and represents the second known sesterterpene synthase from bacteria. Isotopic labelling experiments in conjunction with DFT calculations were performed that provided detailed insight into its complex cyclisation mechanism. Enzyme engineering through site‐directed mutagenesis gave access to a high‐yielding enzyme variant that provided six additional minor products and the main product in sufficient quantities to study its chemistry. John Wiley and Sons Inc. 2022-12-01 2023-01-02 /pmc/articles/PMC10107272/ /pubmed/36350768 http://dx.doi.org/10.1002/anie.202215688 Text en © 2022 The Authors. Angewandte Chemie International Edition published by Wiley-VCH GmbH https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Communications Gu, Binbin Goldfuss, Bernd Dickschat, Jeroen S. Mechanistic Characterisation and Engineering of Sesterviolene Synthase from Streptomyces violens |
title | Mechanistic Characterisation and Engineering of Sesterviolene Synthase from Streptomyces violens
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title_full | Mechanistic Characterisation and Engineering of Sesterviolene Synthase from Streptomyces violens
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title_fullStr | Mechanistic Characterisation and Engineering of Sesterviolene Synthase from Streptomyces violens
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title_full_unstemmed | Mechanistic Characterisation and Engineering of Sesterviolene Synthase from Streptomyces violens
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title_short | Mechanistic Characterisation and Engineering of Sesterviolene Synthase from Streptomyces violens
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title_sort | mechanistic characterisation and engineering of sesterviolene synthase from streptomyces violens |
topic | Communications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10107272/ https://www.ncbi.nlm.nih.gov/pubmed/36350768 http://dx.doi.org/10.1002/anie.202215688 |
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