Rerouting and Improving Dauc‐8‐en‐11‐ol Synthase from Streptomyces venezuelae to a High Yielding Biocatalyst

The dauc‐8‐en‐11‐ol synthase from Streptomyces venezuelae was investigated for its catalytic activity towards alternative terpene precursors, specifically designed to enable new cyclisation pathways. Exchange of aromatic amino acid residues at the enzyme surface by site‐directed mutagenesis led to a...

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Detalles Bibliográficos
Autores principales: Lauterbach, Lukas, Hou, Anwei, Dickschat, Jeroen S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2021
Materias:
Full Papers
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8252471/
https://www.ncbi.nlm.nih.gov/pubmed/33769623
http://dx.doi.org/10.1002/chem.202100962
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author Lauterbach, Lukas
Hou, Anwei
Dickschat, Jeroen S.
author_facet Lauterbach, Lukas
Hou, Anwei
Dickschat, Jeroen S.
author_sort Lauterbach, Lukas
collection PubMed
description The dauc‐8‐en‐11‐ol synthase from Streptomyces venezuelae was investigated for its catalytic activity towards alternative terpene precursors, specifically designed to enable new cyclisation pathways. Exchange of aromatic amino acid residues at the enzyme surface by site‐directed mutagenesis led to a 4‐fold increase of the yield in preparative scale incubations, which likely results from an increased enzyme stability instead of improved enzyme kinetics.
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spelling pubmed-82524712021-07-07 Rerouting and Improving Dauc‐8‐en‐11‐ol Synthase from Streptomyces venezuelae to a High Yielding Biocatalyst Lauterbach, Lukas Hou, Anwei Dickschat, Jeroen S. Chemistry Full Papers The dauc‐8‐en‐11‐ol synthase from Streptomyces venezuelae was investigated for its catalytic activity towards alternative terpene precursors, specifically designed to enable new cyclisation pathways. Exchange of aromatic amino acid residues at the enzyme surface by site‐directed mutagenesis led to a 4‐fold increase of the yield in preparative scale incubations, which likely results from an increased enzyme stability instead of improved enzyme kinetics. John Wiley and Sons Inc. 2021-05-01 2021-05-20 /pmc/articles/PMC8252471/ /pubmed/33769623 http://dx.doi.org/10.1002/chem.202100962 Text en © 2021 The Authors. Chemistry - A European Journal 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 Full Papers
Lauterbach, Lukas
Hou, Anwei
Dickschat, Jeroen S.
Rerouting and Improving Dauc‐8‐en‐11‐ol Synthase from Streptomyces venezuelae to a High Yielding Biocatalyst
title Rerouting and Improving Dauc‐8‐en‐11‐ol Synthase from Streptomyces venezuelae to a High Yielding Biocatalyst
title_full Rerouting and Improving Dauc‐8‐en‐11‐ol Synthase from Streptomyces venezuelae to a High Yielding Biocatalyst
title_fullStr Rerouting and Improving Dauc‐8‐en‐11‐ol Synthase from Streptomyces venezuelae to a High Yielding Biocatalyst
title_full_unstemmed Rerouting and Improving Dauc‐8‐en‐11‐ol Synthase from Streptomyces venezuelae to a High Yielding Biocatalyst
title_short Rerouting and Improving Dauc‐8‐en‐11‐ol Synthase from Streptomyces venezuelae to a High Yielding Biocatalyst
title_sort rerouting and improving dauc‐8‐en‐11‐ol synthase from streptomyces venezuelae to a high yielding biocatalyst
topic Full Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8252471/
https://www.ncbi.nlm.nih.gov/pubmed/33769623
http://dx.doi.org/10.1002/chem.202100962
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