Exploiting the inherent promiscuity of the acyl transferase of the stambomycin polyketide synthase for the mutasynthesis of analogues

Li Su; Yaouba Souaibou; Laurence Hôtel; Christophe Jacob; Peter Grün; Yan-Ni Shi; Alicia Chateau; Sophie Pinel; Helge B. Bode; Bertrand Aigle; Kira J. Weissman

doi:10.1101/2024.10.29.620781

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Exploiting the inherent promiscuity of the acyl transferase of the stambomycin polyketide synthase for the mutasynthesis of analogues

View ORCID ProfileLi Su, View ORCID ProfileYaouba Souaibou, Laurence Hôtel, View ORCID ProfileChristophe Jacob, Peter Grün, View ORCID ProfileYan-Ni Shi, Alicia Chateau, View ORCID ProfileSophie Pinel, View ORCID ProfileHelge B. Bode, View ORCID ProfileBertrand Aigle, View ORCID ProfileKira J. Weissman

doi: https://doi.org/10.1101/2024.10.29.620781

Li Su

aUniversité de Lorraine, CNRS, IMoPA, F-54000 Nancy, France

bUniversité de Lorraine, INRAE, DynAMic, F-54000 Nancy, France

cMax-Planck-Institute for Terrestrial Microbiology, Department of Natural Products in Organismic Interactions, 35043 Marburg, Germany

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ORCID record for Li Su

Yaouba Souaibou

aUniversité de Lorraine, CNRS, IMoPA, F-54000 Nancy, France

bUniversité de Lorraine, INRAE, DynAMic, F-54000 Nancy, France

dIPHC, UMR 7178, CNRS, Université de Strasbourg, Equipe de Chimie Analytique des Molécules Bioactives et Pharmacognosie, Illkirch, France

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Laurence Hôtel

bUniversité de Lorraine, INRAE, DynAMic, F-54000 Nancy, France

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Christophe Jacob

aUniversité de Lorraine, CNRS, IMoPA, F-54000 Nancy, France

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Peter Grün

cMax-Planck-Institute for Terrestrial Microbiology, Department of Natural Products in Organismic Interactions, 35043 Marburg, Germany

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Yan-Ni Shi

cMax-Planck-Institute for Terrestrial Microbiology, Department of Natural Products in Organismic Interactions, 35043 Marburg, Germany

fMolecular Biotechnology, Department of Biosciences, Goethe University Frankfurt, 60438 Frankfurt am Main, Germany

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Alicia Chateau

eUniversité de Lorraine, CNRS, CRAN, F-54000 Nancy, France

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Sophie Pinel

eUniversité de Lorraine, CNRS, CRAN, F-54000 Nancy, France

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Helge B. Bode

cMax-Planck-Institute for Terrestrial Microbiology, Department of Natural Products in Organismic Interactions, 35043 Marburg, Germany

fMolecular Biotechnology, Department of Biosciences, Goethe University Frankfurt, 60438 Frankfurt am Main, Germany

gChemical Biology, Department of Chemistry, Philipps University of Marburg, 35043 Marburg, Germany

hSenckenberg Gesellschaft für Naturforschung, 60325 Frankfurt am Main, Germany

iCenter for Synthetic Microbiology (SYNMIKRO), University of Marburg, 35043 Marburg, Germany

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Bertrand Aigle

bUniversité de Lorraine, INRAE, DynAMic, F-54000 Nancy, France

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For correspondence: bertrand.aigle@univ-lorraine.fr

Kira J. Weissman

aUniversité de Lorraine, CNRS, IMoPA, F-54000 Nancy, France

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For correspondence: bertrand.aigle@univ-lorraine.fr

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Posted October 29, 2024.

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Exploiting the inherent promiscuity of the acyl transferase of the stambomycin polyketide synthase for the mutasynthesis of analogues

Li Su, Yaouba Souaibou, Laurence Hôtel, Christophe Jacob, Peter Grün, Yan-Ni Shi, Alicia Chateau, Sophie Pinel, Helge B. Bode, Bertrand Aigle, Kira J. Weissman

bioRxiv 2024.10.29.620781; doi: https://doi.org/10.1101/2024.10.29.620781

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Exploiting the inherent promiscuity of the acyl transferase of the stambomycin polyketide synthase for the mutasynthesis of analogues

Li Su, Yaouba Souaibou, Laurence Hôtel, Christophe Jacob, Peter Grün, Yan-Ni Shi, Alicia Chateau, Sophie Pinel, Helge B. Bode, Bertrand Aigle, Kira J. Weissman

bioRxiv 2024.10.29.620781; doi: https://doi.org/10.1101/2024.10.29.620781

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