Correction: 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
TL;DR
This paper corrects a previous study on using an enzyme's flexibility to create new antibiotic compounds.
Contribution
The paper provides corrections to prior findings on enzyme promiscuity in antibiotic synthesis.
Findings
Errors in the original study's methodology are identified and corrected.
The acyl transferase's promiscuity is confirmed but with revised experimental details.
New data supports the potential for creating diverse antibiotic analogues.
Abstract
Correction for ‘Exploiting the inherent promiscuity of the acyl transferase of the stambomycin polyketide synthase for the mutasynthesis of analogues’ by Li Su et al., Chem. Sci., 2025, https://doi.org/10.1039/d4sc06976e.
- —Université de Lorraine10.13039/100008990
- —Centre National de la Recherche Scientifique10.13039/501100004794
- —Max-Planck-Gesellschaft10.13039/501100004189
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Taxonomy
TopicsMicrobial Natural Products and Biosynthesis · Chemical Synthesis and Analysis · Enzyme Catalysis and Immobilization
The authors hereby amend the Acknowledgements section of their published article to thank Dr Benjamin Chagot for NMR analysis of certain fed substrates.
The Royal Society of Chemistry apologises for these errors and any consequent inconvenience to authors and readers.