Dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates
Royal Society of Chemistry
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Moretto, L., Vance, S., Heames, B., & Broadhurst, B. (2017). Dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates. Chemical Communications, 53 11457-11460. https://doi.org/10.1039/c7cc04625a
Interaction studies using fragments excised from the modular mycolactone polyketide synthase show that ketoreductase domains possess a generic binding site for acyl carrier protein domains and provide evidence that the pendant 5′-phosphopantetheine prosthetic group plays a key role in delivering acyl substrates to the active site in the correct orientation.
The authors would like to thank the Wellcome Trust (grant number 094252/Z/10/Z) for funding this research. LM was supported by an EPSRC PhD studentship.
Wellcome Trust (094252/Z/10/Z)
External DOI: https://doi.org/10.1039/c7cc04625a
This record's URL: https://www.repository.cam.ac.uk/handle/1810/279838
Attribution 4.0 International (CC BY 4.0)
Licence URL: https://creativecommons.org/licenses/by/4.0/