Dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates

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Abstract

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.

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Moretto, L., Vance, S., Heames, B., & Broadhurst, R. W. (2017). Dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates. Chemical Communications, 53(83), 11457–11460. https://doi.org/10.1039/c7cc04625a

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