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Issue 83, 2017
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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.

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

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Publication details

The article was received on 15 Jun 2017, accepted on 29 Jun 2017 and first published on 05 Oct 2017


Article type: Communication
DOI: 10.1039/C7CC04625A
Citation: Chem. Commun., 2017,53, 11457-11460
  • Open access: Creative Commons BY license
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    Dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates

    L. Moretto, S. Vance, B. Heames and R. W. Broadhurst, Chem. Commun., 2017, 53, 11457
    DOI: 10.1039/C7CC04625A

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