2. Academic Validation
  3. Dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates

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

  • Chem Commun (Camb). 2017 Oct 25;53(83):11457-11460. doi: 10.1039/c7cc04625a.
Luisa Moretto 1,  Steven Vance,  Brennan Heames,  R William Broadhurst
Affiliations

Affiliation

  • 1 Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA.
PMID: 28980673 DOI: 10.1039/c7cc04625a
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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