Issue 83, 2017

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

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

Supplementary files

Article information

Article type
Communication
Submitted
15 Jun 2017
Accepted
29 Jun 2017
First published
05 Oct 2017
This article is Open Access
Creative Commons BY license

Chem. Commun., 2017,53, 11457-11460

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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