Dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates. Issue 83 (5th October 2017)

• Record Type: Journal Article
• Authors: Moretto, Luisa; Vance, Steven; Heames, Brennan; Broadhurst, R. William
• Is Part Of: Chemical communications. Volume 53:Issue 83(2017)
• Page Start: 11457
• Page End: 11460
• Publication Date: 2017-10-05
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c7cc04625a
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : Interaction studies show that KR domains possess a generic binding site for ACP domains and provide evidence that the 5′-phosphopantetheine prosthetic group plays a key role in delivering acyl substrates to the active site in the correct orientation. 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.