Issue 6, 2011
From the journal:

Chemical Communications

Active site modification of the β-ketoacyl-ACP synthase FabF3 of Streptomyces coelicolor affects the fatty acid chain length of the CDA lipopeptides†

Richard A. Lewis,a   Laura Nunns,b   Jenny Thirlway,b   Kathleen Carroll,b   Colin P. Smitha  and  Jason Micklefield*b  

* Corresponding authors

a FHMS, University of Surrey, Guildford, Surrey, UK

b School of Chemistry and Manchester Interdisciplinary Biocentre, The University of Manchester, 131 Princess Street, Manchester, UK
E-mail: j.micklefield@manchester.ac.uk
Tel: +44 (0)161 306 4509

Abstract

Using site directed mutagenesis we altered an active site residue (Phe107) of the enzyme encoded by fabF3 (SCO3248) in the Streptomyces coelicolorgene cluster required for biosynthesis of the calcium dependent antibiotics (CDAs), successfully generating two novel CDA derivatives comprising truncated (C4) lipid side chains and confirming that fabF3 encodes a KAS-II homologue that is involved in determining CDA fatty acid chain length.

Graphical abstract: Active site modification of the β-ketoacyl-ACP synthase FabF3 of Streptomyces coelicolor affects the fatty acid chain length of the CDA lipopeptides

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Article information

DOI
https://doi.org/10.1039/C0CC03444D
Article type
Communication
Submitted
24 Aug 2010
Accepted
17 Nov 2010
First published
06 Dec 2010

Chem. Commun., 2011,47, 1860-1862

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Active site modification of the β-ketoacyl-ACP synthase FabF3 of Streptomyces coelicolor affects the fatty acid chain length of the CDA lipopeptides

R. A. Lewis, L. Nunns, J. Thirlway, K. Carroll, C. P. Smith and J. Micklefield, Chem. Commun., 2011, 47, 1860 DOI: 10.1039/C0CC03444D

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