Issue 7, 2011

Insights into the stereospecificity of ketoreduction in a modular polyketide synthase

Abstract

Ketoreductase enzymes are responsible for the generation of hydroxyl stereocentres during the biosynthesis of complex polyketide natural products. Previous studies of isolated polyketide ketoreductases have shown that the stereospecificity of ketoreduction can be switched by mutagenesis of selected active site amino acids. We show here that in the context of the intact polyketide synthase multienzyme the same changes do not alter the stereochemical outcome in the same way. These findings point towards additional factors that govern ketoreductase stereospecificity on intact multienzymes in vivo.

Graphical abstract: Insights into the stereospecificity of ketoreduction in a modular polyketide synthase

Supplementary files

Article information

Article type
Communication
Submitted
05 Jan 2011
Accepted
01 Feb 2011
First published
02 Feb 2011

Org. Biomol. Chem., 2011,9, 2053-2056

Insights into the stereospecificity of ketoreduction in a modular polyketide synthase

D. H. Kwan, M. Tosin, N. Schläger, F. Schulz and P. F. Leadlay, Org. Biomol. Chem., 2011, 9, 2053 DOI: 10.1039/C1OB00022E

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