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Issue 7, 2011
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Insights into the stereospecificity of ketoreduction in a modular polyketide synthase

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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

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Publication details

The article was received on 05 Jan 2011, accepted on 01 Feb 2011 and first published on 02 Feb 2011


Article type: Communication
DOI: 10.1039/C1OB00022E
Org. Biomol. Chem., 2011,9, 2053-2056

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    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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