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Insights into the stereospecificity of ketoreduction in a modular polyketide synthase

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Kwan, David H., Tosin, Manuela, Schläger, Nadin, Schulz, F. (Frank) and Leadlay, P. F. (2011) Insights into the stereospecificity of ketoreduction in a modular polyketide synthase. Organic & Biomolecular Chemistry, Vol.9 (No.7). pp. 2053-2056. doi:10.1039/c1ob00022e

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Official URL: http://dx.doi.org/10.1039/C1OB00022E

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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.

Item Type: Journal Article
Subjects: Q Science > QD Chemistry
Divisions: Faculty of Science > Chemistry
Library of Congress Subject Headings (LCSH): Stereochemistry, Polyketides, Enzymes, Biosynthesis
Journal or Publication Title: Organic & Biomolecular Chemistry
Publisher: Royal Society of Chemistry
ISSN: 1477-0520
Official Date: 2011
Dates:
DateEvent
2011Published
Volume: Vol.9
Number: No.7
Page Range: pp. 2053-2056
DOI: 10.1039/c1ob00022e
Status: Peer Reviewed
Publication Status: Published
Funder: Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), University of Cambridge Herchel Smith Fund, University of Cambridge. Cambridge Commonwealth Trusts, Overseas Research Students Award Scheme (ORSAS), Natural Sciences and Engineering Research Council Canada (NSERC), Sixth Framework Programme (European Commission) (FP6)
Grant number: 8/B18119 (BBSRC)

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