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By SEAN JENNETT

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29). However, several studies have successfully demonstrated that by simply mimicking the terminal region of the phosphopantetheine chain using N-acetylcysteamine, enzymatic activity of PKS domains can be monitored [65, 95]. A simple coupling reaction between N-acetylcysteamine and the free acid of the desired acyl group can be used to generate substrate N-acetylcysteamine (SNAC) thioesters mimics of PKS intermediates. The use of SNAC thioesters has many advantages. Firstly, the commercially available N-acetylcysteamine is far cheaper than CoA, making the synthesis of a range of substrate probes financially viable.

Chem. Soc. T. M. Stroud, The structure of a ketoreductase determines the organization of the beta-carbon processing enzymes of modular polyketide synthases. T. Keatinge-Clay, A tylosin ketoreductase reveals how chirality is determined in polyketides. Chem. Biol. J. A. K. T.

Rev. G. S. Gokhale, D. Mohanty, Towards prediction of metabolic products of polyketide synthases: an In Silico analysis. PLoS Comput. Biol. Q. L. Tang, B. Shen, Type I polyketide synthase requiring a discrete acyltransferase for polyketide biosynthesis. Proc. Natl. Acad. Sci. J. Piel, A polyketide synthase-peptide synthetase gene cluster from an uncultured bacterial symbiont of Paederus beetles. Proc. Natl. Acad. Sci. T. Gulder, M. Freeman, J. Piel, The catalytic diversity of multimodular polyketide synthases: natural product biosynthesis beyong textbook assembly rules.

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Cornwall and the Isles of Scilly by SEAN JENNETT


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