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• W2023941006 abstract "The iterative, highly-reducing polyketide synthases use a single copy of each domain to transform multiple substrates, defying conventional rules regarding enzyme function. Synthetic tool compounds and hybrid constructs now provide insights into the specificity of the ketoreductase in dehydrozearalenol biosynthesis. Iterative highly reducing polyketide synthases from filamentous fungi are the most complex and enigmatic type of polyketide synthase discovered to date. Here we uncover an unusual degree of programming by the hypothemycin highly reducing polyketide synthase, in which a single ketoreductase domain shows stereospecificity that is controlled by substrate length. Mapping of the structural domains responsible for this feature allowed for the biosynthesis of an unnatural diastereomer of the natural product dehydrozearalenol." @default.
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• W2023941006 date "2012-03-11" @default.
• W2023941006 modified "2023-10-17" @default.
• W2023941006 title "A fungal ketoreductase domain that displays substrate-dependent stereospecificity" @default.
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• W2023941006 doi "https://doi.org/10.1038/nchembio.912" @default.
• W2023941006 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3307869" @default.
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