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Ketoreductase domain mutagenesis reprogrammes chain-length control in alternapyrone biosynthesis
Inthira Tapeng1, Jaiyfungkhong Phakeovilay2, Pakorn Wattana-Amorn1,2
1Department of Chemistry and Center of Excellence for Innovation in Chemistry, Faculty of Science, Kasetsart University, Bangkok, 10900, Thailand. fscipwa@ku.ac.th.
Abstract:
Mutation of the ketoreductase domain in alternapyrone polyketide synthase abolished production of the decaketide-derived alternapyrone and redirected biosynthesis to non-reduced triketide-derived α-pyrones with promiscuous utilisation of starter units ranging from C2 to C8. These findings reveal a role of the KR domain in controlling polyketide chain-length programming during alternapyrone biosynthesis.
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