Ketoreductase domain mutagenesis reprogrammes chain-length control in alternapyrone biosynthesis

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.