elucidation of the crucial but complex oxidative tailoring steps in rufomycin biosynthesis enables one pot conversion of rufomycin B to rufomycin C

The antimycobacterial peptides, rufomycins, have their antibiotic activity conferred by oxidative tailoring of the cyclic peptide. Here we elucidate the roles of cytochrome P450s RufS and RufM in regioselective epoxidation and alkyl oxidation respectively and demonstrate how RufM and RufS create a c...

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Published in:Chemical communications (Cambridge, England) England), 2021-11, Vol.57 (89), p.11795-11798
Main Authors: Perez Ortiz, Gustavo, Sidda, John D, de los Santos, Emmanuel L. C, Hubert, Catherine B, Barry, Sarah M
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Summary:The antimycobacterial peptides, rufomycins, have their antibiotic activity conferred by oxidative tailoring of the cyclic peptide. Here we elucidate the roles of cytochrome P450s RufS and RufM in regioselective epoxidation and alkyl oxidation respectively and demonstrate how RufM and RufS create a complex product profile dependent on redox partner availability. Finally, we report the in vitro one pot conversion of rufomycin B to rufomycin C. Cytochrome P450s RufS and RufM catalyse regioselective and stereoselective epoxidation and alkyl oxidation respectively, in a complex series of reactions in the biosynthesis of the antimycobacterial peptides, rufomycins.
ISSN:1359-7345
1364-548X
DOI:10.1039/d1cc04794a