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A carbonate-forming Baeyer-Villiger monooxygenase
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A carbonate-forming Baeyer-Villiger monooxygenase
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A carbonate-forming Baeyer-Villiger monooxygenase
A carbonate-forming Baeyer-Villiger monooxygenase
Journal Article

A carbonate-forming Baeyer-Villiger monooxygenase

2014
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Overview
Carbonates exist in a few natural products, but their biosynthetic origins have been unclear. Genetic and biochemical characterization of a flavin-dependent monooxygenase from the cytochalasin cluster now demonstrates conversion of a ketone into a carbonate prior to other tailoring steps. Despite the remarkable versatility displayed by flavin-dependent monooxygenases (FMOs) in natural product biosynthesis, one notably missing activity is the oxidative generation of carbonate functional groups. We describe a multifunctional Baeyer-Villiger monooxygenase, CcsB, which catalyzes the formation of an in-line carbonate in the macrocyclic portion of cytochalasin E. This study expands the repertoire of activities of FMOs and provides a possible synthetic strategy for transformation of ketones into carbonates.