Extensive substrate profiling of cyclopentadecanone monooxygenase as Baeyer–Villiger biocatalyst reveals novel regiodivergent oxidations

Cyclopentadecanone monooxygenase (CPDMO) is one of the latest additions to the established library of Baeyer–Villiger monooxygenases. Desymmetrizations of substituted cyclobutanones and -hexanones as well as kinetic resolutions of racemic cycloketones are efficiently catalyzed by CPDMO. Moreover the enzyme shows unprecedented preference in regiodivergent oxidations of terpenones and the bicyclic Geissman–Waiss lactone precursor giving access to the optical antipode of retronecine and other pyrrolizidine alkaloids.