| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 70075 | Journal of Molecular Catalysis B: Enzymatic | 2011 | 8 Pages |
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.
Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Extensive substrate profile of cyclopentadecanone monooxygenase. ► Comparison of enzyme performance to other BVMOs in light of phylogenetic relations. ► Novel features were discovered in context with regiodivergent biooxygenations. ► Performance of CPDMO is highly novel and complements the available set of BVMOs.
