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

• Published in: Journal of molecular catalysis. B, Enzymatic Vol. 73; no. 1; pp. 9 - 16
• Main Authors: Fink, Michael J., Fischer, Thomas C., Rudroff, Florian, Dudek, Hanna, Fraaije, Marco W., Mihovilovic, Marko D.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 01.12.2011; Elsevier
• Subjects: Baeyer–Villiger monooxygenases; biocatalysts; Bioconversions. Hemisynthesis; Biological and medical sciences; Biooxygenation; Biotechnology; catalytic activity; Fundamental and applied biological sciences. Psychology; Geissman–Waiss lactone; Methods. Procedures. Technologies; Regioselective biotransformation; retronecine; Terpenones; Geissman–Waiss lactone; Terpenones; Baeyer–Villiger monooxygenases; Regioselective biotransformation; Biooxygenation; Baeyer Villiger reaction; Substrate; Regioselectivity; Geissman-Waiss lactone; Biotransformation; Lactone; Oxidation; Baeyer-Villiger monooxygenases; Biocatalyst
• ISSN: 1381-1177; 1873-3158
• DOI: 10.1016/j.molcatb.2011.07.003

[Display omitted] ► 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. 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.