Background: Bacterial steroid monooxygenase degrades progesterone. Results: The crystallographic and mutagenesis analysis outline a robust active-site scaffold, capable of performing BaeyerVilliger oxidations on chemically diverse molecules. Conclusion: This and related enzymes represent a fascinating case for the comparative evaluation of user tailored protein engineering with enzyme variants arising through evolution. Significance: These findings highlight the biocatalytic potential of Baeyer-Villiger monooxygenases.

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