Structural highlights
FunctionPublication Abstract from PubMedAlthough biocatalysis offers complementary or alternative approaches to traditional synthetic methods, the limited range of available enzymatic reactions currently poses challenges in synthesizing a diverse array of desired compounds. Consequently, there is a significant demand for developing novel biocatalytic processes to enable reactions that were previously unattainable. Herein, we report the discovery and subsequent protein engineering of a unique halohydrin dehalogenase to develop a biocatalytic platform for enantioselective formation and ring-opening of oxetanes. This biocatalytic platform, exhibiting high efficiency, excellent enantioselectivity, and broad scopes, facilitates the preparative-scale synthesis of chiral oxetanes and a variety of chiral gamma-substituted alcohols. Additionally, both the enantioselective oxetane formation and ring-opening processes are proven scalable for large-scale transformations at high substrate concentrations, and can be integrated efficiently in a one-pot, one-catalyst cascade system. This work expands the enzymatic toolbox for non-natural reactions and will promote further exploration of the catalytic repertoire of halohydrin dehalogenases in synthetic and pharmaceutical chemistry. Biocatalytic enantioselective formation and ring-opening of oxetanes.,Hua X, Wang YF, Jin X, Yu HY, Wang HH, Chen YZ, Wan NW Nat Commun. 2025 Jan 30;16(1):1170. doi: 10.1038/s41467-025-56463-z. PMID:39885154[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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