8XXB
Crystal Structure of a triple-mutant (A69F/M124P/R127G) of halohydrin dehalogenase HheD8 complexed with chloride
Summary for 8XXB
| Entry DOI | 10.2210/pdb8xxb/pdb |
| Descriptor | Short-chain dehydrogenase/reductase SDR, CHLORIDE ION (3 entities in total) |
| Functional Keywords | halohydrin dehalogenase, hydrolase |
| Biological source | Thauera aminoaromatica S2 |
| Total number of polymer chains | 1 |
| Total formula weight | 24758.84 |
| Authors | Wan, N.W. (deposition date: 2024-01-18, release date: 2024-01-31, Last modification date: 2025-02-26) |
| Primary citation | Hua, X.,Wang, Y.F.,Jin, X.,Yu, H.Y.,Wang, H.H.,Chen, Y.Z.,Wan, N.W. Biocatalytic enantioselective formation and ring-opening of oxetanes. Nat Commun, 16:1170-1170, 2025 Cited by PubMed Abstract: Although 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 γ-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. PubMed: 39885154DOI: 10.1038/s41467-025-56463-z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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