Structural highlights
Function
T2B4K5_ASPUS
Publication Abstract from PubMed
Structure-guided microtuning of an Aspergillus usamii epoxide hydrolase was executed. One mutant, A214C/A250I, displayed a 12.6-fold enhanced enantiomeric ratio (E = 202) toward rac-styrene oxide, achieving its nearly perfect kinetic resolution at 0.8 M in pure water or 1.6 M in n-hexanol/water. Several other beneficial mutants also displayed significantly improved E values, offering promising biocatalysts to access 19 structurally diverse chiral monosubstituted epoxides (97.1 - >/= 99% ees) and vicinal diols (56.2-98.0% eep) with high yields.
Structure-Guided Regulation in the Enantioselectivity of an Epoxide Hydrolase to Produce Enantiomeric Monosubstituted Epoxides and Vicinal Diols via Kinetic Resolution.,Hu D, Hu BC, Hou XD, Zhang D, Lei YQ, Rao YJ, Wu MC Org Lett. 2022 Mar 11;24(9):1757-1761. doi: 10.1021/acs.orglett.1c04348. Epub, 2022 Mar 1. PMID:35229602[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hu D, Hu BC, Hou XD, Zhang D, Lei YQ, Rao YJ, Wu MC. Structure-Guided Regulation in the Enantioselectivity of an Epoxide Hydrolase to Produce Enantiomeric Monosubstituted Epoxides and Vicinal Diols via Kinetic Resolution. Org Lett. 2022 Mar 11;24(9):1757-1761. doi: 10.1021/acs.orglett.1c04348. Epub, 2022 Mar 1. PMID:35229602 doi:http://dx.doi.org/10.1021/acs.orglett.1c04348