6IX2

Structure of the A214C/A250I mutant of an epoxide hydrolase from Aspergillus usamii E001 (AuEH2) at 1.48 Angstroms resolution

Summary for 6IX2

• Entry DOI: 10.2210/pdb6ix2/pdb
• Descriptor: Microsomal epoxide hyddrolase, GLYCEROL (3 entities in total)
• Functional Keywords: alpha and beta proteins, alpha/beta-hydrolases, styrene oxide, hydrolase
• Biological source: Aspergillus usamii
• Total number of polymer chains: 2
• Total formula weight: 97233.70

Authors

Hu, D.,Hu, B.C.,Hou, X.D.,Rao, Y.J.,Wu, M.C. (deposition date: 2018-12-09, release date: 2019-12-11, Last modification date: 2023-11-29)

Primary citation

Hu, D.,Hu, B.C.,Hou, X.D.,Zhang, D.,Lei, Y.Q.,Rao, Y.J.,Wu, M.C.
Structure-Guided Regulation in the Enantioselectivity of an Epoxide Hydrolase to Produce Enantiomeric Monosubstituted Epoxides and Vicinal Diols via Kinetic Resolution.
Org.Lett., 24:1757-1761, 2022

PubMed Abstract: Structure-guided microtuning of an epoxide hydrolase was executed. One mutant, A214C/A250I, displayed a 12.6-fold enhanced enantiomeric ratio ( = 202) toward -styrene oxide, achieving its nearly perfect kinetic resolution at 0.8 M in pure water or 1.6 M in -hexanol/water. Several other beneficial mutants also displayed significantly improved values, offering promising biocatalysts to access 19 structurally diverse chiral monosubstituted epoxides (97.1 - ≥ 99% ee) and vicinal diols (56.2-98.0% ee) with high yields.

PubMed: 35229602
DOI: 10.1021/acs.orglett.1c04348

Experimental method

X-RAY DIFFRACTION (1.478 Å)