Regio- and enantioselective hydrolysis of phenyloxiranes catalyzed by soluble epoxide hydrolase |
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| Institution: | 1. Department of Chemistry, Renmin University of China, Beijing 100872, PR China;2. College of Chemistry, Beijing Normal University, Beijing 100875, PR China;1. Department of Analytical Chemistry, Faculty of Science and Technology, University of the Basque Country (UPV/EHU), P.O. Box 644, 48080 Bilbao, Spain;2. Department of Applied Environmental Science (ITM), Stockholm University, SE-10691 Stockholm, Sweden;1. Key Laboratory of Inorganic-Organic Hybrid Functional Material Chemistry, Ministry of Education, Tianjin Normal University, Tianjin 300387, China;2. Tianjin Key Laboratory of Structure and Performance for Functional Molecule, College of Chemistry, Tianjin Normal University, Tianjin 300387, China;3. Department of Chemistry and Biology, Rensselaer Polytechnic Institute (RPI), Troy, NY 12180, US |
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| Abstract: | The regio- and enantioselective hydrolysis of several phenyloxiranes catalyzed by soluble epoxide hydrolase (sEH) was investigated using recombinant human, mouse or cress sEH. Results indicate that human and mouse sEH enantioselectively hydrolyze (S,S)-alkyl-phenyloxiranes faster than the (R,R)-alkyl-phenyloxiranes investigated in this study, while cress sEH displayed opposite enantioselectivity. Preparation of pure (2R,3R)-3-phenylglycidol from the racemic mixture was achieved with a 31% yield using human sEH as catalyst. The sEH enzymes were found to be regioselective at the benzylic carbon of the phenyloxiranes, supporting the proposed mechanism in which one or more tyrosine residues in the active site of the enzyme act as a general acid catalyst in the alkylation half reaction. |
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