Regio- and enantioselective hydrolysis of phenyloxiranes catalyzed by soluble epoxide hydrolase

The regio- and enantioselective hydrolysis of several phenyloxiranes cataly zed by soluble epoxide hydrolase (sEH) was investigated using recombinant h uman, mouse or cress sEH. Results indicate that human and mouse sEH enantio selectively hydrolyze (S,S)-alkyl-phenyloxiranes faster than the (R,R)-alky l-phenyloxiranes investigated in this study, while cress sEH displayed oppo site enantioselectivity. Preparation of pure (2R,3R)-3-phenylglycidol from the racemic mixture was achieved with a 31% yield using human sEH as cataly st. The sEH enzymes were found to be regioselective at the benzylic carbon of the phenyloxiranes, supporting the proposed mechanism in which one or mo re tyrosine residues in the active site of the enzyme act as a general acid catalyst in the alkylation half reaction. (C) 2000 Published by Elsevier S cience Ltd.