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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 4451-4462 |
| Number of pages | 12 |
| Journal | Tetrahedron Asymmetry |
| Volume | 11 |
| Issue number | 22 |
| DOIs | |
| State | Published - Nov 17 2000 |
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ASJC Scopus subject areas
- Inorganic Chemistry
- Organic Chemistry
- Materials Chemistry
- Drug Discovery
Cite this
Regio- and enantioselective hydrolysis of phenyloxiranes catalyzed by soluble epoxide hydrolase. / Williamson, Kristin C.; Morisseau, Christophe; Maxwell, Joseph E.; Hammock, Bruce D.
In: Tetrahedron Asymmetry, Vol. 11, No. 22, 17.11.2000, p. 4451-4462.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Regio- and enantioselective hydrolysis of phenyloxiranes catalyzed by soluble epoxide hydrolase
AU - Williamson, Kristin C.
AU - Morisseau, Christophe
AU - Maxwell, Joseph E.
AU - Hammock, Bruce D.
PY - 2000/11/17
Y1 - 2000/11/17
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0034680480&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0034680480&partnerID=8YFLogxK
U2 - 10.1016/S0957-4166(00)00437-7
DO - 10.1016/S0957-4166(00)00437-7
M3 - Article
AN - SCOPUS:0034680480
VL - 11
SP - 4451
EP - 4462
JO - Tetrahedron Asymmetry
JF - Tetrahedron Asymmetry
SN - 0957-4166
IS - 22
ER -