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  • Title: Stereochemical preference of yeast epoxide hydrolase for the O-axial C3 epimers of 1-oxaspiro[2.5]octanes.
    Author: Weijers CA, Könst PM, Franssen MC, Sudhölter EJ.
    Journal: Org Biomol Chem; 2007 Oct 07; 5(19):3106-14. PubMed ID: 17878969.
    Abstract:
    The 1-oxaspiro[2.5]octane moiety is a common motif in many biologically active spiroepoxide compounds. Stereochemistry plays an important role in the action of these spiroepoxides, since the O-axial C3 epimers are predominantly responsible for biological activity. In view of this, the reactivity of the yeast epoxide hydrolase (YEH) from Rhodotorula glutinis towards both O-axial and O-equatorial C3 epimers of various 1-oxaspiro[2.5]octanes was investigated. O-axial C3 Epimers were hydrolyzed faster than the O-equatorial C3 epimers. The stereochemical preference was greatly dependent on the type of substitution on the cyclohexane ring. The preference of YEH for O-axial C3 epimers, found throughout this study, illustrates the effectiveness of YEH in enzymatic detoxification of spiroepoxides.
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