Weijers Carel A G M, Könst Paul M, Franssen Maurice C R, Sudhölter Ernst J R
Laboratory of Organic Chemistry, Wageningen University, Dreijenplein 8, 6703HB, Wageningen, The Netherlands.
Org Biomol Chem. 2007 Oct 7;5(19):3106-14. doi: 10.1039/b709742e. Epub 2007 Aug 21.
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.
