title: Stereochemical preference of yeast epoxide hydrolase for the O-axial C3 epimers of 1-oxaspiro[2.5]octanes.
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.
authors: Laboratory of Organic Chemistry, Wageningen University, Dreijenplein 8, 6703HB, Wageningen, The Netherlands.
authors: Carel A G M
authors: CA
authors: Weijers
authors: Paul M
authors: PM
authors: Könst
authors: Maurice C R
authors: MC
authors: Franssen
authors: Ernst J R
authors: EJ
authors: Sudhölter
mesh_terms: D001665:Binding Sites; D002384:Catalysis; D004851:Epoxide Hydrolases / Q000378:metabolism*; D004852:Epoxy Compounds / Q000737:chemistry / Q000378:metabolism*; D009795:Octanes / Q000737:chemistry / Q000378:metabolism*; D012248:Rhodotorula / Q000201:enzymology*; D013237:Stereoisomerism; D013379:Substrate Specificity
chemical_list: D004852:Epoxy Compounds; D009795:Octanes; D004851:Epoxide Hydrolases