Stereochemical preference of yeast epoxide hydrolase for the O-axial C3 epimers of 1-oxaspiro[2.5] octanes

C.A.G.M. Weijers, P. Koenst, M.C.R. Franssen, E.J.R. Sudhölter

Research output: Contribution to journalArticleAcademicpeer-review

10 Citations (Scopus)

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
Original languageEnglish
Pages (from-to)3106-3114
JournalOrganic & Biomolecular Chemistry
Volume5
Issue number19
DOIs
Publication statusPublished - 2007

Keywords

  • angiogenesis inhibitors
  • kinetic resolution
  • natural-products
  • methionine aminopeptidase
  • conformational-analysis
  • rhodotorula-glutinis
  • variable-temperature
  • fumagillin analogs
  • stereoselectivity
  • hydrolysis

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