A chicory cytochrome P450 mono-oxygenase CYP71AV8 for the oxidation of (+)-valencene

K. Cankar, A.M.M.L. van Houwelingen, H.J. Bosch, Th. Sonke, H.J. Bouwmeester, M.J. Beekwilder

Research output: Contribution to journalArticleAcademicpeer-review

95 Citations (Scopus)

Abstract

Chicory (Cichorium intybus L.), which is known to have a variety of terpene-hydroxylating activities, was screened for a P450 mono-oxygenase to convert (+)-valencene to (+)-nootkatone. A novel P450 cDNA was identified in a chicory root EST library. Co-expression of the enzyme with a valencene synthase in yeast, led to formation of trans-nootkatol, cis-nootkatol and (+)-nootkatone. The novel enzyme was also found to catalyse a three step conversion of germacrene A to germacra-1(10),4,11(13)-trien-12-oic acid, indicating its involvement in chicory sesquiterpene lactone biosynthesis. Likewise, amorpha-4,11-diene was converted to artemisinic acid. Surprisingly, the chicory P450 has a different regio-specificity on (+)-valencene compared to germacrene A and amorpha-4,11-diene
Original languageEnglish
Pages (from-to)178-182
JournalFEBS Letters
Volume585
Issue number1
DOIs
Publication statusPublished - 2011

Keywords

  • functional-characterization
  • yeast expression
  • nootkatone
  • valencene
  • biosynthesis
  • sesquiterpenes
  • artemisinin
  • synthase
  • cloning

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