The Molecular Cloning of Dihydroartemisinic Aldehyde Reductase and its Implication in Artemisinin Biosynthesis in Artemisia annua

Anna-Margareta Ryden, Carolien Ruyter-Spira, Wim J. Quax, Hiroyuki Osada, Toshiya Muranaka, Oliver Kayser*, Harro Bouwmeester

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

41 Citations (Scopus)

Abstract

A key point in the biosynthesis of the antimalarial drug artemisinin is the formation of dihydroartemisinic aldehyde which represents the key difference between chemotype specific pathways. This key intermediate is the substrate for several competing enzymes, some of which increase the metabolic flux towards artemisinin, and some of which - as we show in the present study - may have a negative impact on artemisinin production. In an effort to understand the biosynthetic network of artemisinin biosynthesis, extracts of A. annua flowers were investigated and found to contain an enzyme activity competing in a negative sense with artemisinin biosynthesis. The enzyme Red1 is a broad substrate oxidoreductase belonging to the short chain dehydrogenase/reductase family with high affinity for dihydroartemisinic aldehyde and valuable monoterpenoids. Spatial and temporal analysis of cDNA revealed Red1 to be trichome specific. The relevance of Red1 to artemisinin biosynthesis is discussed.

Original languageEnglish
Pages (from-to)1778-1783
Number of pages6
JournalPlanta Medica
Volume76
Issue number15
DOIs
Publication statusPublished - Oct-2010

Keywords

  • Artemisia annua L.
  • Asteraceae
  • red1
  • dihydroartemisinic aldehyde
  • reductase
  • dehydrogenase
  • trichome
  • CHAIN DEHYDROGENASES/REDUCTASES SDRS
  • AMORPHA-4,11-DIENE SYNTHASE
  • KEY ENZYME
  • FUNCTIONAL ASSIGNMENTS
  • EXPRESSION
  • ACID
  • IDENTIFICATION
  • PLANTS
  • DEHYDROGENASE/REDUCTASE
  • TERPENOIDS

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