Molecular cloning and characterization of a broad substrate terpenoid oxidoreductase from Artemisia annua.

A.M. Ryden, C.P. Ruyter-Spira, R. Litjens, S. Takahashi, W.J. Quax, H. Osada, H.J. Bouwmeester, O. Kayser

Research output: Contribution to journalArticleAcademicpeer-review

11 Citations (Scopus)

Abstract

From Artemisia annua L., a new oxidoreductase (Red 1) was cloned, sequenced and functionally characterized. Through bioinformatics, heterologous protein expression, and enzyme substrate conversion assays, the elucidation of the enzymatic capacities of Red1 was achieved. Red1 acts on monoterpenoids, and in particular functions as a menthone:neomenthol oxidoreductase. The kinetic parameter kcat/Km was determined to be 939 fold more efficient for the reduction of (-)-menthone to (+)-neomenthol, than results previously reported for the menthone:neomenthol reductase from Mentha x piperita. Based on its kinetic properties, the possible use of Red1 in biological crop protection is discussed.
Original languageEnglish
Pages (from-to)1219-1228
JournalPlant and Cell Physiology
Volume51
Issue number7
DOIs
Publication statusPublished - 2010

Keywords

  • chain dehydrogenases/reductases sdrs
  • amorpha-4,11-diene synthase
  • functional assignments
  • biosynthetic-pathway
  • essential oil
  • key enzyme
  • expression
  • reductase
  • peppermint
  • acid

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