Ecdysone 20-monooxygenase, a cytochrome P450 enzyme from spinach, Spinacia oleracea

Robert J. Grebenok, David W. Galbraith, Irene Benveniste, Rene Feyereisen

Research output: Contribution to journalArticlepeer-review

21 Scopus citations


A microsomal preparation isolated from first leaves of 25-day-old spinach catalysed the hydroxylation of ecdysone to produce the insect moulting hormone, 20-hydroxyecdysone. Hydroxylation was dependent on NADPH and molecular oxygen, and was inhibited by carbon monoxide. Carbon monoxide inhibition was partially reversible by white light. Polyclonal antibodies to the Jerusalem artichoke NADPH-cytochrome P450 reductase inhibited the hydroxylation reaction as well as the spinach microsomal NADPH cytochrome c reductase. These results taken together establish ecdysone hydroxylation as a cytochrome P450 dependent reaction in spinach, which is known to synthesize large amounts of phytoecdysteroids.

Original languageEnglish (US)
Pages (from-to)927-933
Number of pages7
Issue number4
StatePublished - Jul 1996


  • 20-hydroxyecdysone
  • Chenopodiaceae
  • Spinacia oleracea
  • cytochrome P450
  • ecdysone
  • enzymology
  • monooxygenase
  • oleracea
  • phytoecdysteroids

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Plant Science
  • Horticulture


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