Dioxygenases catalyze the O-demethylation steps of morphine biosynthesis in opium poppy

Nat Chem Biol. 2010 Apr;6(4):273-5. doi: 10.1038/nchembio.317. Epub 2010 Mar 14.

Abstract

Two previously undetected enzymes involved in morphine biosynthesis and unique among plants to opium poppy have been identified as non-heme dioxygenases, in contrast to the functionally analogous cytochrome P450s found in mammals. We used functional genomics to isolate thebaine 6-O-demethylase (T6ODM) and codeine O-demethylase (CODM), the only known 2-oxoglutarate/Fe(II)-dependent dioxygenases that catalyze O-demethylation. Virus-induced gene silencing of T6ODM and CODM in opium poppy efficiently blocked metabolism at thebaine and codeine, respectively.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biocatalysis
  • Dioxygenases / metabolism*
  • Methylation
  • Morphine / biosynthesis*
  • Morphine / chemistry
  • Papaver / chemistry
  • Papaver / enzymology
  • Papaver / metabolism*

Substances

  • Morphine
  • Dioxygenases

Associated data

  • PubChem-Substance/87544089
  • PubChem-Substance/87544090
  • PubChem-Substance/87544091
  • PubChem-Substance/87544092
  • PubChem-Substance/87544093
  • PubChem-Substance/87544094
  • PubChem-Substance/87544095
  • PubChem-Substance/87544096
  • PubChem-Substance/87544097
  • PubChem-Substance/87544098
  • PubChem-Substance/87544099
  • PubChem-Substance/87544100
  • PubChem-Substance/87544101
  • PubChem-Substance/87544102
  • PubChem-Substance/87544103
  • PubChem-Substance/87544104