Dioxygenases catalyze the O-demethylation steps of morphine biosynthesis in opium poppy.
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.
Department of Biological Sciences, University of Calgary, Calgary, Alberta, Canada.
Jillian M
JM
Hagel
Peter J
PJ
Facchini
D055162:Biocatalysis; D049308:Dioxygenases / Q000378:metabolism*; D008745:Methylation; D009020:Morphine / Q000096:biosynthesis* / Q000737:chemistry; D010207:Papaver / Q000737:chemistry / Q000201:enzymology / Q000378:metabolism*
D009020:Morphine; D049308:Dioxygenases