1.14.11.32: codeine 3-O-demethylase
This is an abbreviated version!
For detailed information about codeine 3-O-demethylase, go to the full flat file.
Word Map on EC 1.14.11.32
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1.14.11.32
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thebaine
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morphine
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poppy
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opium
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papaver
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somniferum
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benzylisoquinoline
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o-demethylation
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codeinone
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morphinans
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virus-induced
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analgesics
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dioxygenases
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acinetobacter
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narcotic
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opiate
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salutaridinol
- 1.14.11.32
- thebaine
- morphine
- poppy
-
opium
-
papaver
- somniferum
-
benzylisoquinoline
-
o-demethylation
- codeinone
-
morphinans
-
virus-induced
-
analgesics
- dioxygenases
- acinetobacter
-
narcotic
-
opiate
- salutaridinol
Reaction
Synonyms
codeine O-demethylase, codeine-O-demethylase, CODM
ECTree
1.14.11.32 codeine 3-O-demethylaseAdvanced search results
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General Information on EC 1.14.11.32 - codeine 3-O-demethylase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
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the enzyme belongs to the 2-oxoglutarate/Fe(II)-dependent dioxygenase superfamily
malfunction
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virus-induced gene silencing of CODM in opium poppy efficiently blocks metabolism at codeine
metabolism
physiological function
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codeine O-demethylase catalyzes the last step of morphine biosynthesis in opium poppy, but it also catalyze the O,O-demethylenation of methylenedioxy bridges on protopine alkaloids. No or poor activity with papaverine, (R,S)-tetrahydropapaverine, (R,S)-canadine, (R,S)-stylopine, berberine, and oripavine
metabolism
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codeine O-demethylase catalyzes the last step of morphine biosynthesis in opium poppy
metabolism
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the enzyme is involved in the morphinan pathway via codeine of the biosynthesis of benzylisoquinoline alkaloids in Papaver somniferum, overview
metabolism
thebaine binds at the two distinct sites of thebaine 6-O-demethylase T6ODM, Ec 1.14.11.31, and codeine-3-O-demethylase CODM, which determines the precise regioselectivity at C6 and C3 positions of thebaine respectively. Thebaine binds in site II (characteristic due to the presence of Asp313) of T6ODM for C6 selectivity. It binds in site I (characteristic due to the presence of Asp143) of CODM for C3 selectivity. Thebaine forms stable ionic interaction with these aspartate residues via its positively charged tertiary amino group and is further stabilized by the hydrophobic interactions via its B ring. The binding of oxygen to the nonheme iron is followed by the Fe(IV)=O bond flip, yielding an octahedral intermediate. During the decarboxylation reaction process, the C-terminal lid in the enzyme changes from the closed conformation in the 5C coordinate Fe(IV)=O complex to an active open conformation in the 6C coordinate complex
