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Literature summary extracted from

  • Alcantara, J.; Bird, D.A.; Franceschi, V.R.; Facchini, P.J.
    Sanguinarine biosynthesis is associated with the endoplasmic reticulum in cultured opium poppy cells after elicitor treatment (2005), Plant Physiol., 138, 173-183.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.14.102 additional information CYP80B1 is rapidly induced to high levels in response to fungal elicitor treatment Papaver somniferum
1.21.3.3 additional information expression of protein is enhanced by treatment with Botrytis cinerea homogenate Papaver somniferum

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.247 expressed in Escherichia coli Papaver somniferum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.247 cytosol
-
 Papaver somniferum 5829
-
1.14.14.102 endoplasmic reticulum membrane membrane-bound, CYP80B1 from opium poppy contains a noncleavable N-terminal ER-signal peptide Papaver somniferum 5789
-
1.21.3.3 membrane
-
 Papaver somniferum 16020
-
1.21.3.3 vesicle associated to endoplasmic reticulum Papaver somniferum 31982
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.14.102 Fe2+ P450-dependent hydroxylase Papaver somniferum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.14.102 (S)-N-methylcoclaurine + [reduced NADPH-hemoprotein reductase] + O2 Papaver somniferum one of the key enzymes in biosynthesis of benzylisoquinoline alkaloids in the opium poppy, CYP80B1 catalyzes the second to last step in the formation of (S)-reticuline, the last common intermediate in sanguinarine and morphine biosynthesis, overview (S)-3'-hydroxy-N-methylcoclaurine + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?
1.21.3.3 (S)-reticuline + O2 Papaver somniferum first step of isoquinoline and benzophenanthridine alkaloid biosynthesis, involved in sanguinarine pathway (S)-scoulerine + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.247 Papaver somniferum Q9SQ70 opium poppy
-
1.14.14.102 Papaver somniferum
-
-
-
1.21.3.3 Papaver somniferum P93479
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.247 Ni21-charged HiTrap column chromatography Papaver somniferum

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.14.102 cell culture
-
 Papaver somniferum
-
1.21.3.3 idioblast
-
 Papaver somniferum
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.247 Morphinone + NADPH
-
 Papaver somniferum Morphine + NADP+
-
 ?
1.14.14.102 (S)-N-methylcoclaurine + [reduced NADPH-hemoprotein reductase] + O2 one of the key enzymes in biosynthesis of benzylisoquinoline alkaloids in the opium poppy, CYP80B1 catalyzes the second to last step in the formation of (S)-reticuline, the last common intermediate in sanguinarine and morphine biosynthesis, overview Papaver somniferum (S)-3'-hydroxy-N-methylcoclaurine + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?
1.14.14.102 (S)-N-methylcoclaurine + [reduced NADPH-hemoprotein reductase] + O2 specific for the substrate Papaver somniferum (S)-3'-hydroxy-N-methylcoclaurine + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?
1.21.3.3 (S)-reticuline + O2
-
 Papaver somniferum (S)-scoulerine + H2O2
-
 ?
1.21.3.3 (S)-reticuline + O2 first step of isoquinoline and benzophenanthridine alkaloid biosynthesis, involved in sanguinarine pathway Papaver somniferum (S)-scoulerine + H2O2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.247 codeinone reductase
-
 Papaver somniferum
1.1.1.247 COR
-
 Papaver somniferum
1.14.14.102 (S)-N-methylcoclaurine 3'-hydroxylase
-
 Papaver somniferum
1.14.14.102 CYP80B1
-
 Papaver somniferum

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.247 NADPH
-
 Papaver somniferum
1.14.14.102 cytochrome P450 P450-dependent hydroxylase Papaver somniferum