Cloned (Comment) | Organism |
---|---|
DNA and amino acid sequence determination and analysis, the genetic locus, designated STORR [(S)- to (R)-reticuline] encodes both cytochrome P450 and oxidoreductase modules | Papaver somniferum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
1,2-dehydroreticulinium + NADPH + H+ | Papaver somniferum | - |
(R)-reticuline + NADP+ | - |
ir |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Papaver somniferum | P0DKI7 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1,2-dehydroreticulinium + NADPH + H+ | - |
Papaver somniferum | (R)-reticuline + NADP+ | - |
ir |
Synonyms | Comment | Organism |
---|---|---|
STORR | - |
Papaver somniferum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADPH | - |
Papaver somniferum |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the aldo-keto reductase family | Papaver somniferum |
physiological function | direction of metabolites to morphinan biosynthesis requires isomerization of (S)- to (R)-reticuline. The P450 module of the bifunctional enzyme is responsible for the conversion of (S)-reticuline to 1,2-dehydroreticuline, whereas the oxidoreductase module converts 1,2-dehydroreticuline to (R)-reticuline rather than functioning as a P450 redox partner. Proteomic analysis confirms that these two modules are contained on a single polypeptide in vivo | Papaver somniferum |