EC Number | Cloned (Comment) | Organism |
---|---|---|
1.5.1.27 | 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 |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.14.19.54 | 0.013 | - |
(S)-reticuline | Cyp82Y2 module, pH not specified in the publication, temperature not specified in the publication | Papaver somniferum |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.14.19.54 | microsome | - |
Papaver somniferum | - |
- |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.5.1.27 | 1,2-dehydroreticulinium + NADPH + H+ | Papaver somniferum | - |
(R)-reticuline + NADP+ | - |
ir |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.5.1.27 | Papaver somniferum | P0DKI7 | - |
- |
1.14.19.54 | Papaver somniferum | P0DKI7 | bifunctional protein, the P450 module 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 | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.5.1.27 | 1,2-dehydroreticulinium + NADPH + H+ | - |
Papaver somniferum | (R)-reticuline + NADP+ | - |
ir | |
1.14.19.54 | (S)-reticuline + [reduced NADPH-hemoprotein reductase] + O2 | - |
Papaver somniferum | 1,2-dehydroreticuline + [oxidized NADPH-hemoprotein reductase] + 2 H2O | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.5.1.27 | STORR | - |
Papaver somniferum |
1.14.19.54 | STORR | - |
Papaver somniferum |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.5.1.27 | NADPH | - |
Papaver somniferum | |
1.14.19.54 | cytochrome P450 | - |
Papaver somniferum |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.5.1.27 | evolution | the enzyme belongs to the aldo-keto reductase family | Papaver somniferum |
1.5.1.27 | 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 |