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Literature summary for 1.5.1.27 extracted from

  • Winzer, T.; Kern, M.; King, A.J.; Larson, T.R.; Teodor, R.I.; Donninger, S.L.; Li, Y.; Dowle, A.A.; Cartwright, J.; Bates, R.; Ashford, D.; Thomas, J.; Walker, C.; Bowser, T.A.; Graham, I.A.
    Plant science. Morphinan biosynthesis in opium poppy requires a P450-oxidoreductase fusion protein (2015), Science, 349, 309-312 .
    View publication on PubMed
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Cloned(Commentary)

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Papaver somniferum P0DKI7
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,2-dehydroreticulinium + NADPH + H+
-
 Papaver somniferum (R)-reticuline + NADP+
-
 ir

Synonyms

Synonyms Comment Organism
STORR
-
 Papaver somniferum

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Papaver somniferum

General Information

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