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Literature summary for 1.14.19.67 extracted from

  • Gerardy R.; Zenk, M.H.
    Formation of salutaridine from (R)-reticuline by a membrane-bound cytochrome P-450 enzyme from Papaver somniferum (1993), Phytochemistry, 32, 79-86.
No PubMed abstract available
Search for more literature for 1.14.19.67

Inhibitors

Inhibitors Comment Organism Structure
Ancymidole
-
 Papaver somniferum
CO in darkness but not in light Papaver somniferum
Prochloraz
-
 Papaver somniferum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.017
-
 (R)-reticuline
-
 Papaver somniferum
0.15
-
 [reduced NADPH-hemoprotein reductase]
-
 Papaver somniferum

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome membrane-bound Papaver somniferum
-
-
mitochondrion
-
 Papaver somniferum 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(R)-reticuline + [reduced NADPH-hemoprotein reductase] + O2 Papaver somniferum formation of salutaridine, a key intermediate in morphine biosynthesis salutaridine + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Papaver somniferum
-
-
-

Reaction

Reaction Comment Organism Reaction ID
(R)-reticuline + [reduced NADPH-hemoprotein reductase] + O2 = salutaridine + [oxidized NADPH-hemoprotein reductase] + 2 H2O regioselective and stereoselective para-ortho oxidative coupling Papaver somniferum
a

Source Tissue

Source Tissue Comment Organism Textmining
cell suspension culture thebaine-producing Papaver somniferum
-
additional information no enzyme activity in latex Papaver somniferum
-
plant capsule
-
 Papaver somniferum
-
root
-
 Papaver somniferum
-
shoot
-
 Papaver somniferum
-

Storage Stability

Storage Stability Organism
-20°C, microsome-bound enzyme, freezing causes a total loss of activity Papaver somniferum
-70°C, microsome-bound enzyme, 20% loss of activity after 1 month Papaver somniferum
22°C, microsome-bound enzyme, half-life: 2 h Papaver somniferum
in ice water, microsome-bound enzyme, half-life: 20 h Papaver somniferum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-reticuline + [reduced NADPH-hemoprotein reductase] + O2 strictly dependent on NADPH as reducing cofactor and on (R)-configurated reticuline Papaver somniferum salutaridine + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?
(R)-reticuline + [reduced NADPH-hemoprotein reductase] + O2 formation of salutaridine, a key intermediate in morphine biosynthesis Papaver somniferum salutaridine + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20 25
-
 Papaver somniferum

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
10 30 10°C: about 30% of maximal activity, 30°C: about 65% of maximal activity Papaver somniferum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Papaver somniferum

pH Range

pH Minimum pH Maximum Comment Organism
6.5 8.5 about 50% of maximal activity at pH 6.5 and pH 8.5 Papaver somniferum

Cofactor

Cofactor Comment Organism Structure
cytochrome P450 enzyme contains cytochrome P450 Papaver somniferum