BRENDA - Enzyme Database show
show all sequences of 1.14.19.67

Formation of salutaridine from (R)-reticuline by a membrane-bound cytochrome P-450 enzyme from Papaver somniferum

Gerardy R.; Zenk, M.H.; Phytochemistry 32, 79-86 (1993)
No PubMed abstract available

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
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
Commentary
Organism
Structure
0.017
-
(R)-reticuline
-
Papaver somniferum
0.15
-
NADPH
-
Papaver somniferum
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
membrane-bound
Papaver somniferum
-
-
mitochondrion
-
Papaver somniferum
5739
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(R)-reticuline + [reduced NADPH-hemoprotein reductase] + O2
Papaver somniferum
formation of salutaridine, a key intermediate in morphine biosynthesis
salutaridine + [oxidized NADPH-hemoprotein reductase] + H2O
-
Papaver somniferum
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Papaver somniferum
-
-
-
Reaction
Reaction
Commentary
Organism
(R)-reticuline + [reduced NADPH-hemoprotein reductase] + O2 = salutaridine + [oxidized NADPH-hemoprotein reductase] + 2 H2O
regioselective and stereoselective para-ortho oxidative coupling
Papaver somniferum
Source Tissue
Source Tissue
Commentary
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
-20C, microsome-bound enzyme, freezing causes a total loss of activity
Papaver somniferum
-70C, microsome-bound enzyme, 20% loss of activity after 1 month
Papaver somniferum
22C, 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
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-reticuline + [reduced NADPH-hemoprotein reductase] + O2
strictly dependent on NADPH as reducing cofactor and on (R)-configurated reticuline
393875
Papaver somniferum
salutaridine + [oxidized NADPH-hemoprotein reductase] + H2O
-
393875
Papaver somniferum
-
(R)-reticuline + [reduced NADPH-hemoprotein reductase] + O2
formation of salutaridine, a key intermediate in morphine biosynthesis
393875
Papaver somniferum
salutaridine + [oxidized NADPH-hemoprotein reductase] + H2O
-
393875
Papaver somniferum
-
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
20
25
-
Papaver somniferum
Temperature Range [C]
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
10
30
10C: about 30% of maximal activity, 30C: about 65% of maximal activity
Papaver somniferum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
-
Papaver somniferum
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6.5
8.5
about 50% of maximal activity at pH 6.5 and pH 8.5
Papaver somniferum
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome P450
enzyme contains cytochrome P450
Papaver somniferum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome P450
enzyme contains cytochrome P450
Papaver somniferum
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Ancymidole
-
Papaver somniferum
CO
in darkness but not in light
Papaver somniferum
Prochloraz
-
Papaver somniferum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.017
-
(R)-reticuline
-
Papaver somniferum
0.15
-
NADPH
-
Papaver somniferum
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
membrane-bound
Papaver somniferum
-
-
mitochondrion
-
Papaver somniferum
5739
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(R)-reticuline + [reduced NADPH-hemoprotein reductase] + O2
Papaver somniferum
formation of salutaridine, a key intermediate in morphine biosynthesis
salutaridine + [oxidized NADPH-hemoprotein reductase] + H2O
-
Papaver somniferum
-
Source Tissue (protein specific)
Source Tissue
Commentary
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 (protein specific)
Storage Stability
Organism
-20C, microsome-bound enzyme, freezing causes a total loss of activity
Papaver somniferum
-70C, microsome-bound enzyme, 20% loss of activity after 1 month
Papaver somniferum
22C, 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) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-reticuline + [reduced NADPH-hemoprotein reductase] + O2
strictly dependent on NADPH as reducing cofactor and on (R)-configurated reticuline
393875
Papaver somniferum
salutaridine + [oxidized NADPH-hemoprotein reductase] + H2O
-
393875
Papaver somniferum
-
(R)-reticuline + [reduced NADPH-hemoprotein reductase] + O2
formation of salutaridine, a key intermediate in morphine biosynthesis
393875
Papaver somniferum
salutaridine + [oxidized NADPH-hemoprotein reductase] + H2O
-
393875
Papaver somniferum
-
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
20
25
-
Papaver somniferum
Temperature Range [C] (protein specific)
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
10
30
10C: about 30% of maximal activity, 30C: about 65% of maximal activity
Papaver somniferum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
-
Papaver somniferum
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6.5
8.5
about 50% of maximal activity at pH 6.5 and pH 8.5
Papaver somniferum
Other publictions for EC 1.14.19.67
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
743574
Fossati
Synthesis of morphinan alkalo ...
Papaver somniferum
PLoS ONE
10
e0124459
2015
-
-
1
-
-
-
-
-
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-
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3
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1
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1
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1
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-
-
-
-
-
-
-
-
-
-
-
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-
728475
Onoyovwe
Morphine biosynthesis in opium ...
Papaver somniferum
Plant Cell
25
4110-4122
2013
-
-
-
-
-
-
-
-
-
-
1
1
-
2
-
-
-
-
-
5
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
1
1
-
-
-
-
-
5
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
720707
Wijekoon
Systematic knockdown of morphi ...
Papaver somniferum
Plant J.
69
1052-1063
2012
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
2
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-
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1
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2
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
698930
Gesell
CYP719B1 is salutaridine synth ...
Papaver somniferum
J. Biol. Chem.
284
24432-24442
2009
-
-
1
-
-
-
-
1
-
-
1
1
-
4
-
-
1
-
-
-
-
-
2
-
2
-
-
1
2
-
-
1
-
-
-
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-
1
1
-
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-
-
-
-
1
-
-
1
1
-
-
-
1
-
-
-
-
2
-
2
-
-
1
2
-
-
-
-
-
-
-
-
-
393876
Amann
-
Purification and characterizat ...
Bos taurus, Homo sapiens, Mus musculus, Ovis aries, Rattus norvegicus, Sus scrofa
Heterocycles
1
425-440
1995
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-
-
-
-
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1
9
-
1
1
-
6
-
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1
-
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1
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3
1
-
-
-
-
-
-
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7
-
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-
7
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-
-
-
-
-
1
9
-
1
1
-
-
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1
-
1
-
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3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
393875
Gerardy R.; Zenk
-
Formation of salutaridine from ...
Papaver somniferum
Phytochemistry
32
79-86
1993
-
-
-
-
-
-
3
2
2
-
-
1
-
1
-
-
-
1
-
5
-
4
2
-
1
1
-
-
1
1
-
1
-
-
-
-
-
-
1
-
-
-
-
3
-
2
2
-
-
1
-
-
-
-
-
5
-
4
2
-
1
1
-
-
1
1
-
-
-
-
-
-
-
-