BRENDA - Enzyme Database show
show all sequences of 1.14.19.65

Two methylenedioxy bridge forming cytochrome P-450 dependent enzymes are involved in (S)-stylopine biosynthesis

Bauer, W.; Zenk, M.H.; Phytochemistry 30, 2953-2961 (1991)
No PubMed abstract available

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0009
-
(S)-scoulerine
-
Eschscholzia californica
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
-
Eschscholzia californica
-
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(S)-scoulerine + [reduced NADPH-hemoprotein reductase] + O2
Eschscholzia californica
enzyme is induced 20 h after challenging the cell suspension cultur with elicitor
(S)-cheilanthifoline + [oxidized NADPH-hemoprotein reductase] + H2O
-
Eschscholzia californica
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Eschscholzia californica
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
cell suspension culture
-
Eschscholzia californica
-
Storage Stability
Storage Stability
Organism
-20°C, 15% loss of activity after 4 months
Eschscholzia californica
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-scoulerine + [reduced NADPH-hemoprotein reductase] + O2
NADPH is essential for activity, NADH displays only 0.5% turnover of that of NADPH
395597
Eschscholzia californica
(S)-cheilanthifoline + [oxidized NADPH-hemoprotein reductase] + H2O
-
395597
Eschscholzia californica
-
(S)-scoulerine + [reduced NADPH-hemoprotein reductase] + O2
enzyme is induced 20 h after challenging the cell suspension cultur with elicitor
395597
Eschscholzia californica
(S)-cheilanthifoline + [oxidized NADPH-hemoprotein reductase] + H2O
-
395597
Eschscholzia californica
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
-
Eschscholzia californica
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
4
-
half-life: 30 h
Eschscholzia californica
25
-
half-life: 2.5 h
Eschscholzia californica
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
-
Eschscholzia californica
pH Range
pH Minimum
pH Maximum
Commentary
Organism
7
9
about 50% of maximal activity at pH 7 and pH 9
Eschscholzia californica
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome P450
the enzyme is a cytochrome P450 dependent monooxygenase
Eschscholzia californica
FAD
0.004 mM, together with the optimal concentration of NADPH, 0.2 mM, enhances activity by 50%
Eschscholzia californica
FMN
0.004 mM, together with the optimal concentration of NADPH, 0.2 mM, enhances activity by 50%
Eschscholzia californica
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome P450
the enzyme is a cytochrome P450 dependent monooxygenase
Eschscholzia californica
FAD
0.004 mM, together with the optimal concentration of NADPH, 0.2 mM, enhances activity by 50%
Eschscholzia californica
FMN
0.004 mM, together with the optimal concentration of NADPH, 0.2 mM, enhances activity by 50%
Eschscholzia californica
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0009
-
(S)-scoulerine
-
Eschscholzia californica
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
-
Eschscholzia californica
-
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(S)-scoulerine + [reduced NADPH-hemoprotein reductase] + O2
Eschscholzia californica
enzyme is induced 20 h after challenging the cell suspension cultur with elicitor
(S)-cheilanthifoline + [oxidized NADPH-hemoprotein reductase] + H2O
-
Eschscholzia californica
-
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
cell suspension culture
-
Eschscholzia californica
-
Storage Stability (protein specific)
Storage Stability
Organism
-20°C, 15% loss of activity after 4 months
Eschscholzia californica
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-scoulerine + [reduced NADPH-hemoprotein reductase] + O2
NADPH is essential for activity, NADH displays only 0.5% turnover of that of NADPH
395597
Eschscholzia californica
(S)-cheilanthifoline + [oxidized NADPH-hemoprotein reductase] + H2O
-
395597
Eschscholzia californica
-
(S)-scoulerine + [reduced NADPH-hemoprotein reductase] + O2
enzyme is induced 20 h after challenging the cell suspension cultur with elicitor
395597
Eschscholzia californica
(S)-cheilanthifoline + [oxidized NADPH-hemoprotein reductase] + H2O
-
395597
Eschscholzia californica
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
-
Eschscholzia californica
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
4
-
half-life: 30 h
Eschscholzia californica
25
-
half-life: 2.5 h
Eschscholzia californica
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
-
Eschscholzia californica
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
7
9
about 50% of maximal activity at pH 7 and pH 9
Eschscholzia californica
Other publictions for EC 1.14.19.65
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)
746047
Yahyazadeh
-
Cloning and characterization ...
Chelidonium majus
Plant Cell Physiol.
58
1421-1430
2017
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
746447
Hori
Efficient microbial productio ...
Eschscholzia californica
Sci. Rep.
6
22201
2016
-
2
1
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
728446
Takemura
Molecular cloning and characte ...
Eschscholzia californica
Phytochemistry
91
100-108
2013
-
-
-
-
-
-
-
-
-
-
-
1
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
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-
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-
-
-
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-
-
-
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-
1
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1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
711025
Diaz Chavez
Characterization of two methyl ...
Argemone mexicana
Arch. Biochem. Biophys.
507
186-193
2011
-
-
1
-
-
-
-
2
-
-
1
-
-
5
-
-
-
-
-
4
-
-
3
-
1
1
-
1
2
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
4
-
-
3
-
1
1
-
1
2
1
-
-
-
1
1
-
-
-
700725
Ikezawa
CYP719A subfamily of cytochrom ...
Eschscholzia californica
Plant Cell Rep.
28
123-133
2009
1
-
1
-
-
-
-
-
-
-
-
1
-
6
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
395597
Bauer
-
Two methylenedioxy bridge form ...
Eschscholzia californica
Phytochemistry
30
2953-2961
1991
-
-
-
-
-
-
-
1
1
-
-
1
-
1
-
-
-
-
-
1
-
1
2
-
1
-
2
-
1
1
-
3
-
-
-
-
-
-
3
-
-
-
-
-
-
1
1
-
-
1
-
-
-
-
-
1
-
1
2
-
1
-
2
-
1
1
-
-
-
-
-
-
-
-