BRENDA - Enzyme Database show
show all sequences of 1.14.14.98

Isolation and characterization of a cDNA encoding (S)-cis-N-methylstylopine 14-hydroxylase from opium poppy, a key enzyme in sanguinarine biosynthesis

Beaudoin, G.; Facchini, P.; Biochem. Biophys. Res. Commun. 431, 597-603 (2013)

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
protopine + [reduced NADPH-hemoprotein reductase] + O2
Papaver somniferum
hydroxylation of protopine by protopine 6-hydroxylase produces the unstable intermediate 6-hydroxyprotopine that spontaneously rearranges to form dihydrosanguinarine
6-hydroxyprotopine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
ir
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Papaver somniferum
-
opium poppy
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
protopine + [reduced NADPH-hemoprotein reductase] + O2
hydroxylation of protopine by protopine 6-hydroxylase produces the unstable intermediate 6-hydroxyprotopine that spontaneously rearranges to form dihydrosanguinarine
726878
Papaver somniferum
6-hydroxyprotopine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
ir
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
protopine + [reduced NADPH-hemoprotein reductase] + O2
Papaver somniferum
hydroxylation of protopine by protopine 6-hydroxylase produces the unstable intermediate 6-hydroxyprotopine that spontaneously rearranges to form dihydrosanguinarine
6-hydroxyprotopine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
ir
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
protopine + [reduced NADPH-hemoprotein reductase] + O2
hydroxylation of protopine by protopine 6-hydroxylase produces the unstable intermediate 6-hydroxyprotopine that spontaneously rearranges to form dihydrosanguinarine
726878
Papaver somniferum
6-hydroxyprotopine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
ir
Other publictions for EC 1.14.14.98
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)
746409
Verma
Improved sanguinarine product ...
Papaver somniferum
Protoplasma
251
1359-1371
2014
-
-
-
-
-
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
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-
-
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-
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-
-
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
1
1
-
-
726878
Beaudoin
Isolation and characterization ...
Papaver somniferum
Biochem. Biophys. Res. Commun.
431
597-603
2013
-
-
-
-
-
-
-
-
-
-
-
1
-
4
-
-
-
-
-
-
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-
1
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-
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1
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1
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-
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-
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-
728446
Takemura
Molecular cloning and characte ...
Eschscholzia californica
Phytochemistry
91
100-108
2013
-
-
1
-
-
-
1
2
1
-
-
-
-
4
-
-
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-
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5
-
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1
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1
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2
1
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5
-
-
-
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7391
Tanahashi
-
Elicitor induction and charact ...
Chelidonium majus, Dicentra cucullaria, Eschscholzia californica, Eschscholzia lobbii, Fumaria parviflora, no activity in Berberis stolonifera, no activity in Catharanthus roseus
Phytochemistry
29
1113-1122
1990
-
-
-
-
-
-
5
1
5
-
-
5
-
7
-
-
-
-
-
5
-
-
10
-
1
1
-
-
1
1
-
1
-
-
-
-
-
-
1
-
-
-
-
5
-
1
5
-
-
5
-
-
-
-
-
5
-
-
10
-
1
1
-
-
1
1
-
-
-
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-
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-