BRENDA - Enzyme Database show
show all sequences of 1.14.14.163

Acetylation serves as a protective group in noscapine biosynthesis in opium poppy

Dang, T.; Chen, X.; Facchini, P.; Nat. Chem. Biol. 11, 104-106 (2015)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Saccharomyces cerevisiae. Owing to difficulties with heterologous expression in yeast, CYP82X2 is synthesized with the first 60 N-terminal amino acids replaced with the first 43 N-terminal amino acids from the lettuce cytochrome P450 germacrene A oxidase
Papaver somniferum
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0178
-
(S)-1-hydroxy-N-methylcanadine
pH 7.5, 30C
Papaver somniferum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(S)-1-hydroxy-N-methylcanadine + [reduced NADPH-hemoprotein reductase] + O2
Papaver somniferum
the enzyme participates in the biosynthesis of the isoquinoline alkaloid noscapine
(13S,14R)-1,13-dihydroxy-N-methylcanadine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Papaver somniferum
I3PLR0
-
-
Purification (Commentary)
Commentary
Organism
-
Papaver somniferum
Source Tissue
Source Tissue
Commentary
Organism
Textmining
stem
-
Papaver somniferum
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-1-hydroxy-N-methylcanadine + [reduced NADPH-hemoprotein reductase] + O2
the enzyme participates in the biosynthesis of the isoquinoline alkaloid noscapine
748729
Papaver somniferum
(13S,14R)-1,13-dihydroxy-N-methylcanadine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(S)-1-hydroxy-N-methylcanadine + [reduced NADPH-hemoprotein reductase] + O2
the enzyme shows strict substrate specificity
748729
Papaver somniferum
(13S,14R)-1,13-dihydroxy-N-methylcanadine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Papaver somniferum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Papaver somniferum
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Saccharomyces cerevisiae. Owing to difficulties with heterologous expression in yeast, CYP82X2 is synthesized with the first 60 N-terminal amino acids replaced with the first 43 N-terminal amino acids from the lettuce cytochrome P450 germacrene A oxidase
Papaver somniferum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0178
-
(S)-1-hydroxy-N-methylcanadine
pH 7.5, 30C
Papaver somniferum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(S)-1-hydroxy-N-methylcanadine + [reduced NADPH-hemoprotein reductase] + O2
Papaver somniferum
the enzyme participates in the biosynthesis of the isoquinoline alkaloid noscapine
(13S,14R)-1,13-dihydroxy-N-methylcanadine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Papaver somniferum
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
stem
-
Papaver somniferum
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-1-hydroxy-N-methylcanadine + [reduced NADPH-hemoprotein reductase] + O2
the enzyme participates in the biosynthesis of the isoquinoline alkaloid noscapine
748729
Papaver somniferum
(13S,14R)-1,13-dihydroxy-N-methylcanadine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(S)-1-hydroxy-N-methylcanadine + [reduced NADPH-hemoprotein reductase] + O2
the enzyme shows strict substrate specificity
748729
Papaver somniferum
(13S,14R)-1,13-dihydroxy-N-methylcanadine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Papaver somniferum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Papaver somniferum
General Information
General Information
Commentary
Organism
malfunction
CYP719A21, CYP82X1 and CXE1 showed reduced transcript levels in CYP82X2-silenced plants
Papaver somniferum
metabolism
the enzyme participates in the biosynthesis of the isoquinoline alkaloid noscapine
Papaver somniferum
General Information (protein specific)
General Information
Commentary
Organism
malfunction
CYP719A21, CYP82X1 and CXE1 showed reduced transcript levels in CYP82X2-silenced plants
Papaver somniferum
metabolism
the enzyme participates in the biosynthesis of the isoquinoline alkaloid noscapine
Papaver somniferum
Other publictions for EC 1.14.14.163
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)
749191
Li
Complete biosynthesis of nosc ...
Papaver somniferum
Proc. Natl. Acad. Sci. USA
115
E3922-E3931
2018
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1
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748743
Li
Engineering biosynthesis of t ...
Papaver somniferum
Nat. Commun.
7
12137
2016
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1
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1
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748729
Dang
Acetylation serves as a prote ...
Papaver somniferum
Nat. Chem. Biol.
11
104-106
2015
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1
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