BRENDA - Enzyme Database show
show all sequences of 1.14.19.66

The purification and characterization of a unique cytochrome P-450 enzyme from Berberis stolonifera plant cell cultures

Stadler, R.; Zenk, M.H.; J. Biol. Chem. 268, 823-831 (1993)

Data extracted from this reference:

Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
46000
-
x * 46000, SDS-PAGE
Berberis stolonifera
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2 (S)-N-methylcoclaurine + 2 (R)-N-methylcoclaurine + [reduced NADPH-hemoprotein reductase] + O2
Berberis stolonifera
enzyme mediates highly regiospecific and stereospecific oxidative phenol coupling to afford natural bisbenzylisoquinoline alkaloids
berbamunine + guattegaumerine + [oxidized NADPH-hemoprotein reductase] + H2O
-
Berberis stolonifera
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Berberis stolonifera
P47195
-
-
Purification (Commentary)
Commentary
Organism
-
Berberis stolonifera
Reaction
Reaction
Commentary
Organism
(S)-N-methylcoclaurine + (R)-N-methylcoclaurine + [reduced NADPH-hemoprotein reductase] + O2 = berbamunine + [oxidized NADPH-hemoprotein reductase] + 2 H2O
regioselective and stereoselective formation of a C-O phenol couple in bisbenzylisoquinoline alkaloid biosynthesis without concomitant incorporation of activated oxygen into the product
Berberis stolonifera
Source Tissue
Source Tissue
Commentary
Organism
Textmining
cell suspension culture
-
Berberis stolonifera
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
additional information
-
-
Berberis stolonifera
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-N-methylcoclaurine + (R)-N-methylcoclaurine + (S)-coclaurine + [reduced NADPH-hemoprotein reductase] + O2
-
393212
Berberis stolonifera
(R,S)-berbamunine + (R,R)-guattegaumerine + (R,S)-2'-norberbamunine + [oxidized NADPH-hemoprotein reductase] + H2O
-
393212
Berberis stolonifera
-
2 (S)-N-methylcoclaurine + 2 (R)-N-methylcoclaurine + [reduced NADPH-hemoprotein reductase] + O2
-
393212
Berberis stolonifera
berbamunine + guattegaumerine + [oxidized NADPH-hemoprotein reductase] + H2O
incubation with equimolar amounts of both (R)-N-methylcoclaurine and (S)-N-methylcoclaurine leads to the formation of berbamunine and guattegaumerine
393212
Berberis stolonifera
-
2 (S)-N-methylcoclaurine + 2 (R)-N-methylcoclaurine + [reduced NADPH-hemoprotein reductase] + O2
enzyme mediates highly regiospecific and stereospecific oxidative phenol coupling to afford natural bisbenzylisoquinoline alkaloids
393212
Berberis stolonifera
berbamunine + guattegaumerine + [oxidized NADPH-hemoprotein reductase] + H2O
-
393212
Berberis stolonifera
-
additional information
incubation with (S)-N-methylcoclaurine and (R)-coclaurine does not lead to a dimeric product, as well as incubations with (S)-N-methylcoclaurine alone or with either (S)-coclaurine or (R)-coclaurine together or individually
393212
Berberis stolonifera
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 46000, SDS-PAGE
Berberis stolonifera
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
35
38
-
Berberis stolonifera
Temperature Range [C]
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
22
46
50% of maximal activity at 22C and 46C
Berberis stolonifera
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
-
Berberis stolonifera
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
8.5
-
Berberis stolonifera
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome P450
enzyme contains 18.2 nmol of cytochrome P450 per mg of enzyme
Berberis stolonifera
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome P450
enzyme contains 18.2 nmol of cytochrome P450 per mg of enzyme
Berberis stolonifera
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
46000
-
x * 46000, SDS-PAGE
Berberis stolonifera
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2 (S)-N-methylcoclaurine + 2 (R)-N-methylcoclaurine + [reduced NADPH-hemoprotein reductase] + O2
Berberis stolonifera
enzyme mediates highly regiospecific and stereospecific oxidative phenol coupling to afford natural bisbenzylisoquinoline alkaloids
berbamunine + guattegaumerine + [oxidized NADPH-hemoprotein reductase] + H2O
-
Berberis stolonifera
-
Purification (Commentary) (protein specific)
Commentary
Organism
-
Berberis stolonifera
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
cell suspension culture
-
Berberis stolonifera
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
additional information
-
-
Berberis stolonifera
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-N-methylcoclaurine + (R)-N-methylcoclaurine + (S)-coclaurine + [reduced NADPH-hemoprotein reductase] + O2
-
393212
Berberis stolonifera
(R,S)-berbamunine + (R,R)-guattegaumerine + (R,S)-2'-norberbamunine + [oxidized NADPH-hemoprotein reductase] + H2O
-
393212
Berberis stolonifera
-
2 (S)-N-methylcoclaurine + 2 (R)-N-methylcoclaurine + [reduced NADPH-hemoprotein reductase] + O2
-
393212
Berberis stolonifera
berbamunine + guattegaumerine + [oxidized NADPH-hemoprotein reductase] + H2O
incubation with equimolar amounts of both (R)-N-methylcoclaurine and (S)-N-methylcoclaurine leads to the formation of berbamunine and guattegaumerine
393212
Berberis stolonifera
-
2 (S)-N-methylcoclaurine + 2 (R)-N-methylcoclaurine + [reduced NADPH-hemoprotein reductase] + O2
enzyme mediates highly regiospecific and stereospecific oxidative phenol coupling to afford natural bisbenzylisoquinoline alkaloids
393212
Berberis stolonifera
berbamunine + guattegaumerine + [oxidized NADPH-hemoprotein reductase] + H2O
-
393212
Berberis stolonifera
-
additional information
incubation with (S)-N-methylcoclaurine and (R)-coclaurine does not lead to a dimeric product, as well as incubations with (S)-N-methylcoclaurine alone or with either (S)-coclaurine or (R)-coclaurine together or individually
393212
Berberis stolonifera
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 46000, SDS-PAGE
Berberis stolonifera
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
35
38
-
Berberis stolonifera
Temperature Range [C] (protein specific)
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
22
46
50% of maximal activity at 22C and 46C
Berberis stolonifera
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
-
Berberis stolonifera
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
8.5
-
Berberis stolonifera
Other publictions for EC 1.14.19.66
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)
393214
Kutchan
Heterologous expression of alk ...
Berberis stolonifera
Gene
179
73-81
1996
-
-
1
-
-
-
-
-
-
-
-
-
-
4
-
-
1
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
393213
Kraus
Molecular cloning and heterolo ...
Berberis stolonifera
Proc. Natl. Acad. Sci. USA
92
2071-2075
1995
-
-
1
-
-
-
-
1
-
-
2
-
-
3
-
-
1
-
-
3
-
-
1
1
2
2
-
1
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
1
-
3
-
-
1
1
2
2
-
1
1
-
-
-
-
-
-
-
-
-
393212
Stadler
The purification and character ...
Berberis stolonifera
J. Biol. Chem.
268
823-831
1993
-
-
-
-
-
-
-
-
-
-
1
1
-
1
-
-
1
1
-
1
1
-
4
1
1
1
-
1
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
1
-
1
1
-
4
1
1
1
-
1
1
-
-
-
-
-
-
-
-
-