BRENDA - Enzyme Database
show all sequences of 1.11.2.3

Purification and characterization of solubilized peroxygenase from microsomes of pea seeds

Ishimaru, A.; J. Biol. Chem. 254, 8427-8433 (1979)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.07
-
indole
partially purified enzyme, using linoleic acid hydroperoxide as cosubstrate, at pH 7.2 and 25°C
Pisum sativum
0.08
-
indole
partially purified enzyme, using linoleic acid hydroperoxide as cosubstrate, at pH 7.2 and 25°C
Pisum sativum
0.26
-
linoleic acid hydroperoxide
partially purified enzyme, at pH 7.2 and 25°C
Pisum sativum
1.3
-
H2O2
partially purified enzyme, at pH 7.2 and 25°C
Pisum sativum
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
-
Pisum sativum
16020
-
microsome
-
Pisum sativum
-
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
41000
-
3 * 62500 + 1 * 41000, SDS-PAGE
Pisum sativum
62500
-
3 * 62500 + 1 * 41000, SDS-PAGE
Pisum sativum
230000
-
gel filtration
Pisum sativum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
additional information
Pisum sativum
peroxygenase exists in nature as a complex with a carotenoid-binding macromolecule
?
-
-
-
Organic Solvent Stability
Organic Solvent
Commentary
Organism
Glycerol
20% (v/v) glycerol remarkably stabilizes the enzyme. The enzyme extracted with cholate or deoxycholate is very stable in the presence of glycerol
Pisum sativum
Triton X-100
the solubilized peroxygenase is unstable especially in the presence of Triton X-100
Pisum sativum
Tween
the solubilized peroxygenase is unstable especially in the presence of Tween 80
Pisum sativum
Organism
Organism
UniProt
Commentary
Textmining
Pisum sativum
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
DEAF-cellulose column chromatography and agarose gel column chromatography
Pisum sativum
Source Tissue
Source Tissue
Commentary
Organism
Textmining
seed
-
Pisum sativum
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.54
-
unpurified microsomal enzyme, at pH 7.2 and 25°C
Pisum sativum
3.4
-
partially purified microsomal enzyme, at pH 7.2 and 25°C
Pisum sativum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
indole + H2O2
-
712329
Pisum sativum
?
-
-
-
?
indole + linoleic acid hydroperoxide
-
712329
Pisum sativum
?
-
-
-
?
additional information
peroxygenase exists in nature as a complex with a carotenoid-binding macromolecule
712329
Pisum sativum
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
heterotetramer
3 * 62500 + 1 * 41000, SDS-PAGE
Pisum sativum
Synonyms
Synonyms
Commentary
Organism
hydrogen peroxide-reducible hemoprotein
-
Pisum sativum
peroxygenase, hydroperoxide-dependent hydroxylase
-
Pisum sativum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.1
-
partially purified enzyme, using 0.2 mM linoleic acid hydroperoxide as cosubstrate
Pisum sativum
7.2
-
membrane-bound enzyme, using 0.2 mM linoleic acid hydroperoxide as cosubstrate; partially purified enzyme, using 1.0 mM H2O2 as cosubstrate
Pisum sativum
8.7
-
membrane-bound enzyme, using 1.0 mM H2O2 as cosubstrate
Pisum sativum
Cofactor
Cofactor
Commentary
Organism
Structure
heme
the purified enzyme preparation contains 3.2 nmol of protoheme/mg of protein
Pisum sativum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
heme
the purified enzyme preparation contains 3.2 nmol of protoheme/mg of protein
Pisum sativum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.07
-
indole
partially purified enzyme, using linoleic acid hydroperoxide as cosubstrate, at pH 7.2 and 25°C
Pisum sativum
0.08
-
indole
partially purified enzyme, using linoleic acid hydroperoxide as cosubstrate, at pH 7.2 and 25°C
Pisum sativum
0.26
-
linoleic acid hydroperoxide
partially purified enzyme, at pH 7.2 and 25°C
Pisum sativum
1.3
-
H2O2
partially purified enzyme, at pH 7.2 and 25°C
Pisum sativum
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
-
Pisum sativum
16020
-
microsome
-
Pisum sativum
-
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
41000
-
3 * 62500 + 1 * 41000, SDS-PAGE
Pisum sativum
62500
-
3 * 62500 + 1 * 41000, SDS-PAGE
Pisum sativum
230000
-
gel filtration
Pisum sativum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
additional information
Pisum sativum
peroxygenase exists in nature as a complex with a carotenoid-binding macromolecule
?
-
-
-
Organic Solvent Stability (protein specific)
Organic Solvent
Commentary
Organism
Glycerol
20% (v/v) glycerol remarkably stabilizes the enzyme. The enzyme extracted with cholate or deoxycholate is very stable in the presence of glycerol
Pisum sativum
Triton X-100
the solubilized peroxygenase is unstable especially in the presence of Triton X-100
Pisum sativum
Tween
the solubilized peroxygenase is unstable especially in the presence of Tween 80
Pisum sativum
Purification (Commentary) (protein specific)
Commentary
Organism
DEAF-cellulose column chromatography and agarose gel column chromatography
Pisum sativum
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
seed
-
Pisum sativum
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.54
-
unpurified microsomal enzyme, at pH 7.2 and 25°C
Pisum sativum
3.4
-
partially purified microsomal enzyme, at pH 7.2 and 25°C
Pisum sativum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
indole + H2O2
-
712329
Pisum sativum
?
-
-
-
?
indole + linoleic acid hydroperoxide
-
712329
Pisum sativum
?
-
-
-
?
additional information
peroxygenase exists in nature as a complex with a carotenoid-binding macromolecule
712329
Pisum sativum
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
heterotetramer
3 * 62500 + 1 * 41000, SDS-PAGE
Pisum sativum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.1
-
partially purified enzyme, using 0.2 mM linoleic acid hydroperoxide as cosubstrate
Pisum sativum
7.2
-
membrane-bound enzyme, using 0.2 mM linoleic acid hydroperoxide as cosubstrate; partially purified enzyme, using 1.0 mM H2O2 as cosubstrate
Pisum sativum
8.7
-
membrane-bound enzyme, using 1.0 mM H2O2 as cosubstrate
Pisum sativum
Other publictions for EC 1.11.2.3
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
Synonyms
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)
742334
Shimada
Leaf oil bodies are subcellul ...
Arabidopsis thaliana
Curr. Opin. Plant Biol.
25
145-150
2015
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1
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3
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1
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3
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1
1
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743541
Hanano
Involvement of the caleosin/p ...
Arabidopsis thaliana
Plant Signal. Behav.
10
e991574
2015
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6
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1
1
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743492
Blee
The reductase activity of the ...
Arabidopsis thaliana
Plant Physiol.
166
109-124
2014
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1
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4
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1
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11
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11
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1
1
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725747
Fuchs
-
Epoxidation, hydroxylation and ...
Solanum lycopersicum
J. Mol. Catal. B
96
52-60
2013
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1
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3
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1
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724973
Blee
A non-canonical caleosin from ...
Arabidopsis thaliana
FEBS J.
279
3981-3995
2012
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1
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1
1
1
3
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4
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3
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4
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3
1
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726143
Kim
A stress-responsive caleosin-l ...
Arabidopsis thaliana
Plant Cell Physiol.
52
874-884
2011
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1
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1
1
1
1
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726222
Meesapyodsuk
A peroxygenase pathway involve ...
Avena sativa
Plant Physiol.
157
454-463
2011
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1
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2
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1
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1
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6
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1
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1
1
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713295
Partridge
Roles of a membrane-bound cale ...
Arabidopsis thaliana
Plant Physiol. Biochem.
47
796-806
2009
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3
1
2
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6
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1
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712256
Piazza
-
One-pot synthesis of fatty aci ...
Avena sativa
J. Am. Oil Chem. Soc.
83
1021-1025
2006
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712359
Hanano
Plant seed peroxygenase is an ...
Arabidopsis thaliana, Avena sativa
J. Biol. Chem.
281
33140-33151
2006
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2
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2
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2
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4
2
2
10
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7
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2
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10
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2
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10
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10
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671684
Magri
-
Immobilization of soybean seed ...
Glycine max
Biocatal. Biotransform.
23
339-346
2005
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712357
Kandel
Cloning, functional expression ...
Triticum aestivum
J. Biol. Chem.
280
35881-35889
2005
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712255
Piazza
-
Synthesis of a fatty tetrahydr ...
Avena sativa
J. Am. Oil Chem. Soc.
81
933-937
2004
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712776
Piazza
-
Epoxidation of fatty acids, fa ...
Avena sativa
J. Mol. Catal. B
21
143-151
2003
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1
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15
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15
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713275
Lequeu
Formation of plant cuticle: ev ...
Avena sativa, Glycine max, Zea mays
Plant J.
36
155-164
2003
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18
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6
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3
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3
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15
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15
18
3
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1
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3
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6
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6
6
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439735
Henriksen
Structure of soybean seed coat ...
Soja hispida
Protein Sci.
10
108-115
2001
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1
1
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1
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711277
Takamura
Oxygenation of (3Z)-alkenal to ...
Glycine max
Biochim. Biophys. Acta
1303
83-91
1996
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713303
Hamberg
Peroxygenase-catalyzed fatty a ...
Avena sativa, Hordeum vulgare, Hordeum vulgare subsp. vulgare, Secale cereale, Triticum aestivum
Plant Physiol.
110
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