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Literature summary extracted from

  • Ishimaru, A.
    Purification and characterization of solubilized peroxygenase from microsomes of pea seeds (1979), J. Biol. Chem., 254, 8427-8433.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.11.2.3 0.07
-
 indole partially purified enzyme, using linoleic acid hydroperoxide as cosubstrate, at pH 7.2 and 25°C Pisum sativum
1.11.2.3 0.08
-
 indole partially purified enzyme, using linoleic acid hydroperoxide as cosubstrate, at pH 7.2 and 25°C Pisum sativum
1.11.2.3 0.26
-
 linoleic acid hydroperoxide partially purified enzyme, at pH 7.2 and 25°C Pisum sativum
1.11.2.3 1.3
-
 H2O2 partially purified enzyme, at pH 7.2 and 25°C Pisum sativum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.11.2.3 membrane
-
 Pisum sativum 16020
-
1.11.2.3 microsome
-
 Pisum sativum
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.11.2.3 41000
-
 3 * 62500 + 1 * 41000, SDS-PAGE Pisum sativum
1.11.2.3 62500
-
 3 * 62500 + 1 * 41000, SDS-PAGE Pisum sativum
1.11.2.3 230000
-
 gel filtration Pisum sativum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.11.2.3 additional information Pisum sativum peroxygenase exists in nature as a complex with a carotenoid-binding macromolecule ?
-
 ?

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
1.11.2.3 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
1.11.2.3 Triton X-100 the solubilized peroxygenase is unstable especially in the presence of Triton X-100 Pisum sativum
1.11.2.3 Tween the solubilized peroxygenase is unstable especially in the presence of Tween 80 Pisum sativum

Organism

EC Number Organism UniProt Comment Textmining
1.11.2.3 Pisum sativum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.2.3 DEAF-cellulose column chromatography and agarose gel column chromatography Pisum sativum

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.11.2.3 seed
-
 Pisum sativum
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.11.2.3 0.54
-
 unpurified microsomal enzyme, at pH 7.2 and 25°C Pisum sativum
1.11.2.3 3.4
-
 partially purified microsomal enzyme, at pH 7.2 and 25°C Pisum sativum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.2.3 indole + H2O2
-
 Pisum sativum ?
-
 ?
1.11.2.3 indole + linoleic acid hydroperoxide
-
 Pisum sativum ?
-
 ?
1.11.2.3 additional information peroxygenase exists in nature as a complex with a carotenoid-binding macromolecule Pisum sativum ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.11.2.3 heterotetramer 3 * 62500 + 1 * 41000, SDS-PAGE Pisum sativum

Synonyms

EC Number Synonyms Comment Organism
1.11.2.3 hydrogen peroxide-reducible hemoprotein
-
 Pisum sativum
1.11.2.3 peroxygenase, hydroperoxide-dependent hydroxylase
-
 Pisum sativum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.11.2.3 7.1
-
 partially purified enzyme, using 0.2 mM linoleic acid hydroperoxide as cosubstrate Pisum sativum
1.11.2.3 7.2
-
 membrane-bound enzyme, using 0.2 mM linoleic acid hydroperoxide as cosubstrate Pisum sativum
1.11.2.3 7.2
-
 partially purified enzyme, using 1.0 mM H2O2 as cosubstrate Pisum sativum
1.11.2.3 8.7
-
 membrane-bound enzyme, using 1.0 mM H2O2 as cosubstrate Pisum sativum

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.2.3 heme the purified enzyme preparation contains 3.2 nmol of protoheme/mg of protein Pisum sativum