Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.11.2.3 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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment 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 Comment Organism GeneOntology No. Textmining
membrane
-
Pisum sativum 16020
-
microsome
-
Pisum sativum
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment 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 Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Pisum sativum peroxygenase exists in nature as a complex with a carotenoid-binding macromolecule ?
-
?

Organic Solvent Stability

Organic Solvent Comment 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 Comment Textmining
Pisum sativum
-
-
-

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining
seed
-
Pisum sativum
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment 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 Comment Substrates Organism Products Comment (Products) Rev. Reac.
indole + H2O2
-
Pisum sativum ?
-
?
indole + linoleic acid hydroperoxide
-
Pisum sativum ?
-
?
additional information peroxygenase exists in nature as a complex with a carotenoid-binding macromolecule Pisum sativum ?
-
?

Subunits

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

Synonyms

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment 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 Pisum sativum
7.2
-
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 Comment Organism Structure
heme the purified enzyme preparation contains 3.2 nmol of protoheme/mg of protein Pisum sativum