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Literature summary extracted from

  • Wariishi, H.; Akileswaran, L.; Gold, M.H.
    Manganese peroxidase from the basidiomycete Phanerochaete chrysosporium: spectral characterization of the oxidized states and the catalytic cycle (1988), Biochemistry, 27, 5365-5370.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.11.1.13 H2O2 H2O2-dependent Phanerodontia chrysosporium

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.11.1.13 extracellular
-
 Phanerodontia chrysosporium
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.11.1.13 46000
-
-
 Phanerodontia chrysosporium

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.11.1.13 Mn2+ + H+ + H2O2 Phanerodontia chrysosporium important component of lignin degradation system Mn3+ + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.13 Phanerodontia chrysosporium
-
 white rot basidomycete
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.11.1.13 glycoprotein
-
 Phanerodontia chrysosporium

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.13
-
 Phanerodontia chrysosporium

Reaction

EC Number Reaction Comment Organism Reaction ID
1.11.1.13 2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O mechanism Phanerodontia chrysosporium
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.13 Mn2+ + H+ + H2O2 absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes syringic acid, 4-hydroxy-3-methoxycinnamic acid, isoeugenol, ascorbate ?
1.11.1.13 Mn2+ + H+ + H2O2 absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes vanillyl alcohol ?
1.11.1.13 Mn2+ + H+ + H2O2 absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes o-dianisidine ?
1.11.1.13 Mn2+ + H+ + H2O2 absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate Phanerodontia chrysosporium Mn3+ + H2O Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines ?
1.11.1.13 Mn2+ + H+ + H2O2 absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes p-cresol ?
1.11.1.13 Mn2+ + H+ + H2O2 absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes guaiacol ?
1.11.1.13 Mn2+ + H+ + H2O2 important component of lignin degradation system Phanerodontia chrysosporium Mn3+ + H2O
-
 ?
1.11.1.13 additional information no oxidation of Co2+ Phanerodontia chrysosporium ?
-
 ?
1.11.1.13 additional information catalytic cycle of enzyme, oxidation states: native enzyme via compound I via compound II to native enzyme, Mn2+ and phenols reduce MnP compound I to compound II, but only Mn2+ is a substrate for MnP compound II, Mn(II)/Mn(III) redox couple enables enzyme to rapidly oxidize terminal phenolic substrates Phanerodontia chrysosporium ?
-
 ?
1.11.1.13 additional information enzyme oxidizes ferrocyanide Phanerodontia chrysosporium ?
-
 ?
1.11.1.13 additional information large substrates have no ready access to the catalytic center Phanerodontia chrysosporium ?
-
 ?
1.11.1.13 additional information no oxidation of Ni2+ Phanerodontia chrysosporium ?
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.13 heme iron protoporphyrin IX prosthetic group Phanerodontia chrysosporium
1.11.1.13 heme heme protein Phanerodontia chrysosporium