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Literature summary for 1.11.1.13 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

Activating Compound Comment Organism Structure
H2O2 H2O2-dependent Phanerodontia chrysosporium

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Phanerodontia chrysosporium
-
-

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Phanerodontia chrysosporium
-
white rot basidomycete
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
Phanerodontia chrysosporium

Purification (Commentary)

Purification (Comment) Organism
-
Phanerodontia chrysosporium

Reaction

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
Mn2+ + H+ + H2O2 absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes vanillyl alcohol ?
Mn2+ + H+ + H2O2 absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes o-dianisidine ?
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 ?
Mn2+ + H+ + H2O2 absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes p-cresol ?
Mn2+ + H+ + H2O2 absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes guaiacol ?
Mn2+ + H+ + H2O2 important component of lignin degradation system Phanerodontia chrysosporium Mn3+ + H2O
-
?
additional information no oxidation of Co2+ Phanerodontia chrysosporium ?
-
?
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 ?
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?
additional information enzyme oxidizes ferrocyanide Phanerodontia chrysosporium ?
-
?
additional information large substrates have no ready access to the catalytic center Phanerodontia chrysosporium ?
-
?
additional information no oxidation of Ni2+ Phanerodontia chrysosporium ?
-
?

Cofactor

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