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Literature summary for 1.11.1.13 extracted from

  • Banci, L.; Bertini, I.; Pease, E.A.; Tien, M.; Turano, P.
    1H NMR investigation of manganese peroxidase from Phanerochaete chrysosporium. A comparison with other peroxidases (1992), Biochemistry, 31, 10009-10017.
    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
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Mn2+ + H+ + H2O2 Phanerodontia chrysosporium initial depolymerization of the lignin polymer Mn3+ + H2O
-
?

Organism

Organism UniProt Comment Textmining
Phanerodontia chrysosporium
-
overproducing strain PSBL-1
-
Phanerodontia chrysosporium
-
isoenzymes H3, H4 and H5
-

Purification (Commentary)

Purification (Comment) Organism
isoenzyme H4 Phanerodontia chrysosporium

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Mn2+ + H+ + H2O2 oxidation of Mn2+ to Mn3+ at a redox potential of 1.5 V Phanerodontia chrysosporium Mn3+ + H2O
-
?
Mn2+ + H+ + H2O2 initial depolymerization of the lignin polymer Phanerodontia chrysosporium Mn3+ + H2O
-
?
additional information structural properties Phanerodontia chrysosporium ?
-
?

Cofactor

Cofactor Comment Organism Structure
heme enzyme contains a pentacoordinated, essentially high-spin ferric heme Phanerodontia chrysosporium