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Literature summary for 1.11.1.13 extracted from

  • Paszczynski, A.; Huynh, V.B.; Crawford, R.L.
    Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium (1986), Arch. Biochem. Biophys., 244, 750-765.
    View publication on PubMed
Search for more literature for 1.11.1.13

Activating Compound

Activating Compound Comment Organism Structure
H2O2 H2O2-dependent Phanerodontia chrysosporium
additional information 1 mM verartryl alcohol in growth medium increases activity 2fold Phanerodontia chrysosporium

General Stability

General Stability Organism
heat-inactivated protein, 100°C for 5 min, regains 80% of original activity by storage at 0°C for 1 h Phanerodontia chrysosporium

Inhibitors

Inhibitors Comment Organism Structure
ascorbic acid 0.1 mM, 100% inhibition Phanerodontia chrysosporium
Co2+ 0.1 mM, 67% inhibition Phanerodontia chrysosporium
Cu2+ 0.1 mM, 62% inhibition Phanerodontia chrysosporium
Fe2+ 0.1 mM, 77% inhibition Phanerodontia chrysosporium
Fe3+ 0.1 mM, 34% inhibition Phanerodontia chrysosporium
H2O2 above 0.2 mM Phanerodontia chrysosporium
additional information not inhibited by 5% ethanol, v/v; not inhibited by salicylic acid Phanerodontia chrysosporium
Superoxide dismutase inhibits oxidation of vanillylacetone by about 80% Phanerodontia chrysosporium

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular appears to be closely related to mycelium Phanerodontia chrysosporium
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ stimulates Phanerodontia chrysosporium

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Mn2+ + H+ + H2O2 Phanerodontia chrysosporium involved in lignin-degradation Mn3+ + H2O the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by veratryl alcohol ?

Organism

Organism UniProt Comment Textmining
Phanerodontia chrysosporium
-
-
-
Phanerodontia chrysosporium
-
 white rot basidomycete
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Phanerodontia chrysosporium BKM-F 1767
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein 17% carbohydrates Phanerodontia chrysosporium

Purification (Commentary)

Purification (Comment) Organism
8.1-16fold purification Phanerodontia chrysosporium

Reaction

Reaction Comment Organism Reaction ID
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O mechanism Phanerodontia chrysosporium
a
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O shows properties of a peroxidase and an oxidase Phanerodontia chrysosporium
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
65 134 depending on culture age Phanerodontia chrysosporium

Storage Stability

Storage Stability Organism
5°C, unstable Phanerodontia chrysosporium
frozen, tartrate buffer, pH 4.5, 6 months, stable Phanerodontia chrysosporium

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Mn2+ + H+ + H2O2 completion of MnP catalytic cycle requires Mn2+ Phanerodontia chrysosporium Mn3+ + H2O Mn3+ complex oxidizes a variety of organic substrates ?
Mn2+ + H+ + H2O2 completion of MnP catalytic cycle requires Mn2+ Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes phenolic lignin model compounds ?
Mn2+ + H+ + H2O2 completion of MnP catalytic cycle requires Mn2+ Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes vanillylacetone ?
Mn2+ + H+ + H2O2 completion of MnP catalytic cycle requires Mn2+ Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes syringyl alcohol, syringyl aldehyde, syringic acid, syringaldazine, coniferyl alcohol, sinapic acid ?
Mn2+ + H+ + H2O2 completion of MnP catalytic cycle requires Mn2+ Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes 2,6-dimethoxyphenol ?
Mn2+ + H+ + H2O2 completion of MnP catalytic cycle requires Mn2+ Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes o-dianisidine ?
Mn2+ + H+ + H2O2 completion of MnP catalytic cycle requires Mn2+ Phanerodontia chrysosporium Mn3+ + H2O the diffusible product is Mn3+ ?
Mn2+ + H+ + H2O2 completion of MnP catalytic cycle requires Mn2+ Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes a variety of phenols ?
Mn2+ + H+ + H2O2 completion of MnP catalytic cycle requires Mn2+ Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes guaiacol ?
Mn2+ + H+ + H2O2 oxidizes Mn2+ in presence of H2O2 to a higher oxidation state, enzyme activity is dependent on Mn2+ acting as electron carriers Phanerodontia chrysosporium Mn3+ + H2O Mn3+ complex oxidizes a variety of organic substrates ?
Mn2+ + H+ + H2O2 oxidizes Mn2+ in presence of H2O2 to a higher oxidation state, enzyme activity is dependent on Mn2+ acting as electron carriers Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes phenolic lignin model compounds ?
Mn2+ + H+ + H2O2 oxidizes Mn2+ in presence of H2O2 to a higher oxidation state, enzyme activity is dependent on Mn2+ acting as electron carriers Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes vanillylacetone ?
Mn2+ + H+ + H2O2 oxidizes Mn2+ in presence of H2O2 to a higher oxidation state, enzyme activity is dependent on Mn2+ acting as electron carriers Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes syringyl alcohol, syringyl aldehyde, syringic acid, syringaldazine, coniferyl alcohol, sinapic acid ?
Mn2+ + H+ + H2O2 oxidizes Mn2+ in presence of H2O2 to a higher oxidation state, enzyme activity is dependent on Mn2+ acting as electron carriers Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes 2,6-dimethoxyphenol ?
Mn2+ + H+ + H2O2 oxidizes Mn2+ in presence of H2O2 to a higher oxidation state, enzyme activity is dependent on Mn2+ acting as electron carriers Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes o-dianisidine ?
Mn2+ + H+ + H2O2 oxidizes Mn2+ in presence of H2O2 to a higher oxidation state, enzyme activity is dependent on Mn2+ acting as electron carriers Phanerodontia chrysosporium Mn3+ + H2O the diffusible product is Mn3+ ?
Mn2+ + H+ + H2O2 oxidizes Mn2+ in presence of H2O2 to a higher oxidation state, enzyme activity is dependent on Mn2+ acting as electron carriers Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes a variety of phenols ?
Mn2+ + H+ + H2O2 oxidizes Mn2+ in presence of H2O2 to a higher oxidation state, enzyme activity is dependent on Mn2+ acting as electron carriers Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes guaiacol ?
Mn2+ + H+ + H2O2 involved in lignin-degradation Phanerodontia chrysosporium Mn3+ + H2O the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by veratryl alcohol ?
additional information in absence of H2O2 the enzyme shows Mn-dependent oxidase activity against glutathione, dithiothreitol and dihydroxymaleic acid, forming H2O2 at the expense of oxygen Phanerodontia chrysosporium ?
-
 ?
additional information in presence of H2O2 and Mn2+ the enzyme oxidizes a variety of phenolic compounds, especially vinyl and syringyl side-chain substituted substrates Phanerodontia chrysosporium ?
-
 ?
additional information in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+ Phanerodontia chrysosporium ?
-
 ?

Subunits

Subunits Comment Organism
? x * 45000-47000, SDS-PAGE Phanerodontia chrysosporium

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Phanerodontia chrysosporium

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
100
-
 complete inactivation after 5 min, 20% of original activity recovered after storage of heat-inactivated protein for 1 h at 0°C, no reactivation possible after boiling for 20 min Phanerodontia chrysosporium

Cofactor

Cofactor Comment Organism Structure
heme heme protein containing protoporphyrin IX, 0.7 heme per enzyme molecule, iron ions are coordinated with prosthetic groups as high-spin ferriheme complexes Phanerodontia chrysosporium