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

BRENDA support

Literature summary extracted from

  • Perie, F.H.; Sheng, D.; Gold, M.H.
    Purification and characterization of two manganese peroxidase isoenzymes from the white-rot basidiomycete Dichomitus squalens (1996), Biochim. Biophys. Acta, 1297, 139-148.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.11.1.13 alpha-hydroxy acid activates by chelating and stabilizing Mn3+ rather than activating the enzyme Dichomitus squalens
1.11.1.13 citrate activates, chelates and stabilizes Mn3+ Dichomitus squalens
1.11.1.13 gluconate activates, chelates and stabilizes Mn3+ Dichomitus squalens
1.11.1.13 glycolate activates, chelates and stabilizes Mn3+ Dichomitus squalens
1.11.1.13 H2O2 H2O2-dependent Dichomitus squalens
1.11.1.13 L-malate activates by chelating and stabilizing Mn3+ Dichomitus squalens
1.11.1.13 L-Tartrate stimulates by chelating and stabilizing Mn3+ Dichomitus squalens
1.11.1.13 Lactate activates, chelates and stabilizes Mn3+ Dichomitus squalens
1.11.1.13 Maleate slightly activates, chelates and stabilizes Mn3+ Dichomitus squalens
1.11.1.13 malonate stimulates by chelating and stabilizing Mn3+ Dichomitus squalens
1.11.1.13 additional information acetate is not an effective chelator Dichomitus squalens
1.11.1.13 oxalate activates by chelating and stabilizing Mn3+ Dichomitus squalens
1.11.1.13 phenylacetate activates, chelates and stabilizes Mn3+ Dichomitus squalens
1.11.1.13 phosphate activates, chelates and stabilizes Mn3+ Dichomitus squalens
1.11.1.13 succinate slightly activates, chelates Mn3+ Dichomitus squalens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.13 MnP1 and MnP2 are encoded by different genes Dichomitus squalens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.11.1.13 0.025
-
Mn2+ MnP2 Dichomitus squalens
1.11.1.13 0.039
-
Mn2+ MnP1 Dichomitus squalens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.11.1.13 extracellular
-
Dichomitus squalens
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.11.1.13 additional information expression of MnP isoenzymes is dependent on the presence of Mn, expression rather than enzymatic activity is regulated by Mn Dichomitus squalens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.11.1.13 48000
-
MnP1 and MnP2, gel filtration Dichomitus squalens
1.11.1.13 48900
-
1 * 48000, MnP1, 1 * 48900, MnP2, SDS-PAGE Dichomitus squalens

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 Dichomitus squalens involved in lignin-degradation Mn3+ + H2O
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.13 Dichomitus squalens
-
white rot fungus
-
1.11.1.13 Dichomitus squalens
-
2 isoenzymes: MnP1 and MnP2, syn. Polyporus anceps
-
1.11.1.13 Dichomitus squalens CBS 432.34
-
2 isoenzymes: MnP1 and MnP2, syn. Polyporus anceps
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.11.1.13 glycoprotein neutral carbohydrate content: MnP1: 8.5%, MnP2: 10.3% Dichomitus squalens

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.13 148fold purification of MnP1 and 157fold purification of MnP2 Dichomitus squalens

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.11.1.13 174
-
MnP1 Dichomitus squalens
1.11.1.13 184
-
MnP2 Dichomitus squalens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.13 Mn2+ + H+ + H2O2 specifically oxidizes Mn2+ Dichomitus squalens Mn3+ + H2O alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme ?
1.11.1.13 Mn2+ + H+ + H2O2 specifically oxidizes Mn2+ Dichomitus squalens Mn3+ + H2O dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme ?
1.11.1.13 Mn2+ + H+ + H2O2 specifically oxidizes Mn2+ Dichomitus squalens Mn3+ + H2O Mn3+ oxidizes o-phenylenediamine and p-anisidine ?
1.11.1.13 Mn2+ + H+ + H2O2 specifically oxidizes Mn2+ Dichomitus squalens Mn3+ + H2O Mn3+ oxidizes o-dianisidine ?
1.11.1.13 Mn2+ + H+ + H2O2 specifically oxidizes Mn2+ Dichomitus squalens Mn3+ + H2O Mn3+ oxidizes amines ?
1.11.1.13 Mn2+ + H+ + H2O2 specifically oxidizes Mn2+ Dichomitus squalens Mn3+ + H2O Mn3+ oxidizes a variety of phenols ?
1.11.1.13 Mn2+ + H+ + H2O2 specifically oxidizes Mn2+ Dichomitus squalens Mn3+ + H2O Mn3+ oxidizes guaiacol ?
1.11.1.13 Mn2+ + H+ + H2O2 single Mn2+ binding site in the vicinity of the heme Dichomitus squalens Mn3+ + H2O alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme ?
1.11.1.13 Mn2+ + H+ + H2O2 single Mn2+ binding site in the vicinity of the heme Dichomitus squalens Mn3+ + H2O dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme ?
1.11.1.13 Mn2+ + H+ + H2O2 single Mn2+ binding site in the vicinity of the heme Dichomitus squalens Mn3+ + H2O Mn3+ oxidizes o-phenylenediamine and p-anisidine ?
1.11.1.13 Mn2+ + H+ + H2O2 single Mn2+ binding site in the vicinity of the heme Dichomitus squalens Mn3+ + H2O Mn3+ oxidizes o-dianisidine ?
1.11.1.13 Mn2+ + H+ + H2O2 single Mn2+ binding site in the vicinity of the heme Dichomitus squalens Mn3+ + H2O Mn3+ oxidizes amines ?
1.11.1.13 Mn2+ + H+ + H2O2 single Mn2+ binding site in the vicinity of the heme Dichomitus squalens Mn3+ + H2O Mn3+ oxidizes a variety of phenols ?
1.11.1.13 Mn2+ + H+ + H2O2 single Mn2+ binding site in the vicinity of the heme Dichomitus squalens Mn3+ + H2O Mn3+ oxidizes guaiacol ?
1.11.1.13 Mn2+ + H+ + H2O2 oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators Dichomitus squalens Mn3+ + H2O alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme ?
1.11.1.13 Mn2+ + H+ + H2O2 oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators Dichomitus squalens Mn3+ + H2O dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme ?
1.11.1.13 Mn2+ + H+ + H2O2 oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators Dichomitus squalens Mn3+ + H2O Mn3+ oxidizes o-phenylenediamine and p-anisidine ?
1.11.1.13 Mn2+ + H+ + H2O2 oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators Dichomitus squalens Mn3+ + H2O Mn3+ oxidizes o-dianisidine ?
1.11.1.13 Mn2+ + H+ + H2O2 oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators Dichomitus squalens Mn3+ + H2O Mn3+ oxidizes amines ?
1.11.1.13 Mn2+ + H+ + H2O2 oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators Dichomitus squalens Mn3+ + H2O Mn3+ oxidizes a variety of phenols ?
1.11.1.13 Mn2+ + H+ + H2O2 oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators Dichomitus squalens Mn3+ + H2O Mn3+ oxidizes guaiacol ?
1.11.1.13 Mn2+ + H+ + H2O2 involved in lignin-degradation Dichomitus squalens Mn3+ + H2O
-
?
1.11.1.13 additional information no oxidation of Co2+ Dichomitus squalens ?
-
?
1.11.1.13 additional information enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+ Dichomitus squalens ?
-
?
1.11.1.13 additional information catalytic cycle with oxidized intermediates MnP compound I and II Dichomitus squalens ?
-
?
1.11.1.13 additional information no activity with veratryl alcohol Dichomitus squalens ?
-
?
1.11.1.13 additional information no oxidation of Fe2+, Cu2+, Zn2+ Dichomitus squalens ?
-
?
1.11.1.13 additional information no other metal can substitute Mn2+ Dichomitus squalens ?
-
?
1.11.1.13 additional information enzyme oxidizes 2,6-dimethoxyphenol Dichomitus squalens ?
-
?
1.11.1.13 additional information no oxidation of Ni2+ Dichomitus squalens ?
-
?
1.11.1.13 additional information no oxidation of Co2+ Dichomitus squalens CBS 432.34 ?
-
?
1.11.1.13 additional information enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+ Dichomitus squalens CBS 432.34 ?
-
?
1.11.1.13 additional information catalytic cycle with oxidized intermediates MnP compound I and II Dichomitus squalens CBS 432.34 ?
-
?
1.11.1.13 additional information no activity with veratryl alcohol Dichomitus squalens CBS 432.34 ?
-
?
1.11.1.13 additional information no oxidation of Fe2+, Cu2+, Zn2+ Dichomitus squalens CBS 432.34 ?
-
?

Subunits

EC Number Subunits Comment Organism
1.11.1.13 monomer 1 * 48000, MnP1, 1 * 48900, MnP2, SDS-PAGE Dichomitus squalens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.11.1.13 additional information
-
assay at room temperature Dichomitus squalens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.11.1.13 additional information
-
MnP1: pI 4.1, MnP2: pI 3.9 Dichomitus squalens
1.11.1.13 4.5
-
MnP1 in 50 mM malonate Dichomitus squalens
1.11.1.13 5
-
MnP2 in 50 mM malonate Dichomitus squalens

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.13 heme enzyme contains a pentacoordinated, essentially high-spin ferric heme Dichomitus squalens
1.11.1.13 heme one iron protoporphyrin IX prosthetic group per enzyme molecule Dichomitus squalens