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Literature summary for 1.11.1.13 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

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

Cloned(Commentary)

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

KM Value [mM]

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

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Dichomitus squalens
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
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]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Mn2+ + H+ + H2O2 Dichomitus squalens involved in lignin-degradation Mn3+ + H2O
-
?

Organism

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

Posttranslational Modification

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

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

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