BRENDA - Enzyme Database

Purification and characterization of two manganese peroxidase isoenzymes from the white-rot basidiomycete Dichomitus squalens

Perie, F.H.; Sheng, D.; Gold, M.H.; Biochim. Biophys. Acta 1297, 139-148 (1996)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
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
Commentary
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
Commentary
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
Commentary
Organism
GeneOntology No.
Textmining
1.11.1.13
extracellular
-
Dichomitus squalens
-
-
Metals/Ions
EC Number
Metals/Ions
Commentary
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]
Commentary
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
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.11.1.13
Mn2+ + H+ + H2O2
Dichomitus squalens
involved in lignin-degradation
Mn3+ + H2O
-
Dichomitus squalens
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.11.1.13
Dichomitus squalens
-
2 isoenzymes: MnP1 and MnP2, syn. Polyporus anceps; white rot fungus
-
1.11.1.13
Dichomitus squalens CBS 432.34
-
2 isoenzymes: MnP1 and MnP2, syn. Polyporus anceps
-
Posttranslational Modification
EC Number
Posttranslational Modification
Commentary
Organism
1.11.1.13
glycoprotein
neutral carbohydrate content: MnP1: 8.5%, MnP2: 10.3%
Dichomitus squalens
Purification (Commentary)
EC Number
Commentary
Organism
1.11.1.13
148fold purification of MnP1 and 157fold purification of MnP2
Dichomitus squalens
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1.11.1.13
174
-
MnP1
Dichomitus squalens
1.11.1.13
184
-
MnP2
Dichomitus squalens
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.11.1.13
Mn2+ + H+ + H2O2
specifically oxidizes Mn2+
439842
Dichomitus squalens
Mn3+ + H2O
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
specifically oxidizes Mn2+
439842
Dichomitus squalens
Mn3+ + H2O
dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
specifically oxidizes Mn2+
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes o-phenylenediamine and p-anisidine
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
specifically oxidizes Mn2+
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes o-dianisidine
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
specifically oxidizes Mn2+
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes amines
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
specifically oxidizes Mn2+
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes a variety of phenols
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
specifically oxidizes Mn2+
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes guaiacol
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
single Mn2+ binding site in the vicinity of the heme
439842
Dichomitus squalens
Mn3+ + H2O
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
single Mn2+ binding site in the vicinity of the heme
439842
Dichomitus squalens
Mn3+ + H2O
dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
single Mn2+ binding site in the vicinity of the heme
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes o-phenylenediamine and p-anisidine
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
single Mn2+ binding site in the vicinity of the heme
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes o-dianisidine
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
single Mn2+ binding site in the vicinity of the heme
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes amines
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
single Mn2+ binding site in the vicinity of the heme
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes a variety of phenols
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
single Mn2+ binding site in the vicinity of the heme
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes guaiacol
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
439842
Dichomitus squalens
Mn3+ + H2O
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
439842
Dichomitus squalens
Mn3+ + H2O
dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes o-phenylenediamine and p-anisidine
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes o-dianisidine
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes amines
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes a variety of phenols
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes guaiacol
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
involved in lignin-degradation
439842
Dichomitus squalens
Mn3+ + H2O
-
439842
Dichomitus squalens
?
1.11.1.13
additional information
no oxidation of Co2+
439842
Dichomitus squalens
?
-
-
-
-
1.11.1.13
additional information
enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
439842
Dichomitus squalens
?
-
-
-
-
1.11.1.13
additional information
catalytic cycle with oxidized intermediates MnP compound I and II
439842
Dichomitus squalens
?
-
-
-
-
1.11.1.13
additional information
no activity with veratryl alcohol
439842
Dichomitus squalens
?
-
-
-
-
1.11.1.13
additional information
no oxidation of Fe2+, Cu2+, Zn2+
439842
Dichomitus squalens
?
-
-
-
-
1.11.1.13
additional information
no other metal can substitute Mn2+
439842
Dichomitus squalens
?
-
-
-
-
1.11.1.13
additional information
enzyme oxidizes 2,6-dimethoxyphenol
439842
Dichomitus squalens
?
-
-
-
-
1.11.1.13
additional information
no oxidation of Ni2+
439842
Dichomitus squalens
?
-
-
-
-
1.11.1.13
additional information
no oxidation of Co2+
439842
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+
439842
Dichomitus squalens CBS 432.34
?
-
-
-
-
1.11.1.13
additional information
catalytic cycle with oxidized intermediates MnP compound I and II
439842
Dichomitus squalens CBS 432.34
?
-
-
-
-
1.11.1.13
additional information
no activity with veratryl alcohol
439842
Dichomitus squalens CBS 432.34
?
-
-
-
-
1.11.1.13
additional information
no oxidation of Fe2+, Cu2+, Zn2+
439842
Dichomitus squalens CBS 432.34
?
-
-
-
-
Subunits
EC Number
Subunits
Commentary
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]
Commentary
Organism
1.11.1.13
additional information
-
assay at room temperature
Dichomitus squalens
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
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
Commentary
Organism
Structure
1.11.1.13
heme
enzyme contains a pentacoordinated, essentially high-spin ferric heme; one iron protoporphyrin IX prosthetic group per enzyme molecule
Dichomitus squalens
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
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) (protein specific)
EC Number
Commentary
Organism
1.11.1.13
MnP1 and MnP2 are encoded by different genes
Dichomitus squalens
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.11.1.13
heme
enzyme contains a pentacoordinated, essentially high-spin ferric heme; one iron protoporphyrin IX prosthetic group per enzyme molecule
Dichomitus squalens
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.11.1.13
0.025
-
Mn2+
MnP2
Dichomitus squalens
1.11.1.13
0.039
-
Mn2+
MnP1
Dichomitus squalens
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
1.11.1.13
extracellular
-
Dichomitus squalens
-
-
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
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] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
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) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.11.1.13
Mn2+ + H+ + H2O2
Dichomitus squalens
involved in lignin-degradation
Mn3+ + H2O
-
Dichomitus squalens
?
Posttranslational Modification (protein specific)
EC Number
Posttranslational Modification
Commentary
Organism
1.11.1.13
glycoprotein
neutral carbohydrate content: MnP1: 8.5%, MnP2: 10.3%
Dichomitus squalens
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.11.1.13
148fold purification of MnP1 and 157fold purification of MnP2
Dichomitus squalens
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1.11.1.13
174
-
MnP1
Dichomitus squalens
1.11.1.13
184
-
MnP2
Dichomitus squalens
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.11.1.13
Mn2+ + H+ + H2O2
specifically oxidizes Mn2+
439842
Dichomitus squalens
Mn3+ + H2O
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
specifically oxidizes Mn2+
439842
Dichomitus squalens
Mn3+ + H2O
dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
specifically oxidizes Mn2+
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes o-phenylenediamine and p-anisidine
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
specifically oxidizes Mn2+
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes o-dianisidine
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
specifically oxidizes Mn2+
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes amines
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
specifically oxidizes Mn2+
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes a variety of phenols
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
specifically oxidizes Mn2+
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes guaiacol
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
single Mn2+ binding site in the vicinity of the heme
439842
Dichomitus squalens
Mn3+ + H2O
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
single Mn2+ binding site in the vicinity of the heme
439842
Dichomitus squalens
Mn3+ + H2O
dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
single Mn2+ binding site in the vicinity of the heme
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes o-phenylenediamine and p-anisidine
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
single Mn2+ binding site in the vicinity of the heme
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes o-dianisidine
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
single Mn2+ binding site in the vicinity of the heme
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes amines
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
single Mn2+ binding site in the vicinity of the heme
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes a variety of phenols
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
single Mn2+ binding site in the vicinity of the heme
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes guaiacol
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
439842
Dichomitus squalens
Mn3+ + H2O
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
439842
Dichomitus squalens
Mn3+ + H2O
dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes o-phenylenediamine and p-anisidine
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes o-dianisidine
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes amines
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes a variety of phenols
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
439842
Dichomitus squalens
Mn3+ + H2O
Mn3+ oxidizes guaiacol
439842
Dichomitus squalens
?
1.11.1.13
Mn2+ + H+ + H2O2
involved in lignin-degradation
439842
Dichomitus squalens
Mn3+ + H2O
-
439842
Dichomitus squalens
?
1.11.1.13
additional information
no oxidation of Co2+
439842
Dichomitus squalens
?
-
-
-
-
1.11.1.13
additional information
enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
439842
Dichomitus squalens
?
-
-
-
-
1.11.1.13
additional information
catalytic cycle with oxidized intermediates MnP compound I and II
439842
Dichomitus squalens
?
-
-
-
-
1.11.1.13
additional information
no activity with veratryl alcohol
439842
Dichomitus squalens
?
-
-
-
-
1.11.1.13
additional information
no oxidation of Fe2+, Cu2+, Zn2+
439842
Dichomitus squalens
?
-
-
-
-
1.11.1.13
additional information
no other metal can substitute Mn2+
439842
Dichomitus squalens
?
-
-
-
-
1.11.1.13
additional information
enzyme oxidizes 2,6-dimethoxyphenol
439842
Dichomitus squalens
?
-
-
-
-
1.11.1.13
additional information
no oxidation of Ni2+
439842
Dichomitus squalens
?
-
-
-
-
1.11.1.13
additional information
no oxidation of Co2+
439842
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+
439842
Dichomitus squalens CBS 432.34
?
-
-
-
-
1.11.1.13
additional information
catalytic cycle with oxidized intermediates MnP compound I and II
439842
Dichomitus squalens CBS 432.34
?
-
-
-
-
1.11.1.13
additional information
no activity with veratryl alcohol
439842
Dichomitus squalens CBS 432.34
?
-
-
-
-
1.11.1.13
additional information
no oxidation of Fe2+, Cu2+, Zn2+
439842
Dichomitus squalens CBS 432.34
?
-
-
-
-
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.11.1.13
monomer
1 * 48000, MnP1, 1 * 48900, MnP2, SDS-PAGE
Dichomitus squalens
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.11.1.13
additional information
-
assay at room temperature
Dichomitus squalens
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
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