BRENDA - Enzyme Database

Characterization of Ceriporiopsis subvermispora bicupin oxalate oxidase expressed in Pichia pastoris

Moussatche, P.; Angerhofer, A.; Imaram, W.; Hoffer, E.; Uberto, K.; Brooks, C.; Bruce, C.; Sledge, D.; Richards, N.G.; Moomaw, E.W.; Arch. Biochem. Biophys. 509, 100-107 (2011)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
1.2.3.4
expressed in Pichia pastoris strain X-33
Gelatoporia subvermispora
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
1.2.3.4
acetate
competitive inhibition
Gelatoporia subvermispora
1.2.3.4
glycolate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
Gelatoporia subvermispora
1.2.3.4
glyoxylate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
Gelatoporia subvermispora
1.2.3.4
malate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
Gelatoporia subvermispora
1.2.3.4
malonate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
Gelatoporia subvermispora
1.2.3.4
pyruvate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
Gelatoporia subvermispora
1.2.3.4
succinate
competitive inhibition
Gelatoporia subvermispora
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.2.3.4
0.1
-
oxalate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
1.2.3.4
1.5
-
oxalate
in succinate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
1.2.3.4
14.9
-
oxalate
in acetate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
1.2.3.4
Mn2+
contains between 0.1 and 0.4 mole Mn per mole enzyme
Gelatoporia subvermispora
1.2.3.4
additional information
incubation of the apoenzyme with a 100fold molar excess of MgCl2, CoCl2, CuCl2, ZnCl2, NiCl2, FeCl2 or FeCl3, individually, does not influence enzymatic activity
Gelatoporia subvermispora
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.2.3.4
45000
-
x * 45000, calculated from amino acid sequence
Gelatoporia subvermispora
1.2.3.4
66000
-
x * 66000, SDS-PAGE
Gelatoporia subvermispora
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.2.3.4
additional information
Gelatoporia subvermispora
the recombinant enzyme possesses less than 0.1% oxalate decarboxylase activity
?
-
-
-
1.2.3.4
oxalate + O2 + 2 H+
Gelatoporia subvermispora
-
CO2 + 2 H2O2
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.2.3.4
Gelatoporia subvermispora
Q5ZH56
-
-
Posttranslational Modification
EC Number
Posttranslational Modification
Commentary
Organism
1.2.3.4
glycoprotein
carbohydrates make up approximately 30% of the enzyme’s mass
Gelatoporia subvermispora
Purification (Commentary)
EC Number
Commentary
Organism
1.2.3.4
DEAE-Sepharose column chromatography and butyl Sepharose column chromatography
Gelatoporia subvermispora
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1.2.3.4
0.4
-
crude extract, in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
1.2.3.4
12.7
-
after 32fold purification, in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.3.4
additional information
the recombinant enzyme possesses less than 0.1% oxalate decarboxylase activity
724114
Gelatoporia subvermispora
?
-
-
-
-
1.2.3.4
oxalate + O2 + 2 H+
-
724114
Gelatoporia subvermispora
CO2 + 2 H2O2
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
1.2.3.4
?
x * 45000, calculated from amino acid sequence; x * 66000, SDS-PAGE
Gelatoporia subvermispora
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.2.3.4
4
-
-
Gelatoporia subvermispora
pH Range
EC Number
pH Minimum
pH Maximum
Commentary
Organism
1.2.3.4
3.5
5.5
about 57% activity at pH 3.5, 100% activity at pH 4.0, about 82% activity at pH 4.5, about 60% activity at pH 5.0, about 27% activity at pH 5.5
Gelatoporia subvermispora
Ki Value [mM]
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
1.2.3.4
3
-
malonate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
1.2.3.4
3.9
-
acetate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
1.2.3.4
15
-
glyoxylate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
1.2.3.4
17
-
pyruvate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
1.2.3.4
28
-
glycolate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
1.2.3.4
52
-
malate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.2.3.4
expressed in Pichia pastoris strain X-33
Gelatoporia subvermispora
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.2.3.4
acetate
competitive inhibition
Gelatoporia subvermispora
1.2.3.4
glycolate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
Gelatoporia subvermispora
1.2.3.4
glyoxylate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
Gelatoporia subvermispora
1.2.3.4
malate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
Gelatoporia subvermispora
1.2.3.4
malonate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
Gelatoporia subvermispora
1.2.3.4
pyruvate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
Gelatoporia subvermispora
1.2.3.4
succinate
competitive inhibition
Gelatoporia subvermispora
Ki Value [mM] (protein specific)
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
1.2.3.4
3
-
malonate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
1.2.3.4
3.9
-
acetate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
1.2.3.4
15
-
glyoxylate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
1.2.3.4
17
-
pyruvate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
1.2.3.4
28
-
glycolate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
1.2.3.4
52
-
malate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.2.3.4
0.1
-
oxalate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
1.2.3.4
1.5
-
oxalate
in succinate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
1.2.3.4
14.9
-
oxalate
in acetate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
1.2.3.4
Mn2+
contains between 0.1 and 0.4 mole Mn per mole enzyme
Gelatoporia subvermispora
1.2.3.4
additional information
incubation of the apoenzyme with a 100fold molar excess of MgCl2, CoCl2, CuCl2, ZnCl2, NiCl2, FeCl2 or FeCl3, individually, does not influence enzymatic activity
Gelatoporia subvermispora
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.2.3.4
45000
-
x * 45000, calculated from amino acid sequence
Gelatoporia subvermispora
1.2.3.4
66000
-
x * 66000, SDS-PAGE
Gelatoporia subvermispora
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.2.3.4
additional information
Gelatoporia subvermispora
the recombinant enzyme possesses less than 0.1% oxalate decarboxylase activity
?
-
-
-
1.2.3.4
oxalate + O2 + 2 H+
Gelatoporia subvermispora
-
CO2 + 2 H2O2
-
-
?
Posttranslational Modification (protein specific)
EC Number
Posttranslational Modification
Commentary
Organism
1.2.3.4
glycoprotein
carbohydrates make up approximately 30% of the enzyme’s mass
Gelatoporia subvermispora
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.2.3.4
DEAE-Sepharose column chromatography and butyl Sepharose column chromatography
Gelatoporia subvermispora
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1.2.3.4
0.4
-
crude extract, in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
1.2.3.4
12.7
-
after 32fold purification, in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.3.4
additional information
the recombinant enzyme possesses less than 0.1% oxalate decarboxylase activity
724114
Gelatoporia subvermispora
?
-
-
-
-
1.2.3.4
oxalate + O2 + 2 H+
-
724114
Gelatoporia subvermispora
CO2 + 2 H2O2
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.2.3.4
?
x * 45000, calculated from amino acid sequence; x * 66000, SDS-PAGE
Gelatoporia subvermispora
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.2.3.4
4
-
-
Gelatoporia subvermispora
pH Range (protein specific)
EC Number
pH Minimum
pH Maximum
Commentary
Organism
1.2.3.4
3.5
5.5
about 57% activity at pH 3.5, 100% activity at pH 4.0, about 82% activity at pH 4.5, about 60% activity at pH 5.0, about 27% activity at pH 5.5
Gelatoporia subvermispora
Expression
EC Number
Organism
Commentary
Expression
1.2.3.4
Gelatoporia subvermispora
expression is induced by methanol
up
Expression (protein specific)
EC Number
Organism
Commentary
Expression
1.2.3.4
Gelatoporia subvermispora
expression is induced by methanol
up