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Literature summary extracted from

  • Moussatche, P.; Angerhofer, A.; Imaram, W.; Hoffer, E.; Uberto, K.; Brooks, C.; Bruce, C.; Sledge, D.; Richards, N.G.; Moomaw, E.W.
    Characterization of Ceriporiopsis subvermispora bicupin oxalate oxidase expressed in Pichia pastoris (2011), Arch. Biochem. Biophys., 509, 100-107.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.3.4 expressed in Pichia pastoris strain X-33 Gelatoporia subvermispora

Inhibitors

EC Number Inhibitors Comment 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 Comment 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 Comment 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] Comment 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 Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 UniProt Comment Textmining
1.2.3.4 Gelatoporia subvermispora Q5ZH56
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.2.3.4 glycoprotein carbohydrates make up approximately 30% of the enzyme’s mass Gelatoporia subvermispora

Purification (Commentary)

EC Number Purification (Comment) 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] Comment 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 Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.3.4 additional information the recombinant enzyme possesses less than 0.1% oxalate decarboxylase activity Gelatoporia subvermispora ?
-
 ?
1.2.3.4 oxalate + O2 + 2 H+
-
 Gelatoporia subvermispora CO2 + 2 H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.3.4 ? x * 66000, SDS-PAGE Gelatoporia subvermispora
1.2.3.4 ? x * 45000, calculated from amino acid sequence Gelatoporia subvermispora

Synonyms

EC Number Synonyms Comment Organism
1.2.3.4 OxOx
-
 Gelatoporia subvermispora

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.3.4 4
-
-
 Gelatoporia subvermispora

pH Range

EC Number pH Minimum pH Maximum Comment 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 Comment 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

Expression

EC Number Organism Comment Expression
1.2.3.4 Gelatoporia subvermispora expression is induced by methanol up