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Literature summary for 1.2.3.4 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
Search for more literature for 1.2.3.4

Cloned(Commentary)

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

Inhibitors

Inhibitors Comment Organism Structure
acetate competitive inhibition Gelatoporia subvermispora
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
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
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
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
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
succinate competitive inhibition Gelatoporia subvermispora

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.1
-
 oxalate in citrate buffer, at pH 4.0 and 22°C Gelatoporia subvermispora
1.5
-
 oxalate in succinate buffer, at pH 4.0 and 22°C Gelatoporia subvermispora
14.9
-
 oxalate in acetate buffer, at pH 4.0 and 22°C Gelatoporia subvermispora

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ contains between 0.1 and 0.4 mole Mn per mole enzyme Gelatoporia subvermispora
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]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45000
-
 x * 45000, calculated from amino acid sequence Gelatoporia subvermispora
66000
-
 x * 66000, SDS-PAGE Gelatoporia subvermispora

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Gelatoporia subvermispora the recombinant enzyme possesses less than 0.1% oxalate decarboxylase activity ?
-
 ?
oxalate + O2 + 2 H+ Gelatoporia subvermispora
-
 CO2 + 2 H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Gelatoporia subvermispora Q5ZH56
-
-

Posttranslational Modification

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

Purification (Commentary)

Purification (Comment) Organism
DEAE-Sepharose column chromatography and butyl Sepharose column chromatography Gelatoporia subvermispora

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.4
-
 crude extract, in citrate buffer, at pH 4.0 and 22°C Gelatoporia subvermispora
12.7
-
 after 32fold purification, in citrate buffer, at pH 4.0 and 22°C Gelatoporia subvermispora

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
OxOx
-
 Gelatoporia subvermispora

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4
-
-
 Gelatoporia subvermispora

pH Range

pH Minimum pH Maximum Comment Organism
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]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3
-
 malonate in citrate buffer, at pH 4.0 and 22°C Gelatoporia subvermispora
3.9
-
 acetate in citrate buffer, at pH 4.0 and 22°C Gelatoporia subvermispora
15
-
 glyoxylate in citrate buffer, at pH 4.0 and 22°C Gelatoporia subvermispora
17
-
 pyruvate in citrate buffer, at pH 4.0 and 22°C Gelatoporia subvermispora
28
-
 glycolate in citrate buffer, at pH 4.0 and 22°C Gelatoporia subvermispora
52
-
 malate in citrate buffer, at pH 4.0 and 22°C Gelatoporia subvermispora

Expression

Organism Comment Expression
Gelatoporia subvermispora expression is induced by methanol up