1.2.3.4: oxalate oxidase
This is an abbreviated version!
For detailed information about oxalate oxidase, go to the full flat file.
Word Map on EC 1.2.3.4
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1.2.3.4
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wheat
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barley
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sclerotinia
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apoplastic
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powdery
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mildew
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pathogenesis-related
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sclerotiorum
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graminis
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hyperoxaluria
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blumeria
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hordei
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erysiphe
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nodorum
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bicupins
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dentata
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castanea
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oxalate-degrading
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berk
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alkylamine
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septoria
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medicine
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analysis
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industry
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synthesis
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agriculture
- 1.2.3.4
- wheat
- barley
- sclerotinia
- apoplastic
-
powdery
- mildew
-
pathogenesis-related
- sclerotiorum
- graminis
- hyperoxaluria
- blumeria
-
hordei
- erysiphe
- nodorum
-
bicupins
- dentata
-
castanea
-
oxalate-degrading
-
berk
- alkylamine
- septoria
- medicine
- analysis
- industry
- synthesis
- agriculture
Reaction
Synonyms
aero-oxalo dehydrogenase, Germin, Germin GF-2.8, Germin GF-3.8, germin-like oxidase, germin-like protein, gl-OXO, glp1, GLP2, HvOxo1, oxalate oxidase, oxalate oxidase GF-2.8, oxalate: O2 oxidoreductase, oxalate:oxygen oxidoreductase, oxalic acid oxidase, OXO, OXO-G, OXO1, OXO2, OXO3, OXO4, OxOx, TaOxo1, TaOxo2
ECTree
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Inhibitors
Inhibitors on EC 1.2.3.4 - oxalate oxidase
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Fe(NO3)2
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1 mM concentration 98% inhibition; Fe(NO3)2 + EDTA 1 mM concentration 96% inhibition
ferrous acetate
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94% inhibition at 0.01 mM concentration; ferrous acetate + EDTA 96% inhibition at 0.01 mM concentration
glyoxylate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
H2O2
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hydrogen peroxide is both a reversible noncompetitive inhibitor of the OxOx catalyzed oxidation of oxalate and an irreversible inactivator. The build-up of the turnover-generated hydrogen peroxide product leads to the inactivation of the enzyme. The introduction of catalase to reaction mixtures protects the enzyme from inactivation allowing reactions to proceed to completion. No changes in global protein structure take place in the presence of hydrogen peroxide
lignosulfonate
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at a lignosulfonate concentration of 50 mg/ml and a pH of 3.8, 2-16% of the activity of oxalate oxidase remain
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malate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
malonate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
SDS
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isoforms OxO1-4, are very sensitive to 0.1% SDS with a nearly total loss of their enzyme activities
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wild type and immobilized 88% and 81% inhibition respectively
ascorbate
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ascorbate causes 80% inhibition in the activity of immobilized enzyme
glycolate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
NaCl
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at 1 mM concentration 43% activity retained by free protein, 85% activity retained by immobilized protein
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1 mM concentration 15% inhibition of the free enzyme, not of the immobilized enzyme
pyruvate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
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1 mM concentration, 10% inhibition of the free enzyme, not of the immobilized enzyme
additional information
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the enzyme does not show substrate inhibition up to a oxalate concentration of 50 mM
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additional information
for wild type oxalate oxidase, glycolate does not serve as a substrate and does not significantly inhibit turnover when included in the assay at equimolar (20mM) concentrations of oxalate
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additional information
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the presence of either superoxide dismutase or manganese catalase in the assay mixture dramatically accelerates turnover inactivation and resultes in a vanishingly small Vs value in the steady state
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additional information
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acetone precipitation has no influence on the activity of barley oxalate oxidase
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