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
1.2.3.4 oxalate oxidaseAdvanced search results
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results (Metals Ions
Metals Ions on EC 1.2.3.4 - oxalate oxidase
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AlCl3
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the activity of oxalate oxidase and the production of H2O2 in the root border colls is higher in Al-treated root tips relative to those of the control plants
Cu2+
Fe2+
Mg2+
Mn2+
Mn3+
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treatment of the periodate-oxidized enzyme with ascorbate results in a substantioal decrease in absorption, forming a complex that is spectroscopically identified as a Mn3+ species. Mn3+ form has a 5fold higher specific activity than native recombinant oxalate oxidase.
Mn5+
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titration of oxalate oxidase with sodium periodate results in nearly stoichometric oxidation of the enzyme to an intensely colored yellow complex, whose complete spectroscopic characterization lead to assignment to a superoxidized Mn5+ complex. Treatment of Mn2+ S49A oxalate oxidase generates the same yellow species as the glycosylated wild type enzyme. Mass spectra of isolated and periodate-treated oxalate oxidase are virtually identical, demonstating that no protein oxidation occurred. Peroxidate oxidation increases the specific activity about 5fold.
NaCl
NH4Cl
specific activity of the wild type oxalate oxidase is lower in the presence of 1 M NaCl
SDS
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enzyme activity of the C isoform is lost in the presence of sodium dodecyl sulfate
Zn2+
additional information
Mg2+
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Soluble and active protein obtained only when the enzyme is coexpressed with the chaperones DnaK and DnaJ (G isoform) and when a manganese salt is added to the growth medium (C and G isoform)
Mn2+
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titration of periodate-oxidized oxalate oxidase with hydroxylamine completely eliminates the visible absorption, forming a homogeneous Mn2+ form of the enzyme. The fully reduced Mn2+ form lacks any detectable oxidase activity, reoxidation substantially restores the maximum activity.
NaCl
specific activity of the wild type oxalate oxidase is lower in the presence of 1 M NH4Cl
NaCl
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the specific activity of oxalate oxidase is increased in seedlings grown in a NaCl containing medium compared to normal, which reveals the increased de novo synthesis of the enzyme to sustain oxalate egradation
additional information
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the enzymatic activity is not influenced by K+, Na+, Zn2+, Fe3+, Mn2+, and Mg2+
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
additional information
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incubation of the apoenzyme with a 100fold molar excess of MgCl2, CoCl2, CuCl2, ZnCl2, NiCl2, FeCl2 or FeCl3, individually, does not influence enzymatic activity
additional information
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not activated by Mg2+, Co2+, Zn2+, Ni2+, and Fe2+
additional information
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Na2SO4, EDTA-Na2, KCl, NaCl, K2CO3, Na2CO3, Na2HPO4 and NaH2PO4 have no significant effect on the enzyme activities
additional information
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the immobilized oxalate oxidase shows no increase in activity in the presence of 10 mM K+ or Na+
