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Enzyme Nomenclature
Information on EC 1.2.3.4 - oxalate oxidase
Word Map on EC 1.2.3.4
- 1.2.3.4
- wheat
- barley
- sclerotinia
- graminis
- sclerotiorum
-
powdery
- mildew
- blumeria
- alkylamine
- septoria
- medicine
-
erysiphe
-
bicupins
- subvermispora
-
berk
- nodorum
- hyperoxaluria
-
ceriporiopsis
- calluses
- industry
- agriculture
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.2.3.4
-
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RECOMMENDED NAME
GeneOntology No.
oxalate oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
oxalate + O2 + 2 H+ = 2 CO2 + H2O2
-
-
-
-
oxalate + O2 + 2 H+ = 2 CO2 + H2O2
The computer model supports the following reaction mechanism: The Oxo-Mn(2)-oxalate complex exists as a mixture of five-and six-coordinate species. The form with coordinatively unsaturated Mn(2) site reacts with dioxygen on the quartet potential energy surface. In this step, the proton from oxalate monoanion is transferred to dioxygen through the first-shell glutamate. The proton-transfer triggers the C-C bond cleavage, and the electron follows the proton. Simultaneously, the second electron, necessary to produce the peroxo species, is provided by manganese. This step, which is also rate-limiting, yields the first CO2 molecule and the reactive intermediate in which the formyl radical anion coordinates the high-spin Mn(3). The quartet to sextet spin transition, which involves a small apparent barrier, allows for the formyl radical -> Mn(3) electron transfer. This step leads to the product-active site complex, which upon protonation decays to H2O2, CO2, and the active site is then ready to begin the next catalytic cycle
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
oxalate:oxygen oxidoreductase
Contains Mn2+ as a cofactor. The enzyme is not a flavoprotein as had been thought [3].
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CAS REGISTRY NUMBER
COMMENTARY
9031-79-2
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
oat, with freshly sliced oat radicles little oxalate degradation is oberserved
-
-
cultivars PI 255956, PI 535278 (Tars-046A) and cv. Wolven Pole, oxalate concentration in infected (infected with Sclerotinia sclerotiorum) stems of Wolven Pole is higher than in PI 255956 and PI535278. Inoculated stems of Wolven Pole have oxalate oxidase, the Sclerotinia sclerotorum resistent lines PI 255959 and PI 535278 not. Phaseolus coccineus is not as oxalat sensitiv as Phaseolus vulgaris. Infection of Phaseolus coccineus with Sclerotinia scerotorum increased the levels of oxalate, with the highest concentration in Woven Pole
-
-
cvs. Huron (navy), Othello (pinto) and Newport (navy), Phaseolus vulgaris is more oxalate sensitive than Phaseolus coccineus, with Othello being the most sensitive, Huron the most tolerant, and Newport intermediate. Huron is more resistant to Sclerotinia sclerotiorum than the other two cultivars
-
-
Sorghum sp.
commercial blend, freshly sliced spelt radicles are less effective in oxalate degradation than rye radicles
-
-
-
-
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barley, var. Alpaca, freshly sliced barley radicles are less effective in oxalate degradation than rye radicles
-
-
transgenic potato plantlets expressing the barley oxalate oxidase enzyme, show a relatively higher salinity tolerance than the non-transgenic genotypes in vitro, but in the glasshouse the results are less consistent
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wheat, var.Zentos, freshly sliced wheat radicles are less effective in oxalate degradation than rye radicles
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-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the enzyme is capable of stimulating the ester-linked diferulic acid formation. The enzyme is capable of modifying the metabolism of ester-linked ferulates in cell walls of wheat shoots by promoting the peroxidase action via supply of hydrogen peroxide
physiological function
physiological function
-
the enzyme is involved in the senescence of coleoptiles in rice by catalyzing the oxidation of oxalate
physiological function
-
transgenic Arabidopsis lines that express the enzyme exhibit enhanced resistance to oxalate exposure and Sclerotinia sclerotiorum infection
physiological function
-
the enzyme is not a disease resistance factor in rice. since transgenic rice plants with substantially higher enzyme activity are not more resistant to rice blast and bacterial blight than the wild type
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
oxalate + O2 + 2 H+
2 CO2 + H2O2
-
the substrate affinity and max. activity of oxalate oxidase from NaCl stressed seedlings was adversely affected
-
-
?
oxalate + O2 + H+
CO2 + H2O2
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partially purified enzyme shows highest activity with 0.8 mM oxalate
-
-
?
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
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-
-
-
ir
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
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role in the response of barley to the powdery mildew fungus
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-
ir
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
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role in plant signaling and defense
-
-
ir
additional information
?
-
-
the recombinant enzyme possesses less than 0.1% oxalate decarboxylase activity
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-
-
additional information
?
-
-
model for signal transduction pathway for the regulation of the hypersensitive response is proposed in which oxalate oxidase plays a central role
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-
-
additional information
?
-
glycolate does not serve as a substrate
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-
-
additional information
?
-
-
no detectable activity against other related organic acids including citrate, glyoxylate, malonate, succinate, glutarate, malate, glycolate, acetate, lactate and formate
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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
oxalate + O2 + H+
CO2 + H2O2
-
partially purified enzyme shows highest activity with 0.8 mM oxalate
-
-
?
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
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role in the response of barley to the powdery mildew fungus
-
-
ir
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
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role in plant signaling and defense
-
-
ir
additional information
?
-
-
the recombinant enzyme possesses less than 0.1% oxalate decarboxylase activity
-
-
-
additional information
?
-
-
model for signal transduction pathway for the regulation of the hypersensitive response is proposed in which oxalate oxidase plays a central role
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
FMN, FAD, NAD+, and riboflavin at 1 mM in the presence of nanoparticles have practically no effect on native and immobilized enzymes
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
AlCl3
-
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+
-
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+
-
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
-
enzyme activity of the C isoform is lost in the presence of sodium dodecyl sulfate
Zn2+
additional information
Mg2+
-
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+
-
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
-
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
-
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
-
not activated by Mg2+, Co2+, Zn2+, Ni2+, and Fe2+
additional information
-
the enzymatic activity is not influenced by K+, Na+, Zn2+, Fe3+, Mn2+, and Mg2+
additional information
-
Na2SO4, EDTA-Na2, KCl, NaCl, K2CO3, Na2CO3, Na2HPO4 and NaH2PO4 have no significant effect on the enzyme activities
additional information
-
the immobilized oxalate oxidase shows no increase in activity in the presence of 10 mM K+ or Na+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Fe(NO3)2
-
1 mM concentration 98% inhibition; Fe(NO3)2 + EDTA 1 mM concentration 96% inhibition
ferrous acetate
-
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
lignosulfonate
-
at a lignosulfonate concentration of 50 mg/ml and a pH of 3.8, 2-16% of the activity of oxalate oxidase remain
-
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
-
isoforms OxO1-4, are very sensitive to 0.1% SDS with a nearly total loss of their enzyme activities
ascorbate
-
wild type and immobilized 88% and 81% inhibition respectively
ascorbate
-
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
-
at 1 mM concentration 43% activity retained by free protein, 85% activity retained by immobilized protein
pyruvate
-
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
ZnSO4
-
1 mM concentration, 10% inhibition of the free enzyme, not of the immobilized enzyme
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
-
additional information
-
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
-
acetone precipitation has no influence on the activity of barley oxalate oxidase
-
additional information
-
the enzyme does not show substrate inhibition up to a oxalate concentration of 50 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Formamide
specific activity of the wild type oxalate oxidase is slightly higher when 1 M formamide is added
glucose
-
physiological concentration, 20% activation free protein, 25% activation immobilized protein
glycine
-
1 mM concentration, 10% activation free protein, 18% activation immobilized protein
hippuric acid
-
1 mM concentration, 10% activation free protein, 8% activation immobilized protein
serine
-
1 mM concentration, 12% activation free protein, 10% activation immobilized protein
Sodium periodate
-
the oxalate oxidase activity of the recombinant enzyme is 7fold increased by treatment with sodium periodate
uric acid
-
1 mM concentration, 12% activation free protein, 8% activation immobilized protein
Cu2+
-
0.5 mM concentration 95% activation; Cu2+ + alpha,alpha'-dipyridyl 0.5 mM 120% activation; Cu2+ + diethyldithiocarbamate 0.5 mM 130% activation
Cu2+
Sorghum sp.
-
0.5 mM concentration 200% activation; Cu2+ + 8-hydroxyquinoline 0.5 mM 100% activation; Cu2+ + diethyldithiocarbamate 0.5 mM 60% activation
Cu2+
Sorghum sp.
-
Cu2+ + 2-mercaptoethanol 0.5 mM 62% activation; Cu2+ + 8-hydroxyquinoline 0.5 mM 100% activation; Cu2+ + diethyldithiocarbamate 0.5 mM 60% activation; Cu2+ + FAD 0.5 mM 250% activation; Cu2+ + FMN 0.5 mM 280% activation; Cu2+ + L-cysteine 0.5 mM 46% activation
FAD
-
55.5% stimulation of activity at 0.5 mM; 55.5% stimulation of activity at 0.5 mM FAD
additional information
-
compared to free enzyme, MnO2 nanoparticles(NP)-bound enzyme shows improved activity (35% stimulation at 2.5 mg/ml) while ZnO NPs- and CuO NPs-bound enzymes have no substantial improvement
-
additional information
-
the enzymatic activity is not influenced by D-glucose, urea, and lactate
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.78
oxalate
-
oxalate oxidase activity is measured by oxygen uptake assay with a Clark oxygen electrode in a thermostated cell (25°C). The Km evalutated from initial velocity data exhibits a strong pH dependence with limiting slopes (versus pH) of 0.9 (below pH 4) and 1.5 (above pH 4)
0.8
oxalate
-
wild type enzyme, pH and temperature not specified in the publication
1.1
oxalate
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mutant enzyme D241A, pH and temperature not specified in the publication
2
oxalate
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mutant enzyme A242E, pH and temperature not specified in the publication
6.23
oxalate
-
30°C, pH 6.5, polyvinyl alcohol membrane immobilized oxalate oxidase
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9.7
oxalate
-
oxalate oxidase activity is measured by oxygen uptake assay with a Clark oxygen electrode in a thermostated cell (25°C)
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000002
-
gl-OXO activity in homogenates of embryos 12 days after fertilisation
0.055
asparagine mutant (N85A), thermostated (25°C) Clark oxygen electrode calibrated with the protocatechuic acid/protocatechuate dioxygenase reaction, pH 4, specific activity is higher in the presence of 1 M NH4Cl or 1 M NaCl and slightly lower when 1 M formamide is added
0.24
asparagine mutant (N75A),thermostated (25°C) Clark oxygen electrode calibrated with the protocatechuic acid/protocatechuate dioxygenase reaction, pH 4, specific activity is slightly higher in the presence of 1 M NH4Cl or 1 M NaCl and does not change when 1 M formamide is added
1.3
-
oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 10 mM Al2O3
1.6
-
oxalate oxidase activity after 14 days of cultivation, control, without metal oxide; oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 10 mM CuFe2O4Zn; oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 30 mM Al2O3
1.8
-
oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 20 mM Al2O3
2.3
2.8
-
oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 20 mM ZnO
2.9
-
oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 10 mM MnO2
2.98
3.4
-
oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 30 mM ZnO
4.2
-
oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 20 mM CuFe2O4Zn
4.5
-
oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 20 mM MnO2
5.2
-
oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 30 mM CuFe2O4Zn
5.9
-
oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 10 mM Cu2O; oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 20 mM Cu2O
6.4
-
oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 30 mM MnO2
10.26
wild type, thermostated (25°C) Clark oxygen electrode calibrated with the protocatechuic acid/protocatechuate dioxygenase reaction, pH 4
12.7
-
after 32fold purification, in citrate buffer, at pH 4.0 and 22°C
additional information
2.3
-
oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 10 mM ZnO
6
-
oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 30 mM Cu2O
additional information
-
the effect of the isotopic composition of the solvent is investigated by assaying oxalate oxidase in buffer prepared form H2O/D20 mixtures.The limiting values of Vs (steady state rate) lead to an estimate of the overall solvent kinetic isotope effect kH2O/kD2O = 8.5 (k=burst rate constant); Vimax (initial maximum velocity) is nearly independent of pH over the range from pH 3 to 5
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.2
3.5
3.8
4.5
5.8
6.5
4
-
in situ, max. rate of oxalate degradation in the liquid phase of a spinach (commercial frozen) preparation, the max. rate of oxalate degradation in spinach suspension and the solid phase is reached at pH 3.5
6.5
-
the immobilized enzyme shows maximum activity at pH 6.5 when incubated at 40°C for 15 min
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 3
-
100% activity at pH 2.0, 50% activity at pH 3.0, 10% activity at pH 3.5, no activity at pH 4.0
2.5 - 4.5
2.5 - 6
-
the catalytic efficiency (Vmax/Km) increases continuously to lower pH
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
4.5 - 7
-
approx. 50% of maximal activity at pH 5.0 and pH 7.0, respectively, polyvinyl alcohol membrane immobilized oxalate oxidase
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18 - 35
-
in situ, max. rate of oxalate degradation in the liquid phase of a spinach (commercial frozen) preparation, the rate of oxalate degradation in spinach suspension and the solid phase is lower. In fresh spinach (without any heat treatment) little oxalate degradation occurs
35
37
40
45
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 55
-
in situ, max. oxalate degradation in the liquid phase of a spinach (commercial frozen) preparation, the rate of oxalate degradation in spinach suspension and the solid phase is lower. In fresh spinach (without any heat treatment) little oxalate degradation occurs
20 - 70
-
in situ in an oxalate solution at different time intervals of incubation
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
after 24 h of induction on auxin-containing medium gl-OXO activity is readily detectable within the embryo, particularly within the coleorhiza and on the residual cells of the suspensor
-
When embryos are cultured together with endosperms (endosperm-supported culture, ES), the percentage of callus induction is significantly lower than that when embryos are cultured in the absence of endosperm (non-endosperm-supported culture, NES). The activity of oxalate oxsidase in the callus of ES culture is higher than that in the callus of NES culture, suggesting that the activity of oxalate oxidase may be a parameter for selection of calli with potential for plantlet regeneration
-
fresh or heat dried (55°C for 16 h, with T increased in 5°C steps to reach 75°C) radicles are used. Heat drying reduces the rate of oxalate degradation activity by approximately half. Deep-freezing the radicles to -20°C does not lead to any loss of oxalate degradation activity within 4 weeks of storage
-
different developmental stages were examined (complete seedling with radicles) with the oxalate degradation rate being similarly high for 4-8-old seedlings
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26000
62000
125000
-
migrates as an oligomer, most likely a hexamer in a 12.5% gel using SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
homodecamer
-
10 * 24100, isoform OXO1, calculated from amino acid sequence; 10 * 24200, isoform OXO4, calculated from amino acid sequence; 10 * 24300, isoform OXO2, calculated from amino acid sequence; 10 * 25900, isoform OXO1, SDS-PAGE; 10 * 27200, isoform OXO2, SDS-PAGE; 10 * 27400, isoform OXO4, SDS-PAGE
homooctamer
-
8 * 24000, isoform OXO3, calculated from amino acid sequence; 8 * 27100, isoform OXO3, SDS-PAGE
octamer
additional information
-
NaCl stress does not affect the number of subunits of the enzyme
?
-
x * 45000, calculated from amino acid sequence; x * 66000, SDS-PAGE
dimer
Sorghum sp. CSH-5
-
alpha2, 2 * 62000, SDS-PAGE
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
additional information
glycoprotein
-
carbohydrates make up approximately 30% of the enzyme’s mass
additional information
-
2 potential N-glycosylation sites, only one of them is probably glycosylated
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method solution in 50 mM Tris/HCl, pH 8.5, containing 500 mM NaCl with 4.5% (w/v) PEG 2000
-
hanging-drop vapor diffusion method at 18 °C using 1 micro l of protein (10-15 mg/ml) plus 1 micro l reservoir drops an 1-ml reservoirs, native crystals grown from 2.3M (NH4)2SO4 and 5% 2-propanol are rhombohedral, crystals of recombinant protein, grown from 10% polyethylene glycol 4000 and 0.1 M NaAc, pH 4.6, are tetragonal, Asn75-> Ala OXO are grown from 20% 2-propanol, 0.1 M NaAc, pH 4.6, 0.2 M CaCl2, can be cryo-cooled directly and are rhombohedral
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 6
Sorghum sp.
-
-
288393
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
70
75
60
-
after 10 min wild type 30% activity, immobilized on PEG1900 55% activity and immobilized on PEG5000 70% activity
70
-
metal oxide nanoparticles(NP)-bound enzyme retains more activity when subjected to thermal treatment at 70°C for 30 min., retention of activity in the increasing order being 54%, 65%, 76%, and 87% for native, ZnO NPs-, CuO NPs-, and MnO2 NPs-bound enzyme, respectively
70
-
isoforms OxO2 and OxO3 still maintain all their activities after being heated at 70°C for 1 h while isoforms OxO1 and OxO4 lose about 30% of their activities
75
-
after 30 min wild type 60% activity, immobilized protein 27% activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
after 90 min treatment with trypsin 10% activity retained by free protein, 35% activity retained by immobilized protein on PEG1900 and 30% activity retained by immobilized protein on PEG5000
-
based on the absoption changes at 325 nm, it is possible to estimate the half-life of the Mn5+ species at room temperature: t1/2 = 42 h (pH 4) or 95 h (pH 7)
-
enzyme activity of the C isoform is lost in the presence of sodium dodecyl sulfate (SDS)
-
immobilized on zirkonia coated alkylamine glass, retains 97% of enzyme activity
-
isoforms OxO1-4 are resistant to a treatment with pepsin at 37°C for 30 min at pH 2.0, while the activity of isoform OxO4 is actually increased on pepsin treatment
-
the immobilized enzyme on modified mica chip retains 65.35% of the specific activity of free enzyme
-
the polyvinyl chloride-immobilized enzyme retains 65% of specific activity of free enzyme
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
by treatment with K3Fe(CN)6 decreases activity, desalting restores initial activity
-
288378
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 0.05 M sodium phosphate buffer (pH 6.5), 100 days, the immobilized oxalate oxidase loses 15% of its initial activity-free oxalate oxidase after 150 uses
-
4°C, 20 days, free protein, complete loss of activity, immobilized protein on PEG1900, 60% activity retained and immobilized protein on PEG5000, 35% activity retained
-
4°C, 3 months, distilled water, free protein, complete loss of activity, immobilized protein, 70% of activity retained
-
4°C, under 3 months no loss of activity by free protein, over 2 years immobilized protein
-
8°C, several months, no activity loss, conversion in 4 months to 23 kDa protein, loss of carbohydrate
-
room temperature, immobilized oxalate oxidase between folds of filter paper, 30 d, 50% loss of activity
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-Sephacel column chromatography, and Sephadex G-100 gel filtration
-
anion exchange chromatography, pH precipitation, phosphocellulose chromatography, gel filtration
-
anion exchange column chromatography and butyl Sepharose column chromatography
-
concanavalin A affinity chromatography, carboxymethyl-Sepharose column chromatography, and gel filtration
DEAE-Sepharose column chromatography and butyl Sepharose column chromatography
-
concanavalin A affinity chromatography, carboxymethyl-Sepharose column chromatography, and gel filtration
-
concanavalin A affinity chromatography, carboxymethyl-Sepharose column chromatography, and gel filtration
-
concanavalin A affinity chromatography, carboxymethyl-Sepharose column chromatography, and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Brassica napus cultivar 84039M, the expression leads to considerably increased OXO activity and enhanced resistance to Sclerotinia sclerotiorum
-
expressed in Zea mays, expression in Zea mays leads to increased resistance against Ostrinia nubilalis
-
expression of cDNA in Escherichia coli
into the pBI121 binary vector, the new construct pBI-OxO is transformed into Escherichia coli and then to Agrobacterium tumefaciens LBA4404, subsequently leaf discs of Nicotiana tabacum plants are transformed by culturing with Agrobacterium tumefaciens
-
transgenic potato plants (original potato plant = Solanum tuberosum L. cultivar Maris Brad and Desiree) expressing the oxalate oxidase enzyme are produced unsing Agrobacterium (Agrobacterium tumefaciens strain LBA4404)-mediated transformation
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme activity is very low at 96 h after imbibition, and then increases significantly with a maximum at 240 h
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E216Q
-
mutant exhibits a 200fold loss in decarboxylase activity and a 10fold increase in oxalate oxidase activity
D241A
-
the mutant contains 17% of the Mn2+ content of the recombinant wild type enzyme and 7% of the wild type oxidase activity
S49A
S49A
-
nonglycosylated oxalate oxidase is produced by site-directed mutagenesis (S49A)
S49A
-
the mutant retains essentially full enzyme activity but exhibits altered protein-protein interactions
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
overexpression of oxalate oxidase provides a new strategy for induction of antioxidative defense system against cellular ROS accumulation and for protection of crops from stress injury
industry
medicine
industry
-
oxalate oxidase is useful for oxalic acid removal in industrial bleaching plant filtrates
industry
-
the oxalate oxidase from Costus pictus is used as a cheap source of oxalate oxidase enzyme which is used in oxalate determination in biological fluids
industry
-
the enzyme is capable of removing oxalic acid from a variety of industrial bleaching filtrates
medicine
-
immobilized oxalate oxidase to determine oxalate concentration in urine for diagnosis of various forms of hyperoxaluria
medicine
-
colorimetric or UV-determination of oxalic acid in biological fluids and beverages
medicine
Sorghum sp.
-
immobilized oxalate oxidase to determine oxalate concentration in urine for diagnosis of various forms of hyperoxaluria
medicine
-
oxalate oxidase is immobilized onto arylamine glass beads affixed on the surface of a plastic strip and employed for oxalate determination in urine and serum samples
medicine
Sorghum sp. CSH-5
-
immobilized oxalate oxidase to determine oxalate concentration in urine for diagnosis of various forms of hyperoxaluria
-
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LINKS TO OTHER DATABASES (specific for EC-Number 1.2.3.4)
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