Information on EC 1.2.3.4 - oxalate oxidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.2.3.4
-
RECOMMENDED NAME
GeneOntology No.
oxalate oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
oxalate + O2 + 2 H+ = 2 CO2 + H2O2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
oxalate degradation IV
-
-
Glyoxylate and dicarboxylate metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
oxalate:oxygen oxidoreductase
Contains Mn2+ as a cofactor. The enzyme is not a flavoprotein as had been thought [3].
CAS REGISTRY NUMBER
COMMENTARY hide
9031-79-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
oat, with freshly sliced oat radicles little oxalate degradation is oberserved
-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
strain FP-10572
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
banana
-
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Manually annotated by BRENDA team
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
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-
Manually annotated by BRENDA team
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
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Manually annotated by BRENDA team
strain OX-53
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Manually annotated by BRENDA team
strain OX-53
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Manually annotated by BRENDA team
commercial blend
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-
Manually annotated by BRENDA team
Sorghum sp.
Sorghum sp. CSH-5
strain CSH-5
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-
Manually annotated by BRENDA team
commercial blend, freshly sliced spelt radicles are less effective in oxalate degradation than rye radicles
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
DL-malic acid + O2
?
show the reaction diagram
glyoxylic acid + O2 + 2 H+
CO2 + formaldehyde + H2O2
show the reaction diagram
maleic acid + O2
?
show the reaction diagram
oxalate + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
oxalate + O2 + 2 H+
CO2 + 2 H2O2
show the reaction diagram
-
-
-
-
?
oxalate + O2 + H+
CO2 + H2O2
show the reaction diagram
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
oxalate + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
oxalate + O2 + 2 H+
CO2 + 2 H2O2
show the reaction diagram
-
-
-
-
?
oxalate + O2 + H+
CO2 + H2O2
show the reaction diagram
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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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 hide
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
Ca2+
-
stimulates activity
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.
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
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
8-hydroxyquinoline
acetate
-
competitive inhibition
alpha,alpha'-dipyridyl
arsenite
ascorbate
azide
Cl-
-
1 M concentration 75% inhibition
CuSO4
cyanide
diethyldithiocarbamate
Dithionite
dithiothreitol
-
-
Fe(NO3)2
-
1 mM concentration 98% inhibition; Fe(NO3)2 + EDTA 1 mM concentration 96% inhibition
Fe3+
-
10 mM concentration 35% inhibition
ferrous acetate
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94% inhibition at 0.01 mM concentration; ferrous acetate + EDTA 96% inhibition at 0.01 mM concentration
FeSO4
-
-
fluoride
glutathione
glycolate
glyoxylate
-
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
H3PO4
-
76.9% residual activity at 0.1 mM
Hg2+
-
mM concentration
HgCl2
-
0.1 mM 36% inhibition
hydroxylamine
-
0.1 mM concentration 100% inhibition
iodacetamide
-
0.1 mM concentration 62% inhibition
Iodide
iodoacetate
K+
-
94% residual activity at 1 mM
KBr
-
1 mM concentration 58% inhibition
KCl
-
14% inhibition at 1 mM concentration
KCN
-
41% activity retained at 5 mM concentration
KI
-
1 mM concentration 94% inhibition
KNO3
-
-
L-cysteine
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
-
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
N-ethylmaleimide
Na2SO4
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48.4% residual activity at 0.1 mM
NaNO3
-
-
NEM
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92% residual activity at 1 mM
NH4NO3
-
-
nitrate
nitrite
o-phenanthroline
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0.1 mM concentration 26% inhibition
oxalate
-
substrate inhibition
oxaloacetic acid
-
-
Pb2+
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2 mM concentration 57% inhibition, 20 mM concentration 89% inhibition
pyruvate
salicylate
-
-
SDS
-
isoforms OxO1-4, are very sensitive to 0.1% SDS with a nearly total loss of their enzyme activities
Semicarbazide
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0.1 mM concentration 57% inhibition
Sodium azide
-
86% residual activity at 1 mM
Sodium molybdate
-
71% residual activity at 1 mM
Sodium nitrate
-
45% residual activity at 1 mM
sodium thiocyanate
-
72% residual activity at 1 mM
SrCl2
Sorghum sp.
-
slight inhibition at 0.5 mM concentration
succinate
-
competitive inhibition
ZnSO4
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8-hydroxyquinoline
-
0.4 mM concentration 400% activation
arsenite
-
5 mM concentration slight activation
Ca(CH3COO)2
-
mM concentration 71% activation
Cu(CH3COO)2
-
0.1 mM concentration 20% activation
CuSO4
Sorghum sp.
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0.5 mM concentration 200% activation
cyanide
-
5 mM concentration slight activation
D-fructose 1,6-bisphosphate
-
-
D-fructose 6-phosphate
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D-glucose 6-phosphate
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diethyldithiocarbamate
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35% increase of activity at 1 mM
DW 1750000
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21% increase of activity at 1 mM
FeSO4
Sorghum sp.
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0.5 mM concentration 42% activation
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
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1 mM concentration, 10% activation free protein, 18% activation immobilized protein
hippuric acid
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1 mM concentration, 10% activation free protein, 8% activation immobilized protein
hydroquinone
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0.1 mM concentration 123% activation
MnSO4
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0.1 mM concentration 75% activation
NAD+
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16.6% stimulation of activity at 0.5 mM FAD
o-phenylenediamine
-
0.1 mM concentration 505% activation
Pb(CH3COO)2
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1 mM concentration 157% activation
phenylhydrazine
-
0.1 mM concentration 280% activation
riboflavin
serine
-
1 mM concentration, 12% activation free protein, 10% activation immobilized protein
Sodium periodate
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the oxalate oxidase activity of the recombinant enzyme is 7fold increased by treatment with sodium periodate
Urea
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physiological concentration, 8% activation free protein
uric acid
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1 mM concentration, 12% activation free protein, 8% activation immobilized protein
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015 - 14.9
oxalate
0.024 - 9.5
oxalic acid
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.7 - 85
oxalate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13.3
oxalate
-
succinate buffer, at pH 4.0 and 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.9
acetate
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in citrate buffer, at pH 4.0 and 22°C
28
glycolate
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in citrate buffer, at pH 4.0 and 22°C
15
glyoxylate
-
in citrate buffer, at pH 4.0 and 22°C
52
malate
-
in citrate buffer, at pH 4.0 and 22°C
3
malonate
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in citrate buffer, at pH 4.0 and 22°C
0.00058
nitric oxide
-
at pH 4.0 and 25°C
17
pyruvate
-
in citrate buffer, at pH 4.0 and 22°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1023 - 2446
oxalate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000002
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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
0.39
Sorghum sp.
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H2O2 production
0.4
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crude extract, in citrate buffer, at pH 4.0 and 22°C
1.3
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oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 10 mM Al2O3
1.6
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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
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oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 20 mM Al2O3
2.4
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crude enzyme, at pH 3.5 and 40°C
2.8
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oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 20 mM ZnO
2.9
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oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 10 mM MnO2
3.4
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oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 30 mM ZnO
4.2
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oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 20 mM CuFe2O4Zn
4.5
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oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 20 mM MnO2
5.2
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oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 30 mM CuFe2O4Zn
5.75
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purified recombinant and wild type enzyme
5.9
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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
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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
10.4
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H2O2 production
12.7
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after 32fold purification, in citrate buffer, at pH 4.0 and 22°C
21.9
-
native wild type oxalate oxidase
26.3
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after 11.1fold purification, at pH 3.5 and 40°C
34
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H2O2 production
94
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native S49A oxalate oxidase
139
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periodate-oxidized oxalate oxidase, Mn5+ content 100%
156
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ascorbate-reduced oxalate oxidase, Mn3+ content above 95%
630
-
O2 consumption
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
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isoform OXO3, in succinic acid-NaOH buffer
4 - 4.5
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maximum activity, in situ at 25°C with a oxalate solution
5.2
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crude extract
8.5
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isoforms OXO1 and OXO4, in Tris-HCl buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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 - 4.5
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20% activity at pH 2.0 and 4.5
2.5 - 4.5
2.5 - 6
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the catalytic efficiency (Vmax/Km) increases continuously to lower pH
3.5 - 5.5
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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 - 7
Sorghum sp.
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50% activity at pH 4.0 and 7.0
4.5 - 7
-
approx. 50% of maximal activity at pH 5.0 and pH 7.0, respectively, polyvinyl alcohol membrane immobilized oxalate oxidase
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18 - 35
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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
30
-
polyvinyl alcohol membrane immobilized oxalate oxidase
30 - 60
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in situ in an oxalate solution
additional information
-
activation energy 5.084 kcal/mol
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 55
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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
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in situ in an oxalate solution at different time intervals of incubation
25 - 50
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50% activity at 25°C and 50°C
30 - 80
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more than 50% activity between 30 and 70°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
root border cells (RBC)
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
-
alpha5, 5 * 25000, SDS-PAGE
38000
-
alpha8, 8 * 38000, SDS-PAGE
45000
-
x * 45000, calculated from amino acid sequence
49800
-
C isoform, calculated from protein sequence
56000
-
G isoform, SDS-PAGE
65000
-
alpha2, 2 * 65000, SDS-PAGE
65500
-
alpha6, 6 * 65500, SDS-PAGE
66000
-
x * 66000, SDS-PAGE
95000
-
gene HvOxOb, SDS-PAGE
100000
-
gene HvOxOa, SDS-PAGE
120200
Sorghum sp.
-
gel filtration
124000
-
gel filtration
125000
-
migrates as an oligomer, most likely a hexamer in a 12.5% gel using SDS-PAGE
130000
-
gel filtration
140000
-
gel filtration
222700
-
isoform OXO3, gel filtration
235100
-
isoform OXO1, gel filtration
287000
-
isoform OXO2, gel filtration
295700
-
isoform OXO4, gel filtration
320000
-
gel filtration
400000
-
gel filtration
additional information
-
the molecular weight is not affected by NaCl stress
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
homodimer
-
2 * 62000, SDS-PAGE
homooctamer
-
8 * 24000, isoform OXO3, calculated from amino acid sequence; 8 * 27100, isoform OXO3, SDS-PAGE
octamer
oligomer
-
migrates as an oligomer, most likly a hexamer
pentamer
-
alpha5, 5 * 25000, SDS-PAGE
additional information
-
NaCl stress does not affect the number of subunits of the enzyme
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
additional information
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
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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
in complex with Mn2+ and N3O-donor aminocarboxylate ligands
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 6
Sorghum sp.
-
-
288393
5.5 - 7
-
-
288392
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 80
-
the enzyme is highly stable at 4-80°C for 6 h
50
-
after 10 min 100% activity
80
-
30 min
89
-
after 3 min 49% activity
additional information
-
thermally extremely stable
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 alkylamine glass
-
immobilized on PEG1900 and PEG5000
-
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
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
by treatment with K3Fe(CN)6 decreases activity, desalting restores initial activity
-
288378
resistant against Na2IrCl6
-
288378
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-180°C, several months, no activity loss
-
-20°C, potassium phosphate buffer pH 6.5, 6 months, no activity loss
-
0-4°C, 30 days, 50% activity retained
Sorghum sp.
-
4-8°C, 90 days, native enzyme, up to 70% loss of activity
-
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
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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
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, column chromatography, and gel filtration
-
ammonium sulfate precipitation, DEAE-Sephacel column chromatography, and Sephadex G-100 gel filtration
-
ammonium sulfate, Sephadex G-200, DEAE-Sephacel
-
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-Sephacel column chromatography and Sephadex G-100 gel filtration
-
DEAE-Sepharose column chromatography and butyl Sepharose column chromatography
-
DEAE-Sepharose column chromatography, and Sephadex G-25 gel filtration
-
mutant proteins
partially purified
-
Sephadex G-25 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Arabidopsis thaliana
-
expressed in Brassica napus
-
expressed in Brassica napus cultivar 84039M, the expression leads to considerably increased OXO activity and enhanced resistance to Sclerotinia sclerotiorum
-
expressed in Castanea dentata
-
expressed in cultured BY-2 cells of tobacco
-
expressed in Escherichia coli BL21
-
expressed in Pichia pastoris
-
expressed in Pichia pastoris strain X-33
-
expressed in Pichia pastoris strain X33
-
expressed in Pichia pastoris X33
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expressed in Zea mays, expression in Zea mays leads to increased resistance against Ostrinia nubilalis
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expression of cDNA in Escherichia coli
expression of OXO in sunflower
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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
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mutant enzymes are expressed in Escherichia coli BL21(DE3) cells
-
recombinant barley oxalate oxidase expressed in Pichia pastoris (X33)
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the mutant proteins expressed in Picha pastoris
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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expression is induced by methanol
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E216Q
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mutant exhibits a 200fold loss in decarboxylase activity and a 10fold increase in oxalate oxidase activity
A242E
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the mutant shows 5% of the wild type oxidase activity
D241A
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the mutant contains 17% of the Mn2+ content of the recombinant wild type enzyme and 7% of the wild type oxidase activity
N75A
reduced activity to 2.4% of the wild type level
N85A
reduced activity to 0.5% of the wild type level
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
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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