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
1.2.3.4
-
RECOMMENDED NAME
GeneOntology No.
oxalate oxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
oxalate + O2 + 2 H+ = 2 CO2 + H2O2
show the reaction diagram
-
-
-
-
oxalate + O2 + 2 H+ = 2 CO2 + H2O2
show the reaction diagram
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
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidation
-
-
oxidation
-
-
oxidation
-
-
oxidation
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
reduction
-
-
reduction
-
-
reduction
-
-
reduction
-
-
PATHWAY
KEGG Link
MetaCyc Link
Glyoxylate and dicarboxylate metabolism
-
oxalate degradation IV
-
SYSTEMATIC NAME
IUBMB Comments
oxalate:oxygen oxidoreductase
Contains Mn2+ as a cofactor. The enzyme is not a flavoprotein as had been thought [3].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aero-oxalo dehydrogenase
-
-
-
-
Germin
-
-
-
-
Germin
-
-
Germin
-
-
Germin
-
-
Germin
P15290
-
Germin GF-2.8
-
-
-
-
Germin GF-3.8
-
-
-
-
germin-like oxidase
-
-
HvOxo1
-
-
oxalate oxidase
-
-
oxalate oxidase
-
-
oxalate oxidase
-
-
oxalate oxidase
P15290
-
oxalate: O2 oxidoreductase
-
-
oxalate: O2 oxidoreductase
Hordeum vulgare BH393
-
-
-
oxalate:oxygen oxidoreductase
-
-
oxalic acid oxidase
-
-
-
-
OXO
P45850
-
OXO
Hordeum vulgare BH393
-
-
-
OXO-G
Q5ZH56
G-isoform
CAS REGISTRY NUMBER
COMMENTARY
9031-79-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
oat, with freshly sliced oat radicles little oxalate degradation is oberserved
-
-
Manually annotated by BRENDA team
ATCC 90466, oxalate oxidase allelic isoforms C and G
-
-
Manually annotated by BRENDA team
strain FP-10572
-
-
Manually annotated by BRENDA team
Ceriporiopsis subvermispora FP-10572
strain FP-10572
-
-
Manually annotated by BRENDA team
barley
UniProt
Manually annotated by BRENDA team
barley, var. Alpaca, freshly sliced barley radicles are less effective in oxalate degradation than rye radicles
-
-
Manually annotated by BRENDA team
computer model of the reaction mechanism
-
-
Manually annotated by BRENDA team
strain pallas, P-01, P-02
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
Hordeum vulgare BH393
-
-
-
Manually annotated by BRENDA team
banana
-
-
Manually annotated by BRENDA team
cultivar Xiangnuo 1
-
-
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
-
-
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
-
-
Manually annotated by BRENDA team
strain OX-53
-
-
Manually annotated by BRENDA team
Pseudomonas sp. OX-53
strain OX-53
-
-
Manually annotated by BRENDA team
commercial blend
-
-
Manually annotated by BRENDA team
hybrid, var CSH-14
-
-
Manually annotated by BRENDA team
line CSH-14
-
-
Manually annotated by BRENDA team
variant CSH-14
-
-
Manually annotated by BRENDA team
variant KH-105
-
-
Manually annotated by BRENDA team
Sorghum sp.
-
-
-
Manually annotated by BRENDA team
Sorghum sp.
strain CSH-5
-
-
Manually annotated by BRENDA team
Sorghum sp. CSH-5
strain CSH-5
-
-
Manually annotated by BRENDA team
common wheat
-
-
Manually annotated by BRENDA team
cultivar Daichino-Minori
-
-
Manually annotated by BRENDA team
wheat, var.Zentos, freshly sliced wheat radicles are less effective in oxalate degradation than rye radicles
-
-
Manually annotated by BRENDA team
commercial blend, freshly sliced spelt radicles are less effective in oxalate degradation than rye radicles
-
-
Manually annotated by BRENDA team
maize, with maize radicle negligble oxalate degradation is observed
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
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
-
the enzyme is involved in the senescence of coleoptiles in rice by catalyzing the oxidation of oxalate
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
DL-malic acid + O2
?
show the reaction diagram
Pseudomonas sp., Pseudomonas sp. OX-53
-
-
-
-
?
glyoxylic acid + O2 + 2 H+
CO2 + formaldehyde + H2O2
show the reaction diagram
Pseudomonas sp., Pseudomonas sp. OX-53
-
-
-
-
?
oxalate + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
-
-
-
-
?
oxalate + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
-
-
-
-
?
oxalate + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
-
-
-
-
?
oxalate + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
-
the substrate affinity and max. activity of oxalate oxidase from NaCl stressed seedlings was adversely affected
-
-
?
oxalate + O2 + 2 H+
CO2 + 2 H2O2
show the reaction diagram
-
-
-
-
?
oxalate + O2 + H+
CO2 + H2O2
show the reaction diagram
-
-
-
-
?
oxalate + O2 + H+
CO2 + H2O2
show the reaction diagram
-
-
-
-
?
oxalate + O2 + H+
CO2 + H2O2
show the reaction diagram
-
-
-
-
?
oxalate + O2 + H+
CO2 + H2O2
show the reaction diagram
-
-
-
-
?
oxalate + O2 + H+
CO2 + H2O2
show the reaction diagram
-
-
-
-
?
oxalate + O2 + H+
CO2 + H2O2
show the reaction diagram
-
-
-
-
?
oxalate + O2 + H+
CO2 + H2O2
show the reaction diagram
-
-
-
-
?
oxalate + O2 + H+
CO2 + H2O2
show the reaction diagram
-
partially purified enzyme shows highest activity with 0.8 mM oxalate
-
-
?
oxalate + O2 + H+
CO2 + H2O2
show the reaction diagram
Hordeum vulgare BH393
-
-
-
-
?
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
-
-
-
-
ir
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
-
-
-
-
?
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
-
-
-
-
?
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
-
-
-
-
?
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
-
-
-
-
ir
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
-
-
-
-
ir
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
-
-
-
-
ir
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
-
-
-
-
?
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
-
-
-
-
ir
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
Sorghum sp.
-
-
-
-
ir
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
-
-
-
-
ir
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
-
-
-
-
ir
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
-
-
-
-
ir
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
-
-
-
-
ir
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
P15290
-
-
-
?
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
P45850
-
-
-
?
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
Q5ZH56
-
-
-
?
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
-
role in the response of barley to the powdery mildew fungus
-
-
ir
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
-
role in plant signaling and defense
-
-
ir
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
Ceriporiopsis subvermispora FP-10572
-
-
-
-
ir
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
Pseudomonas sp. OX-53
-
-
-
-
ir
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
Sorghum sp. CSH-5
-
-
-
-
ir
maleic acid + O2
?
show the reaction diagram
Pseudomonas sp., Pseudomonas sp. OX-53
-
-
-
-
?
additional information
?
-
-
model for signal transduction pathway for the regulation of the hypersensitive response is proposed in which oxalate oxidase plays a central role
-
-
-
additional information
?
-
P45850
glycolate does not serve as a substrate
-
-
-
additional information
?
-
-
the recombinant enzyme possesses less than 0.1% oxalate decarboxylase activity
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
oxalate + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
-
-
-
-
?
oxalate + O2 + 2 H+
2 CO2 + H2O2
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
-
-
-
-
?
oxalate + O2 + H+
CO2 + H2O2
show the reaction diagram
-
-
-
-
?
oxalate + O2 + H+
CO2 + H2O2
show the reaction diagram
-
-
-
-
?
oxalate + O2 + H+
CO2 + H2O2
show the reaction diagram
-
-
-
-
?
oxalate + O2 + H+
CO2 + H2O2
show the reaction diagram
-
partially purified enzyme shows highest activity with 0.8 mM oxalate
-
-
?
oxalate + O2 + H+
CO2 + H2O2
show the reaction diagram
Hordeum vulgare BH393
-
-
-
-
?
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
-
role in the response of barley to the powdery mildew fungus
-
-
ir
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
show the reaction diagram
-
role in plant signaling and defense
-
-
ir
additional information
?
-
-
model for signal transduction pathway for the regulation of the hypersensitive response is proposed in which oxalate oxidase plays a central role
-
-
-
additional information
?
-
-
the recombinant enzyme possesses less than 0.1% oxalate decarboxylase activity
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
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
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
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+
-
0.015 g per mol protein
Cu2+
-
0.04 atoms per monomer
Cu2+
Sorghum sp.
-
-
Cu2+
-
14% increased activity at 10 mM Cu2+
Cu2+
-
76% stimulation of activity at 0.5 mM Cu2+
Cu2+
-
21% increase of activity at 1 mM
Fe2+
-
0.015 g per mol protein
Fe2+
-
0.87 atoms per monomer
Fe2+
-
0.09 atoms per subunit
Fe2+
-
10% increase of activity at 1 mM
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)
Mg2+
-
40% increased activity at 10 mM Mg2+
Mn2+
-
0.201 g per monomer, 6-coordination
Mn2+
-
0.41 atoms per monomer
Mn2+
-
1.12 atoms per subunit
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.
Mn2+
-
40% increased activity at 10 mM Mn2+
Mn2+
-
contains between 0.1 and 0.4 mole Mn per mole enzyme
Mn2+
-
37% increase of activity at 1 mM
Mn2+
-
dependent on
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.
NaCl
P45850
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
NH4Cl
P45850
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+
-
0.36-0.62 g per mol protein
Zn2+
-
0.36 atoms per subunit
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.
additional information
-
OXO gene expression is induced by Al3+
additional information
-
the immobilized oxalate oxidase shows no increase in activity in the presence of 10 mM K+ or Na+
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
-
the enzyme is unaffected by 0.1 mM NaCl and Ca2+
additional information
-
not activated by Mg2+, Co2+, Zn2+, Ni2+, and Fe2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
-
2-mercaptoethanol
-
100% inhibition at 0.01 mM concentration
2-mercaptoethanol
Sorghum sp.
-
0.5 mM concentration 40% inhibition
8-hydroxyquinoline
Sorghum sp.
-
0.5 mM concentration 56% activity retained
8-hydroxyquinoline
-
0.1 mM concentration 41% inhibition
acetate
-
competitive inhibition
alpha,alpha'-dipyridyl
Sorghum sp.
-
0.5 mM concentration 26% inhibition
alpha,alpha'-dipyridyl
-
0.1 mM concentration 31% inhibition
arsenite
Sorghum sp.
-
5 mM concentration 12% inhibition
arsenite
-
concentration higher than 5 mM
ascorbate
-
wild type and immobilized 88% and 81% inhibition respectively
ascorbate
-
ascorbate causes 80% inhibition in the activity of immobilized enzyme
azide
-
mM concentration
azide
Sorghum sp.
-
0.5 mM concentration 57% inhibition
azide
-
0.1 mM concentration 10% inhibition
azide
Sorghum sp.
-
5 mM concentration 80% inhibition
Ca2+
-
34% decreased activity at 10 mM Ca2+
Ca2+
-
92% residual activity at 1 mM
Cl-
-
1 M concentration 75% inhibition
Cu2+
-
Cu2+ + EDTA 0.5 mM concentration 90% activity retained
Cu2+
-
mM concentration
CuSO4
-
0.1 mM concentration 36% inhibition
cyanide
-
50 mM concentration
cyanide
-
50% activity at 16 mM concentration
diethyldithiocarbamate
-
-
diethyldithiocarbamate
-
0.5 mM concentration 60% activity retained
diethyldithiocarbamate
Sorghum sp.
-
0.5 mM concentration 64% activity retained
diethyldithiocarbamate
-
strong inhibitor, 30.7% residual activity at 0.1 mM
Dithionite
Sorghum sp.
-
0.5 mM concentration 42% inhibition
Dithionite
Sorghum sp.
-
5 mM concentration 77% inhibition
dithiothreitol
-
-
EDTA
-
0.5 mM concentration 65% activity retained
EDTA
Sorghum sp.
-
0.5 mM concentration 64% activity retained
EDTA
-
0.1 mM concentration 42% inhibition
EDTA
-
strong inhibitor, 61.5% residual activity at 0.1 mM
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
-
94% inhibition at 0.01 mM concentration; ferrous acetate + EDTA 96% inhibition at 0.01 mM concentration
fluoride
-
sub mM concentration
fluoride
Sorghum sp.
-
at 0.5 mM concentration 76% activity retained
fluoride
-
0.5 mM concentration
fluoride
-
50% activity at 0.24 mM concentration
glutathione
-
-
glutathione
-
slight inhibition, wild type and immobilized
glycolate
-
mM concentration
glycolate
-
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
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
-
sub mM concentration
Iodide
Sorghum sp.
-
0.5 mM concentration 14% inhibition
iodoacetate
Sorghum sp.
-
5 mM concentration 47% inhibition
iodoacetate
-
0.5 mM concentration
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
L-cysteine
-
-
L-cysteine
-
slight inhibition
L-cysteine
-
wild type and immobilized slight inhibition
L-cysteine
Sorghum sp.
-
0.5 mM concentration 60% inhibition
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
N-ethylmaleimide
-
43% activity retained
N-ethylmaleimide
-
25% activity retained at 0.2 mM concentration
N-ethylmaleimide
Sorghum sp.
-
5 mM concentration 89% inhibition
Na2SO4
-
48.4% residual activity at 0.1 mM
NaCl
-
10% inhibition at 1 mM concentration
NaCl
-
14% inhibition at mM concentration
NaCl
-
10 mM concentration
NaCl
-
at 1 mM concentration 43% activity retained by free protein, 85% activity retained by immobilized protein
NEM
-
92% residual activity at 1 mM
nitrate
-
mM concentration
-
nitrate
-
mM concentration
-
nitrite
-
sub mM concentration
nitrite
-
1 mM concentration 10% inhibition
o-phenanthroline
-
0.1 mM concentration 26% inhibition
oxalate
-
substrate inhibition
Pb2+
-
2 mM concentration 57% inhibition, 20 mM concentration 89% inhibition
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
Semicarbazide
-
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
-
1 mM concentration, 10% inhibition of the free enzyme, not of the immobilized enzyme
ZnSO4
-
0.1 mM concentration 12% inhibition
ZnSO4
-
61.3% residual activity at 0.1 mM
ZnSO4
-
90% residual activity at 1 mM
malonate
-
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
additional information
-
no effect: metals ions and flavins
-
additional information
P45850
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
-
additional information
-
acetone precipitation has no influence on the activity of barley oxalate oxidase
-
additional information
-
not influenced by FeSO4
-
additional information
-
not influenced by EDTA, NaCl, and MgSO4
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
8-hydroxyquinoline
-
0.4 mM concentration 400% activation
alpha,alpha-dipyridyl
-
21% increase of activity at 1 mM
-
arsenite
-
5 mM concentration slight activation
Ca(CH3COO)2
-
mM concentration 71% activation
Cu(CH3COO)2
-
0.1 mM concentration 20% activation
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
CuSO4
Sorghum sp.
-
0.5 mM concentration 200% activation
cyanide
-
5 mM concentration slight activation
diethyldithiocarbamate
-
35% increase of activity at 1 mM
FAD
-
slight stimulatory effect, increased by addition of Cu2+
FAD
Sorghum sp.
-
0.5 mM concentration 31% activation
FAD
-
0.1 mM concentration 66% activation
FAD
-
0.001 mM concentration
FAD
-
55.5% stimulation of activity at 0.5 mM; 55.5% stimulation of activity at 0.5 mM FAD
FeSO4
Sorghum sp.
-
0.5 mM concentration 42% activation
FMN
-
slight stimulatory effect, increased by addition of Cu2+
FMN
Sorghum sp.
-
0.5 mM concentration 57% activation
FMN
-
0.1 mM concentration 88% activation
FMN
-
0.001 mM concentration
FMN
-
45% stimulation of activity at 0.5 mM
Formamide
P45850
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
hydroquinone
-
0.1 mM concentration 123% activation
NAD+
-
16.6% stimulation of activity at 0.5 mM FAD
o-phenylenediamine
-
0.1 mM concentration 505% activation
Pb(CH3COO)2
-
1 mM concentration 157% activation
phenylhydrazine
-
0.1 mM concentration 280% activation
riboflavin
-
slight stimulatory effect, increased by addition of Cu2+
riboflavin
-
0.1 mM concentration 111% activation
riboflavin
-
0.001 mM concentration
riboflavin
-
33.3% stimulation of activity at 0.5 mM
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
Urea
-
physiological concentration, 8% activation free protein
Uric acid
-
1 mM concentration, 12% activation free protein, 8% activation immobilized protein
MnSO4
-
0.1 mM concentration 75% activation
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.065
-
oxalate
-
in succinate buffer (50 mM, pH 5.0), 10 mM CuSO4, at 40C
0.1
-
oxalate
-
in citrate buffer, at pH 4.0 and 22C
0.121
-
oxalate
-
oxalate oxidase form NaCl stressed seedlings
0.21
-
oxalate
-
-
0.21
-
oxalate
-
-
0.22
-
oxalate
-
at pH 4.5 and 37C
0.37
-
oxalate
-
immobilized protein
0.38
-
oxalate
-
37C, pH 5.0, free enzyme
0.39
-
oxalate
-
immobilized protein
0.42
-
oxalate
-
-
0.78
-
oxalate
-
oxalate oxidase activity is measured by oxygen uptake assay with a Clark oxygen electrode in a thermostated cell (25C). 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
-
mutant enzyme D241A, pH and temperature not specified in the publication
1.31
-
oxalate
-
calorimetry
1.5
-
oxalate
-
in succinate buffer, at pH 4.0 and 22C
1.88
-
oxalate
-
-
2
-
oxalate
-
mutant enzyme A242E, pH and temperature not specified in the publication
2.16
-
oxalate
-
-
2.54
-
oxalate
-
O2 consumption
6.23
-
oxalate
-
30C, pH 6.5, polyvinyl alcohol membrane immobilized oxalate oxidase
14.9
-
oxalate
-
in acetate buffer, at pH 4.0 and 22C
0.024
-
oxalic acid
Sorghum sp.
-
-
0.05
-
oxalic acid
-
-
0.06
-
oxalic acid
-
immobilized on PEG1900
0.07
-
oxalic acid
-
immobilized on PEG5000
0.27
-
oxalic acid
-
-
0.27
-
oxalic acid
-
PVC-immobilized enzyme
0.42
-
oxalic acid
-
-
0.53
-
oxalic acid
-
free enzyme
0.55
-
oxalic acid
-
in 50 mM succinic acid/NaOH, pH 4.0
0.7
-
oxalic acid
-
immobilized enzyme
0.78
-
oxalic acid
-
native enzyme
1.1
-
oxalic acid
P45850
in 50 mM succinic acid/NaOH, pH 4.0
9.5
-
oxalic acid
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
9.7
-
oxalate
-
oxalate oxidase activity is measured by oxygen uptake assay with a Clark oxygen electrode in a thermostated cell (25C)
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3.9
-
acetate
-
in citrate buffer, at pH 4.0 and 22C
28
-
glycolate
-
in citrate buffer, at pH 4.0 and 22C
15
-
glyoxylate
-
in citrate buffer, at pH 4.0 and 22C
52
-
malate
-
in citrate buffer, at pH 4.0 and 22C
3
-
malonate
-
in citrate buffer, at pH 4.0 and 22C
17
-
pyruvate
-
in citrate buffer, at pH 4.0 and 22C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2e-06
-
-
gl-OXO activity in homogenates of embryos 12 days after fertilisation
0.055
-
P45850
asparagine mutant (N85A), thermostated (25C) 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
-
P45850
asparagine mutant (N75A),thermostated (25C) 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.
-
H2O2 production
0.4
-
-
crude extract, in citrate buffer, at pH 4.0 and 22C
0.71
-
-
-
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
-
-
H2O2 production
2.3
-
-
oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 10 mM ZnO
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
-
-
H2O2 production
2.98
-
-
oxalic acid consumption
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
5.75
-
-
purified recombinant and wild type enzyme
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
-
-
H2O2 production
6
-
-
oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 30 mM Cu2O
6.4
-
-
oxalate oxidase activity after 14 days of cultivation on metal-amended plates, 30 mM MnO2
10.26
-
P45850
wild type, thermostated (25C) Clark oxygen electrode calibrated with the protocatechuic acid/protocatechuate dioxygenase reaction, pH 4
10.4
-
-
H2O2 production
12.7
-
-
after 32fold purification, in citrate buffer, at pH 4.0 and 22C
21.9
-
-
native wild type oxalate oxidase
34
-
-
H2O2 production
94
-
-
native S49A oxalate oxidase
139
-
-
periodate-oxidized oxalate oxidase, Mn5+ content 100%
156
-
-
ascorbate-reduced oxalate oxidase, Mn3+ content above 95%
630
-
-
O2 consumption
additional information
-
-
no detectable activity of recombinant TaOxo2
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
additional information
-
-
Vmax 0,182 mmole/min
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.2
-
-
-
3.2
-
-
free enzyme
4
4.5
-
maximum activity, in situ at 25C with a oxalate solution
4
-
-
immobilized protein
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
4
-
-
activity assay
4
-
-
nanoparticle-bound enzyme
4.5
-
-
-
5
-
Sorghum sp.
-
-
5
-
-
free enzyme
5
-
-
native enzyme
5
-
-
free enzyme
5.2
-
-
crude extract
5.8
-
-
oxalate oxidase form NaCl stressed seedlings
5.8
-
-
partially purified enzyme
6.5
-
-
immobilized protein
6.5
-
-
polyvinyl alcohol membrane immobilized oxalate oxidase
6.5
-
-
PVC-immobilized enzyme
6.5
-
-
the immobilized enzyme shows maximum activity at pH 6.5 when incubated at 40C for 15 min
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
4.5
-
20% activity at pH 2.0 and 4.5
2.5
4.5
-
30% activity at pH 2.5 and 4.5
2.5
4.5
-
60% activity at pH 2.5 and 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
7
Sorghum sp.
-
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
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
30
60
-
in situ in an oxalate solution
30
-
-
polyvinyl alcohol membrane immobilized oxalate oxidase
35
-
-
immobilized protein
35
-
-
nanoparticle-bound enzyme
37
-
-
free enzyme
37
-
-
assay of free oxalate oxidase
37
-
-
activity assay
40
-
Sorghum sp.
-
-
40
-
-
native enzyme or PVC-immobilized enzyme
40
-
-
free enzyme
40
-
-
immobilized enzyme
40
-
-
free enzyme
45
-
Sorghum sp.
-
-
additional information
-
-
activation energy 5.084 kcal/mol
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
25
50
-
50% activity at 25C and 50C
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Sorghum sp.
-
-
Manually annotated by BRENDA team
-
leaves of seedlings
Manually annotated by BRENDA team
Sorghum sp. CSH-5
-
-
-
Manually annotated by BRENDA team
-
fresh or heat dried (55C for 16 h, with T increased in 5C steps to reach 75C) radicles are used. Heat drying reduces the rate of oxalate degradation activity by approximately half. Deep-freezing the radicles to -20C does not lead to any loss of oxalate degradation activity within 4 weeks of storage
Manually annotated by BRENDA team
Sorghum sp.
-
-
Manually annotated by BRENDA team
-
barley root cDNA libary
Manually annotated by BRENDA team
Hordeum vulgare BH393, Sorghum sp. CSH-5
-
-
-
Manually annotated by BRENDA team
-
root border cells (RBC)
Manually annotated by BRENDA team
Sorghum sp.
-
-
Manually annotated by BRENDA team
-
different developmental stages were examined (complete seedling with radicles) with the oxalate degradation rate being similarly high for 4-8-old seedlings
Manually annotated by BRENDA team
-
commercially available oxalate oxidase from barley seedlings
Manually annotated by BRENDA team
-
cuttings from seedlings and 3-year old plants
Manually annotated by BRENDA team
-
cuttings from 4 week old seedlings
Manually annotated by BRENDA team
Sorghum sp. CSH-5
-
-
-
Manually annotated by BRENDA team
Sorghum sp.
-
-
Manually annotated by BRENDA team
Sorghum sp. CSH-5
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
26000
-
-
SDS-PAGE, glyoprotein
49800
-
-
C isoform, calculated from protein sequence
56000
-
-
G isoform, 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
320000
-
-
gel filtration
400000
-
-
gel filtration
additional information
-
-
the molecular weight is not affected by NaCl stress
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 45000, calculated from amino acid sequence; x * 66000, SDS-PAGE
dimer
-
alpha2, 2 * 65000, SDS-PAGE
dimer
Sorghum sp.
-
alpha2, 2 * 62000, SDS-PAGE
dimer
Sorghum sp. CSH-5
-
alpha2, 2 * 62000, SDS-PAGE
-
hexamer
-
alpha6, 6 * 26000, SDS-PAGE
hexamer
-
alpha6, 6 * 65500, SDS-PAGE
hexamer
Ceriporiopsis subvermispora FP-10572
-
alpha6, 6 * 65500, SDS-PAGE
-
octamer
-
alpha8, 8 * 38000, SDS-PAGE
octamer
Pseudomonas sp. OX-53
-
alpha8, 8 * 38000, SDS-PAGE
-
oligomer
-
migrates as an oligomer, most likly a hexamer
pentamer
-
alpha5, 5 * 25000, SDS-PAGE
homodimer
-
2 * 62000, SDS-PAGE
additional information
-
NaCl stress does not affect the number of subunits of the enzyme
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
carbohydrates make up approximately 30% of the enzymes mass
glycoprotein
-
-
glycoprotein
-
3 kDa carbohydrate per 1 mol protein
additional information
-
2 potential N-glycosylation sites, only one of them is probably glycosylated
glycoprotein
-
-
additional information
-
2 potential N-glycosylation sites
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
P45850
in complex with Mn2+ and N3O-donor aminocarboxylate ligands
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
6
Sorghum sp.
-
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50
-
-
after 10 min 100% activity
60
-
-
10 min, 96% recovery
60
-
-
after 10 min wild type 30% activity, immobilized on PEG1900 55% activity and immobilized on PEG5000 70% activity
60
-
-
70% activity retained
60
-
-
after 10 min, 76% activity
70
-
-
after 10 min 9% activity
70
-
-
metal oxide nanoparticles(NP)-bound enzyme retains more activity when subjected to thermal treatment at 70C 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
75
-
-
after 30 min wild type 60% activity, immobilized protein 27% activity
75
-
-
80% wild type and 20% immobilized protein
80
-
-
30 min
89
-
-
after 3 min 49% activity
additional information
-
-
thermally extremely stable
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
immobilized on alkylamine glass
-
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
-
immobilized on PEG1900 and PEG5000
-
enzyme activity of the C isoform is lost in the presence of sodium dodecyl sulfate (SDS)
-
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)
-
immobilized on zirkonia coated alkylamine glass, retains 97% of enzyme activity
-
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 ACCESSION NO.
LITERATURE
by treatment with K3Fe(CN)6 decreases activity, desalting restores initial activity
-
288378
resistant against Na2IrCl6
-
288378
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, 3 months, distilled water, free protein, complete loss of activity, immobilized protein, 70% of activity retained
-
4C, 20 days, free protein, complete loss of activity, immobilized protein on PEG1900, 60% activity retained and immobilized protein on PEG5000, 35% activity retained
-
-180C, several months, no activity loss
-
4-8C, 90 days, native enzyme, up to 70% loss of activity
-
4C, under 3 months no loss of activity by free protein, over 2 years immobilized protein
-
8C, several months, no activity loss, conversion in 4 months to 23 kDa protein, loss of carbohydrate
-
-20C, potassium phosphate buffer pH 6.5, 6 months, no activity loss
-
4C, 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
-
room temperature, immobilized oxalate oxidase between folds of filter paper, 30 d, 50% loss of activity
-
0-4C, 30 days, 50% activity retained
Sorghum sp.
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
concanavalin A affinity chromatography, carboxymethyl-Sepharose column chromatography, and 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
-
ammonium sulfate precipitation, column chromatography, and gel filtration
-
concanavalin A affinity chromatography, carboxymethyl-Sepharose column chromatography, and gel filtration
P45850
DEAE-Sephacel column chromatography and Sephadex G-100 gel filtration
-
mutant proteins
P45850
partially purified
-
ammonium sulfate precipitation, DEAE-Sephacel column chromatography, and Sephadex G-100 gel filtration
-
ammonium sulfate, Sephadex G-200, DEAE-Sephacel
-
-
Sorghum sp.
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli BL21
-
expressed in Pichia pastoris strain X-33
-
mutant enzymes are expressed in Escherichia coli BL21(DE3) cells
-
expressed in Pichia pastoris X33
-
expression of cDNA in Escherichia coli
-
recombinant barley oxalate oxidase expressed in Pichia pastoris (X33)
-
the mutant proteins expressed in Picha pastoris
P45850
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
-
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 Pichia pastoris
-
expressed in Zea mays, expression in Zea mays leads to increased resistance against Ostrinia nubilalis
-
expression of cDNA in Escherichia coli
-
expression of OXO in sunflower
-
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
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression is induced by methanol
-
enzyme activity is very low at 96 h after imbibition, and then increases significantly with a maximum at 240 h
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E216Q
-
mutant exhibits a 200fold loss in decarboxylase activity and a 10fold increase in oxalate oxidase activity
A242E
-
the mutant shows 5% of the wild type 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
N75A
P45850
reduced activity to 2.4% of the wild type level
N85A
P45850
reduced activity to 0.5% of the wild type level
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
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
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
-
oxalate oxidase is useful for oxalic acid removal in industrial bleaching plant filtrates
industry
-
the enzyme is capable of removing oxalic acid from a variety of industrial bleaching filtrates
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
Sorghum sp. CSH-5
-
immobilized oxalate oxidase to determine oxalate concentration in urine for diagnosis of various forms of hyperoxaluria
-
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