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Information on EC 1.2.3.4 - oxalate oxidase
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1.2.3.4 oxalate oxidaseIUBMB Comments
Contains Mn2+ as a cofactor. The enzyme is not a flavoprotein as had been thought .
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Word Map
- 1.2.3.4
- wheat
- barley
- sclerotinia
- apoplastic
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powdery
- mildew
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pathogenesis-related
- sclerotiorum
- graminis
- hyperoxaluria
- blumeria
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hordei
- erysiphe
- nodorum
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bicupins
- dentata
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castanea
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oxalate-degrading
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berk
- alkylamine
- septoria
- medicine
- analysis
- industry
- synthesis
- agriculture
The enzyme appears in viruses and cellular organisms
Synonyms
oxalate oxidase, germin, germin-like protein, oxo-g, gl-oxo, germin gf-2.8, oxalic acid oxidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aero-oxalo dehydrogenase
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Germin
Germin GF-2.8
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Germin GF-3.8
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germin-like protein
GLP2
oxalate oxidase
oxalate: O2 oxidoreductase
oxalic acid oxidase
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OXO
OxOx
Germin
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
oxalate + O2 = 2 CO2 + H2O2
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oxalate + O2 = 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
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reduction
oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
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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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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
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the substrate affinity and max. activity of oxalate oxidase from NaCl stressed seedlings was adversely affected
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?
oxalate + O2 + H+
CO2 + H2O2
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partially purified enzyme shows highest activity with 0.8 mM oxalate
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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
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ir
additional information
?
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the recombinant enzyme possesses less than 0.1% oxalate decarboxylase activity
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?
additional information
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the recombinant enzyme possesses less than 0.1% oxalate decarboxylase activity
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?
additional information
?
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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
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glycolate does not serve as a substrate
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additional information
?
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no detectable activity against other related organic acids including citrate, glyoxylate, malonate, succinate, glutarate, malate, glycolate, acetate, lactate and formate
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NATURAL SUBSTRATE
NATURAL 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 + H+
CO2 + H2O2
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partially purified enzyme shows highest activity with 0.8 mM oxalate
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-
?
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
-
role in plant signaling and defense
-
-
ir
additional information
?
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the recombinant enzyme possesses less than 0.1% oxalate decarboxylase activity
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-
?
additional information
?
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the recombinant enzyme possesses less than 0.1% oxalate decarboxylase activity
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?
additional information
?
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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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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
AlCl3
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the activity of oxalate oxidase and the production of H2O2 in the root border colls is higher in Al-treated root tips relative to those of the control plants
Cu2+
Fe2+
Mg2+
Mn2+
Mn3+
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treatment of the periodate-oxidized enzyme with ascorbate results in a substantioal decrease in absorption, forming a complex that is spectroscopically identified as a Mn3+ species. Mn3+ form has a 5fold higher specific activity than native recombinant oxalate oxidase.
Mn5+
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titration of oxalate oxidase with sodium periodate results in nearly stoichometric oxidation of the enzyme to an intensely colored yellow complex, whose complete spectroscopic characterization lead to assignment to a superoxidized Mn5+ complex. Treatment of Mn2+ S49A oxalate oxidase generates the same yellow species as the glycosylated wild type enzyme. Mass spectra of isolated and periodate-treated oxalate oxidase are virtually identical, demonstating that no protein oxidation occurred. Peroxidate oxidation increases the specific activity about 5fold.
NaCl
NH4Cl
specific activity of the wild type oxalate oxidase is lower in the presence of 1 M NaCl
SDS
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enzyme activity of the C isoform is lost in the presence of sodium dodecyl sulfate
Zn2+
additional information
Mg2+
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Soluble and active protein obtained only when the enzyme is coexpressed with the chaperones DnaK and DnaJ (G isoform) and when a manganese salt is added to the growth medium (C and G isoform)
Mn2+
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titration of periodate-oxidized oxalate oxidase with hydroxylamine completely eliminates the visible absorption, forming a homogeneous Mn2+ form of the enzyme. The fully reduced Mn2+ form lacks any detectable oxidase activity, reoxidation substantially restores the maximum activity.
NaCl
specific activity of the wild type oxalate oxidase is lower in the presence of 1 M NH4Cl
NaCl
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the specific activity of oxalate oxidase is increased in seedlings grown in a NaCl containing medium compared to normal, which reveals the increased de novo synthesis of the enzyme to sustain oxalate egradation
additional information
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the enzymatic activity is not influenced by K+, Na+, Zn2+, Fe3+, Mn2+, and Mg2+
additional information
incubation of the apoenzyme with a 100fold molar excess of MgCl2, CoCl2, CuCl2, ZnCl2, NiCl2, FeCl2 or FeCl3, individually, does not influence enzymatic activity
additional information
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incubation of the apoenzyme with a 100fold molar excess of MgCl2, CoCl2, CuCl2, ZnCl2, NiCl2, FeCl2 or FeCl3, individually, does not influence enzymatic activity
additional information
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not activated by Mg2+, Co2+, Zn2+, Ni2+, and Fe2+
additional information
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Na2SO4, EDTA-Na2, KCl, NaCl, K2CO3, Na2CO3, Na2HPO4 and NaH2PO4 have no significant effect on the enzyme activities
additional information
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the immobilized oxalate oxidase shows no increase in activity in the presence of 10 mM K+ or Na+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Fe(NO3)2
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1 mM concentration 98% inhibition; Fe(NO3)2 + EDTA 1 mM concentration 96% inhibition
ferrous acetate
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94% inhibition at 0.01 mM concentration; ferrous acetate + EDTA 96% inhibition at 0.01 mM concentration
glyoxylate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
H2O2
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hydrogen peroxide is both a reversible noncompetitive inhibitor of the OxOx catalyzed oxidation of oxalate and an irreversible inactivator. The build-up of the turnover-generated hydrogen peroxide product leads to the inactivation of the enzyme. The introduction of catalase to reaction mixtures protects the enzyme from inactivation allowing reactions to proceed to completion. No changes in global protein structure take place in the presence of hydrogen peroxide
lignosulfonate
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at a lignosulfonate concentration of 50 mg/ml and a pH of 3.8, 2-16% of the activity of oxalate oxidase remain
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malate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
malonate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
SDS
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isoforms OxO1-4, are very sensitive to 0.1% SDS with a nearly total loss of their enzyme activities
ascorbate
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wild type and immobilized 88% and 81% inhibition respectively
ascorbate
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ascorbate causes 80% inhibition in the activity of immobilized enzyme
CuSO4