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Information on EC 1.2.3.4 - oxalate oxidase and Organism(s) Hordeum vulgare and UniProt Accession P45850
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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
-
powdery
- mildew
-
pathogenesis-related
- sclerotiorum
- graminis
- hyperoxaluria
- blumeria
-
hordei
- erysiphe
- nodorum
-
bicupins
- dentata
-
castanea
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oxalate-degrading
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berk
- alkylamine
- septoria
- medicine
- analysis
- industry
- synthesis
- agriculture
The taxonomic range for the selected organisms is: Hordeum vulgare
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
oxalate oxidase, germin, germin-like protein, oxo-g, gl-oxo, germin gf-2.8, oxalic acid oxidase, 
more
topSYNONYM 
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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oxalic acid oxidase
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Germin
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
redox reaction
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oxidation
reduction
oxidation
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reduction
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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].
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
oxalic acid + O2 + 2 H+
2 CO2 + H2O2
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-
-
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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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glycolate does not serve as a substrate
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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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?
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
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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-
?
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
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
NaCl
specific activity of the wild type oxalate oxidase is lower in the presence of 1 M NH4Cl
NH4Cl
specific activity of the wild type oxalate oxidase is lower in the presence of 1 M NaCl
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+
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.
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.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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ferrous acetate
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ferrous acetate + EDTA 96% inhibition at 0.01 mM concentration
NaCl
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at 1 mM concentration 43% activity retained by free protein, 85% activity retained by immobilized protein
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
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additional information
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acetone precipitation has no influence on the activity of barley oxalate oxidase
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additional information
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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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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
additional information
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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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.78
oxalate
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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)
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9.7
oxalate
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oxalate oxidase activity is measured by oxygen uptake assay with a Clark oxygen electrode in a thermostated cell (25°C)
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
10.26
wild type, thermostated (25°C) Clark oxygen electrode calibrated with the protocatechuic acid/protocatechuate dioxygenase reaction, pH 4
additional information
additional information
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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)
additional information
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Vimax (initial maximum velocity) is nearly independent of pH over the range from pH 3 to 5
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.2
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5 - 6
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the catalytic efficiency (Vmax/Km) increases continuously to lower pH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
expression of barley oxalate oxidase gene confers stable resistance against stem rot in productive and highly susceptible Brassica juncea cv Varuna under field conditions. Stable, single-copy transgenic lines exhibit a significant reduction in the rate of lesion expansion reproducibly over the three-generation i.e. T2, T3, and T4 respectively. The enhanced resistance in the transgenic lines correlated with high oxalate oxidase activity, accumulation of higher levels of H2O2, and robust activation of defense responsive genes upon infection by Sclerotinia sclerotiorum
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). OXO1_HORVU
201
0
21203
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
125000
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migrates as an oligomer, most likely a hexamer in a 12.5% gel using SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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2 potential N-glycosylation sites, only one of them is probably glycosylated
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S49A
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nonglycosylated oxalate oxidase is produced by site-directed mutagenesis (S49A)
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
70
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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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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)
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immobilized on zirkonia coated alkylamine glass, retains 97% of enzyme activity
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
by treatment with K3Fe(CN)6 decreases activity, desalting restores initial activity
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288378
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
concanavalin A affinity chromatography, carboxymethyl-Sepharose column chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
expression of barley oxalate oxidase gene confers stable resistance against stem rot in productive and highly susceptible Brassica juncea cv Varuna under field conditions. Stable, single-copy transgenic lines exhibit a significant reduction in the rate of lesion expansion reproducibly over the three-generation i.e. T2, T3, and T4 respectively. The enhanced resistance in the transgenic lines correlated with high oxalate oxidase activity, accumulation of higher levels of H2O2, and robust activation of defense responsive genes upon infection by Sclerotinia sclerotiorum
industry
medicine
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colorimetric or UV-determination of oxalic acid in biological fluids and beverages
industry
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oxalate oxidase is useful for oxalic acid removal in industrial bleaching plant filtrates
industry
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the enzyme is capable of removing oxalic acid from a variety of industrial bleaching filtrates
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Whittaker, M.M.; Whittaker, J.W.
Characterization of recombinant barley oxalate oxidase expressed by Pichia pastoris
J. Biol. Inorg. Chem.
7
136-145
2002
Hordeum vulgare
Requena, L.; Bornemann, S.
Structure and function studies of oxalate oxidase
Biochem. Soc. Trans.
26
S273
1998
Hordeum vulgare
Zhou, F.; Zhang, Z.; Gregersen, P.L.; Mikkelsen, J.D.; De Neergaard, E.; Collinge, D.B.; Thordal-Christensen, H.
Molecular characterization of the oxalate oxidase involved in the response of barley to the powdery mildew fungus
Plant Physiol.
117
33-41
1998
Hordeum vulgare
Kotsira, V.P.; Clonis, Y.D.
Oxalate oxidase from barley roots: purification to homogeneity and study of some molecular, catalytic, and binding properties
Arch. Biochem. Biophys.
340
239-249
1997
Hordeum vulgare
Pundir, C.S.; Verma, U.
Isolation, purification, immobilization of oxalate oxidase and its clinical applications
Hindustan Antibiot. Bull.
35
173-182
1993
Hordeum vulgare, Musa acuminata
Chiriboga, J.
Purification and properties of oxalic acid oxidase
Arch. Biochem. Biophys.
116
516-523
1966
Hordeum vulgare
Tamas, L.; Simonovicova, M.; Huttova, J.; Mistrik, I.
Elevated oxalate oxidase activity is correlated with Al-induced plasma membrane injury and root growth inhibition in young barley roots
Acta Physiol. Plant.
26
85-93
2004
Hordeum vulgare
-
Cassland, P.; Larsson, S.; Nilvebrant, N.O.; Jonsson, L.J.
Heterologous expression of barley and wheat oxalate oxidase in an E. coli trxB gor double mutant
J. Biotechnol.
109
53-62
2004
Hordeum vulgare, Triticum aestivum
Betsche, T.; Fretzdorff, B.
Biodegradation of oxalic acid from spinach using cereal radicles
J. Agric. Food Chem.
53
9751-9758
2005
Avena sativa, Hordeum vulgare, Secale cereale, Triticum aestivum, Zea mays, Triticum spelta
Opaleye, O.; Rose, R.S.; Whittaker, M.M.; Woo, E.J.; Whittaker, J.W.; Pickersgill, R.W.
Structural and spectroscopic studies shed light on the mechanism of oxalate oxidase
J. Biol. Chem.
281
6428-6433
2006
Hordeum vulgare (P45850)
Whittaker, M.M.; Pan, H.Y.; Yukl, E.T.; Whittaker, J.W.
Burst kinetics and redox transformations of the active site manganese ion in oxalate oxidase: Implications for the catalytic mechanism
J. Biol. Chem.
282
7011-7023
2007
Hordeum vulgare
Borowski, T.; Bassan, A.; Richards, N.G.; Siegbahn, P.E.
Catalytic Reaction Mechanism of Oxalate Oxidase (Germin). A Hybrid DFT Study
J. Chem. Theory Comput.
1
686-693
2005
Hordeum vulgare
Chipps, T.J.; Gilmore, B.; Myers, J.R.; Stotz, H.U.
Relationship between oxalate, oxalate oxidase activity, oxalate sensitivity, and white mold susceptibility in Phaseolus coccineus
Phytopathology
95
292-299
2005
Hordeum vulgare, Phaseolus coccineus, Phaseolus vulgaris
Tamas, L.; Budikova, S.; Huttova, J.; Mistrik, I.; Simonovicova, M.; Siroka, B.
Aluminum-induced cell death of barley-root border cells is correlated with peroxidase- and oxalate oxidase-mediated hydrogen peroxide production
Plant Cell Rep.
24
189-194
2005
Hordeum vulgare
Turhan, H.
Salinity response of transgenic potato genotypes expressing the oxalate oxidase gene
Turk. J. Agric. For.
29
187-195
2005
Hordeum vulgare
-
Burrell, M.R.; Just, V.J.; Bowater, L.; Fairhurst, S.A.; Requena, L.; Lawson, D.M.; Bornemann, S.
Oxalate decarboxylase and oxalate oxidase activities can be interchanged with a specificity switch of up to 282,000 by mutating an active site lid
Biochemistry
46
12327-12336
2007
Bacillus subtilis, Hordeum vulgare (P45850), Gelatoporia subvermispora (Q5ZH56)
Scarpellini, M.; Gaetjens, J.; Martin, O.J.; Kampf, J.W.; Sherman, S.E.; Pecoraro, V.L.
Modeling the resting state of oxalate oxidase and oxalate decarboxylase enzymes
Inorg. Chem.
47
3584-3593
2008
Hordeum vulgare
Cassland, P.; Sjoede, A.; Winestrand, S.; Joensson, L.J.; Nilvebrant, N.O.
Evaluation of oxalate decarboxylase and oxalate oxidase for industrial applications
Appl. Biochem. Biotechnol.
161
255-263
2010
Hordeum vulgare
Winestrand, S.; Larsson, S.; Cassland, P.; Nilvebrant, N.; Jnsson, L.
Effects of ionic substances in bleaching filtrates and of lignosulfonates on the activity of oxalate oxidase from barley
Eng. Life Sci.
11
245-252
2011
Hordeum vulgare
-
Chauhan, N.; Hooda, V.; Pundir, C.
In vitro effects of metal oxide nanoparticles on barley oxalate oxidase
J. Nanopart. Res.
15
1493
2013
Hordeum vulgare, Hordeum vulgare BH393
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