BRENDA - Enzyme Database
show all sequences of 1.2.3.4

Characterization of Ceriporiopsis subvermispora bicupin oxalate oxidase expressed in Pichia pastoris

Moussatche, P.; Angerhofer, A.; Imaram, W.; Hoffer, E.; Uberto, K.; Brooks, C.; Bruce, C.; Sledge, D.; Richards, N.G.; Moomaw, E.W.; Arch. Biochem. Biophys. 509, 100-107 (2011)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Pichia pastoris strain X-33
Gelatoporia subvermispora
Inhibitors
Inhibitors
Commentary
Organism
Structure
acetate
competitive inhibition
Gelatoporia subvermispora
glycolate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
Gelatoporia subvermispora
glyoxylate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
Gelatoporia subvermispora
malate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
Gelatoporia subvermispora
malonate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
Gelatoporia subvermispora
pyruvate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
Gelatoporia subvermispora
succinate
competitive inhibition
Gelatoporia subvermispora
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.1
-
oxalate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
1.5
-
oxalate
in succinate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
14.9
-
oxalate
in acetate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mn2+
contains between 0.1 and 0.4 mole Mn per mole enzyme
Gelatoporia subvermispora
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
Gelatoporia subvermispora
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
45000
-
x * 45000, calculated from amino acid sequence
Gelatoporia subvermispora
66000
-
x * 66000, SDS-PAGE
Gelatoporia subvermispora
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Gelatoporia subvermispora
the recombinant enzyme possesses less than 0.1% oxalate decarboxylase activity
?
-
-
-
oxalate + O2 + 2 H+
Gelatoporia subvermispora
-
CO2 + 2 H2O2
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Gelatoporia subvermispora
Q5ZH56
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
glycoprotein
carbohydrates make up approximately 30% of the enzyme’s mass
Gelatoporia subvermispora
Purification (Commentary)
Commentary
Organism
DEAE-Sepharose column chromatography and butyl Sepharose column chromatography
Gelatoporia subvermispora
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.4
-
crude extract, in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
12.7
-
after 32fold purification, in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the recombinant enzyme possesses less than 0.1% oxalate decarboxylase activity
724114
Gelatoporia subvermispora
?
-
-
-
-
oxalate + O2 + 2 H+
-
724114
Gelatoporia subvermispora
CO2 + 2 H2O2
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 45000, calculated from amino acid sequence; x * 66000, SDS-PAGE
Gelatoporia subvermispora
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4
-
-
Gelatoporia subvermispora
pH Range
pH Minimum
pH Maximum
Commentary
Organism
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
Gelatoporia subvermispora
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
3
-
malonate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
3.9
-
acetate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
15
-
glyoxylate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
17
-
pyruvate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
28
-
glycolate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
52
-
malate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Pichia pastoris strain X-33
Gelatoporia subvermispora
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
acetate
competitive inhibition
Gelatoporia subvermispora
glycolate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
Gelatoporia subvermispora
glyoxylate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
Gelatoporia subvermispora
malate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
Gelatoporia subvermispora
malonate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
Gelatoporia subvermispora
pyruvate
the competitive inhibitor diminishes enzyme velocity at low concentrations of substrate but the velocity reaches uninhibited maximal levels at high concentrations of substrate
Gelatoporia subvermispora
succinate
competitive inhibition
Gelatoporia subvermispora
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
3
-
malonate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
3.9
-
acetate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
15
-
glyoxylate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
17
-
pyruvate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
28
-
glycolate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
52
-
malate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.1
-
oxalate
in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
1.5
-
oxalate
in succinate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
14.9
-
oxalate
in acetate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mn2+
contains between 0.1 and 0.4 mole Mn per mole enzyme
Gelatoporia subvermispora
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
Gelatoporia subvermispora
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
45000
-
x * 45000, calculated from amino acid sequence
Gelatoporia subvermispora
66000
-
x * 66000, SDS-PAGE
Gelatoporia subvermispora
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Gelatoporia subvermispora
the recombinant enzyme possesses less than 0.1% oxalate decarboxylase activity
?
-
-
-
oxalate + O2 + 2 H+
Gelatoporia subvermispora
-
CO2 + 2 H2O2
-
-
?
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
glycoprotein
carbohydrates make up approximately 30% of the enzyme’s mass
Gelatoporia subvermispora
Purification (Commentary) (protein specific)
Commentary
Organism
DEAE-Sepharose column chromatography and butyl Sepharose column chromatography
Gelatoporia subvermispora
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.4
-
crude extract, in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
12.7
-
after 32fold purification, in citrate buffer, at pH 4.0 and 22°C
Gelatoporia subvermispora
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the recombinant enzyme possesses less than 0.1% oxalate decarboxylase activity
724114
Gelatoporia subvermispora
?
-
-
-
-
oxalate + O2 + 2 H+
-
724114
Gelatoporia subvermispora
CO2 + 2 H2O2
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 45000, calculated from amino acid sequence; x * 66000, SDS-PAGE
Gelatoporia subvermispora
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4
-
-
Gelatoporia subvermispora
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
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
Gelatoporia subvermispora
Expression
Organism
Commentary
Expression
Gelatoporia subvermispora
expression is induced by methanol
up
Expression (protein specific)
Organism
Commentary
Expression
Gelatoporia subvermispora
expression is induced by methanol
up
Other publictions for EC 1.2.3.4
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
739783
Graz
Oxalic acid degradation by a n ...
Abortiporus biennis
Acta Biochim. Pol.
63
595-600
2016
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1
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2
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741317
Kumar
New extracellular thermostable ...
Ochrobactrum intermedium, Ochrobactrum intermedium CL6
Prep. Biochem. Biotechnol.
46
734-739
2016
1
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1
1
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3
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4
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2
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1
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1
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1
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739993
Sakamoto
In vitro and in vivo evidence ...
Rhododendron mucronatum
Biochem. Biophys. Res. Commun.
458
536-542
2015
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1
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1
1
1
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4
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740833
Wei
-
Transgenic Arabidopsis thalian ...
Triticum aestivum
J. Integr. Agric.
14
2565-2573
2015
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1
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1
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1
1
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741123
Li
Divergent biochemical and enzy ...
Oryza sativa
Phytochemistry
118
216-223
2015
3
-
-
-
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1
10
4
-
1
12
1
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2
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1
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1
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2
2
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1
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4
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4
3
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1
4
10
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4
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1
12
1
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1
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1
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2
2
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1
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4
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-
739991
Moomaw
Membrane inlet mass spectromet ...
Gelatoporia subvermispora
Biochem. Biophys. Res. Commun.
450
750-754
2014
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1
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1
3
1
1
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1
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3
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1
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1
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1
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1
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1
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1
1
725764
Chauhan
-
In vitro effects of metal oxid ...
Hordeum vulgare, Hordeum vulgare BH393
J. Nanopart. Res.
15
1493
2013
3
-
-
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9
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3
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2
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2
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1
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1
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1
2
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2
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1
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9
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3
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2
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1
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1
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1
2
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2
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1
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2
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726327
Moomaw
Kinetic and spectroscopic stud ...
Gelatoporia subvermispora
PLoS ONE
8
e57933
2013
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1
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5
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3
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2
-
1
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1
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1
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1
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1
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5
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1
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1
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1
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741281
Zhang
Relationship between disease r ...
Oryza sativa
PLoS ONE
8
e78348
2013
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1
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1
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723893
Sathishraj
-
Oxalic acid and oxalate oxidas ...
Costus pictus
Acta Physiol. Plant.
34
657-667
2012
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1
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1
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724114
Moussatche
Characterization of Ceriporiop ...
Gelatoporia subvermispora
Arch. Biochem. Biophys.
509
100-107
2011
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1
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7
3
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2
2
2
-
4
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1
1
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2
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2
1
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1
1
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6
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1
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7
6
3
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2
2
2
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1
1
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2
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2
1
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1
1
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1
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1
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724851
Winestrand
-
Effects of ionic substances in ...
Hordeum vulgare
Eng. Life Sci.
11
245-252
2011
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1
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1
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725122
Kumar
Purification and partial chara ...
Sorghum bicolor
Indian J. Biochem. Biophys.
48
42-46
2011
4
-
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-
7
1
-
2
2
1
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2
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1
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3
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1
1
1
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1
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4
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7
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1
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2
2
1
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1
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3
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1
1
1
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1
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725791
Wakabayashi
Cell wall oxalate oxidase modi ...
Triticum aestivum
J. Plant Physiol.
168
1997-2000
2011
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1
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1
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3
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1
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1
1
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695712
Cassland
Evaluation of oxalate decarbox ...
Hordeum vulgare
Appl. Biochem. Biotechnol.
161
255-263
2010
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726212
Zhang
-
Function of oxalate oxidase (O ...
Oryza sativa
Plant Physiol. Commun.
46
1040-1044
2010
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696598
Graz
Abortiporus biennis tolerance ...
Abortiporus biennis
Biometals
22
401-410
2009
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700647
Wan
Increased tolerance to oxidati ...
Triticum aestivum
Physiol. Plant.
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30-44
2009
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684408
Pundir
Activation of polyvinyl chlori ...
Sorghum bicolor
Anal. Biochem.
374
272-277
2008
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687082
Scarpellini
Modeling the resting state of ...
Hordeum vulgare
Inorg. Chem.
47
3584-3593
2008
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689689
Dong
Expressing a gene encoding whe ...
Triticum aestivum
Planta
228
331-340
2008
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698230
Godara
Urinary & serum oxalate determ ...
Amaranthus spinosus
Indian J. Med. Res.
127
370-376
2008
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674894
Whittaker
Burst kinetics and redox trans ...
Hordeum vulgare
J. Biol. Chem.
282
7011-7023
2007
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678229
Burrell
Oxalate decarboxylase and oxal ...
Bacillus subtilis, Gelatoporia subvermispora, Hordeum vulgare
Biochemistry
46
12327-12336
2007
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684846
Pan
Characterization of wheat germ ...
Triticum aestivum
Biochem. Biophys. Res. Commun.
356
925-929
2007
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685702
Bhambi
Immobilization of grain-sorghu ...
Sorghum bicolor
Biotechnol. Appl. Biochem.
47
125-129
2007
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687227
Mao
Diverted secondary metabolism ...
Triticum aestivum
J. Agric. Food Chem.
55
2582-2589
2007
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689410
Zou
In vivo measurements of change ...
Triticum aestivum
Phytochem. Anal.
18
341-346
2007
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689657
Welch
-
The effects of oxalic acid on ...
Triticum aestivum
Plant Sci.
172
488-496
2007
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671193
Chen
-
Study on plant regeneration of ...
Triticum aestivum
Agric. Sci. China
5
572-578
2006
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674758
Opaleye
Structural and spectroscopic s ...
Hordeum vulgare
J. Biol. Chem.
281
6428-6433
2006
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675632
Singh
-
Purification and properties of ...
Sorghum bicolor
J. Plant Biochem. Biotechnol.
15
55-57
2006
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671415
Escutia
Cloning and sequencing of two ...
Gelatoporia subvermispora
Appl. Environ. Microbiol.
71
3608-3616
2005
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674116
Betsche
Biodegradation of oxalic acid ...
Avena sativa, Hordeum vulgare, Secale cereale, Triticum aestivum, Triticum spelta, Zea mays
J. Agric. Food Chem.
53
9751-9758
2005
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675043
Borowski
Catalytic Reaction Mechanism o ...
Hordeum vulgare
J. Chem. Theory Comput.
1
686-693
2005
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676392
Chipps
Relationship between oxalate, ...
Hordeum vulgare, Phaseolus coccineus, Phaseolus vulgaris
Phytopathology
95
292-299
2005
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676476
Tamas
Aluminum-induced cell death of ...
Hordeum vulgare
Plant Cell Rep.
24
189-194
2005
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677240
Turhan
-
Salinity response of transgeni ...
Hordeum vulgare
Turk. J. Agric. For.
29
187-195
2005
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654148
Tamas
-
Elevated oxalate oxidase activ ...
Hordeum vulgare
Acta Physiol. Plant.
26
85-93
2004
-
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656331
Cassland
Heterologous expression of bar ...
Hordeum vulgare, Triticum aestivum
J. Biotechnol.
109
53-62
2004
-
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2
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6
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657139
Caliskan
Formation of wheat (Triticum a ...
Triticum aestivum
Planta
219
132-140
2004
-
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657057
Hu
Overexpression of a gene encod ...
Triticum aestivum
Plant Physiol.
133
170-181
2003
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288378
Whittaker
Characterization of recombinan ...
Hordeum vulgare
J. Biol. Inorg. Chem.
7
136-145
2002
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655709
Singh
Entrapment of sorghum root oxa ...
Sorghum bicolor
Indian J. Biochem. Biophys.
39
397-400
2002
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1
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288379
Vuletic
Characterization of cell wall ...
Zea mays
Plant Sci.
157
257-263
2000
-
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6
2
2
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6
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1
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288383
Requena
Structure and function studies ...
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1
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1
1
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Molecular characterization of ...
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1
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288385
Kotsira
Oxalate oxidase from barley ro ...
Hordeum vulgare
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1
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2
1
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1
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1
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Partial purification and prope ...
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4
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1
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Altered physicochemical charac ...
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1995
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6
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Isolation, purification, immob ...
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3
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Satyapal
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An oxalate oxidase from grain ...
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Satyapal; Pundir
Purification and properties of ...
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1
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4
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10
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1
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2
1
1
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1
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Pundir
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Detection of an oxalate oxidas ...
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Purification and characterizat ...
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Pundir
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Occurence of an oxalate oxidas ...
Sorghum sp.
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Chiriboga
Purification and properties of ...
Hordeum vulgare
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6
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Oxalate oxidation by an obliga ...
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