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Information on EC 1.1.3.4 - glucose oxidase and Organism(s) Aspergillus niger and UniProt Accession P13006

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EC Tree
     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.3 With oxygen as acceptor
                1.1.3.4 glucose oxidase
IUBMB Comments
A flavoprotein (FAD).
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Select one or more organisms in this record: ?
This record set is specific for:
Aspergillus niger
UNIPROT: P13006
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Word Map
The taxonomic range for the selected organisms is: Aspergillus niger
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
glucose oxidase, d-glucose oxidase, microcid, goxp5, ygoxpenag, cngoxa, beta-d-glucose oxidase, notatin, glucose aerodehydrogenase, beta-d-glucose oxygen 1-oxidoreductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-D-glucose: oxygen 1-oxidoreductase
-
beta-D-glucose oxidase
-
-
-
-
beta-D-glucose oxygen-1-oxidoreductase
-
-
beta-D-glucose:O2 1-oxidoreductase
-
-
beta-D-glucose:oxygen 1-oxido-reductase
-
-
-
-
beta-D-glucose:oxygen 1-oxidoreductase
-
-
beta-D-glucose:oxygen oxidoreductase
-
-
beta-D-glucose:oxygen-1-oxidoreductase
-
-
beta-D-glucose:quinone oxidoreductase
-
-
-
-
corylophyline
-
-
-
-
D-glucose oxidase
-
-
-
-
D-glucose-1-oxidase
-
-
-
-
deoxin-1
-
-
-
-
glucose aerodehydrogenase
-
-
-
-
glucose oxyhydrase
-
-
-
-
glucose-1-oxidase
-
-
microcid
-
-
-
-
notatin
-
-
-
-
oxidase, glucose
-
-
-
-
penatin
-
-
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
beta-D-glucose:oxygen 1-oxidoreductase
A flavoprotein (FAD).
CAS REGISTRY NUMBER
COMMENTARY hide
9001-37-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
-
-
?
2-deoxy-6-fluoro-D-glucose + O2 + H2O
2-deoxy-6-fluoro-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
1.85% relative activity to beta-D-glucose
-
?
2-deoxy-D-glucose + O2
2-deoxy-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
10% activity compared to beta-D-glucose
-
-
?
2-deoxy-d-glucose + O2
? + H2O2
show the reaction diagram
-
10% of the activity compared to beta-D-glucose
-
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
show the reaction diagram
3,6-methyl-D-glucose + O2
3-O,6-O-dimethyl-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
10% activity compared to beta-D-glucose
-
-
?
3,6-methyl-D-glucose + O2
? + H2O2
show the reaction diagram
-
10% of the activity compared to beta-D-glucose
-
-
?
3,6-methyl-D-glucose + O2 + H2O
3,6-methyl-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
1.85% relative activity to beta-D-glucose
-
?
3-deoxy-D-glucose + O2 + H2O
3-deoxy-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
1% relative activity to D-glucose
-
?
4,6-methyl-D-glucose + O2 + H2O
4,6-methyl-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
1.22% relative activity to beta-D-glucose
-
?
4-deoxy-D-glucose + O2
4-deoxy-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
7% activity compared to beta-D-glucose
-
-
?
4-deoxy-d-glucose + O2
? + H2O2
show the reaction diagram
-
7% of the activity compared to beta-D-glucose
-
-
?
4-deoxy-D-glucose + O2 + H2O
4-deoxy-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
2% relative activity to D-glucose
-
?
4-O-methy-D-glucose + O2 + H2O
4-O-methyl-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
15% relative activity to D-glucose
-
?
4-O-methyl-D-glucose + O2
4-O-methyl-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
8% activity compared to beta-D-glucose
-
-
?
4-O-methyl-D-glucose + O2
? + H2O2
show the reaction diagram
-
8% of the activity compared to beta-D-glucose
-
-
?
6-deoxy-D-glucose + O2
6-deoxy-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
12% activity compared to beta-D-glucose
-
-
?
6-deoxy-d-glucose + O2
? + H2O2
show the reaction diagram
-
12% of the activity compared to beta-D-glucose
-
-
?
6-deoxy-D-glucose + O2 + H2O
6-deoxy-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
10% relative activity to D-glucose
-
?
6-O-methyl-D-glucose + O2 + H2O
6-O-methyl-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
1% relative activity to D-glucose
-
?
alpha-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
beta-D-glucose
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
-
-
-
?
beta-D-glucose + 1,2-naphthoquinone
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
beta-D-glucose + 1,2-naphthoquinone-4-sulfonic acid
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
beta-D-glucose + 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
beta-D-glucose + benzoquinone
D-glucono-1,5-lactone + hydroquinone
show the reaction diagram
-
enzyme immobilized onto alumina
immobilized enzyme, yield of conversion: 100%
?
beta-D-glucose + ferrocinium-methanol
?
show the reaction diagram
-
-
-
-
?
beta-D-glucose + methyl-1,4-benzoquinone
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
beta-D-glucose + p-benzoquinone
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
beta-D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
beta-D-glucose + potassium ferricyanide
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
D-galactose + O2 + H2O
?
show the reaction diagram
-
low GOD activity
-
-
?
D-glucose + di-(2,2'-bipyridinyl)ruthenium(III)dichloride
D-glucono-1,5-lactone + di-(2,2'-bipyridinyl)ruthenium(II)dichloride
show the reaction diagram
-
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
D-glucose + [(1,10-phenanthroline)2(Cl)2Ru(III)]
D-glucono-1,5-lactone + [(1,10-phenanthroline)2(Cl)2Ru(II)]
show the reaction diagram
-
-
-
-
?
D-glucose + [(1,8-dimethyl-4,5-phenanthroline)3Ru(II)]PF6-
D-glucono-1,5-lactone + [(1,8-dimethyl-4,5-phenanthroline)3Ru(III)]PF6-
show the reaction diagram
-
-
-
-
?
D-glucose + [(2,2'-(4,4'dimethyl)bipyridine)2(Cl)2Ru(III)]
D-glucono-1,5-lactone + [(2,2'-(4,4'dimethyl)bipyridine)2(Cl)2Ru(II)]
show the reaction diagram
-
-
-
-
?
D-glucose + [(2,2'-(4,4'dimethyl)bipyridine)2(Cl)2Ru(III)]PF6-
D-glucono-1,5-lactone + [(2,2'-(4,4'dimethyl)bipyridine)2(Cl)2Ru(II)]PF6-
show the reaction diagram
-
-
-
-
?
D-glucose + [(2,2'-bipyridine)2(CO32-)1/2Ru(III)]
D-glucono-1,5-lactone + [(2,2'-bipyridine)2(CO32-)1/2Ru(II)]
show the reaction diagram
-
-
-
-
?
D-glucose + [(2,2'-bipyridine)2(H2O)2Ru(III)]PF6-
D-glucono-1,5-lactone + [(2,2'-bipyridine)2(H2O)2Ru(II)]PF6-
show the reaction diagram
-
-
-
-
?
D-glucose + [(2,2'-bipyridine)2(SCN-)2Ru(III)]
D-glucono-1,5-lactone + [(2,2'-bipyridine)2(SCN-)2Ru(II)]
show the reaction diagram
-
-
-
-
?
D-glucose + [(2,2'-bipyridine)3Ru(II)]PF6-
D-glucono-1,5-lactone + [(2,2'-bipyridine)3Ru(III)]PF6-
show the reaction diagram
-
-
-
-
?
D-mannose + O2
? + H2O2
show the reaction diagram
-
9% activity compared to beta-D-glucose
-
-
?
D-mannose + O2 + H2O
?
show the reaction diagram
-
low GOD activity
-
-
?
L-sorbose + O2
? + H2O2
show the reaction diagram
mannose + O2
? + H2O2
show the reaction diagram
-
9% of the activity compared to beta-D-glucose
-
-
?
mannose + O2 + H2O
? + H2O2
show the reaction diagram
-
1% relative activity to D-glucose
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme is rapidly cleared from blood stream after application to rats, enzyme-produced H2O2 has toxic effects of rat liver and causes inflammation, at nontoxic levels it causes increased glutathione oxidation and induction of heme oxygenase 1 in the liver, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
-
both the thermal and chemical denaturation of the enzyme cause dissociation of the flavin cofactor
Flavin-hypoxanthine dinucleotide
-
FHD, can substitute FAD
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
active site bound, required
CuCl2
Iron
-
the enzyme contains 2 mol of iron per 160000 Da
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-butyl-1-methylpyrrolidinium tetrafluoroborate
-
the presence of 1-butyl-1-methylpyrrolidinium tetrafluoroborate on the surface of single-walled carbon nanotubes can significantly affect the electrical transfer properties of the nanotube and lead to the decrease of the electrocatalytic activity of the GOx
1-butyl-3-methylimidazolium tetrafluoroborate
-
the presence of 1-butyl-3-methylimidazolium tetrafluoroborate on the surface of single-walled carbon nanotubes can significantly affect the electrical transfer properties of the nanotube and lead to the decrease of the electrocatalytic activity of the GOx
1-butyl-3-methylpyridinium tetrafluoroborate
-
the presence of 1-butyl-3-methylpyridinium tetrafluoroborate on the surface of single-walled carbon nanotubes can significantly affect the electrical transfer properties of the nanotube and lead to the decrease of the electrocatalytic activity of the GOx
2,4-dichlorphenoxyacetic acid
decreases the enzyme activity by about 70% at 2 mM
2-deoxy-D-glucose
-
-
4-chloromercuribenzoate
-
-
adenine nucleotides
-
inhibition of FAD-binding to apoprotein
AlCl3
-
inhibits the enzyme at low concentrations of 5 mM, and inhibits it completely at higher salt concentrations over 0.1 M
arsenite
-
-
Br-
-
competitive, at low pH
Cl-
-
competitive, at low pH
D-arabinose
-
-
dimedone
-
-
DTNB
complete inhibition at 2 mM
DTT
complete inhibition at 2 mM
F-
-
competitive, at low pH
Fe2+
complete inhibition at 2 mM
fructose
-
incubation of Aspergillus niger glucose oxidase with 100 mM fructose for 8 days results in 88% loss in activity
glucose
-
incubation of Aspergillus niger glucose oxidase with 100 mM glucose for 8 days results in 71% loss in activity
hydrazine
-
-
hydroxylamine
-
-
lecithin
6% inhibition at 2%
Mg2+
-
total inhibition of the enzyme at a Mg2+ concentration of 1.9 M
Na+
-
the inhibiting effect of Na+ions is reduced at Na+concentrations over 0.5 M
NaF
decreases the enzyme activity by about 5% at 2 mM
NaN3
decreases the enzyme activity by about 8% at 2 mM
NaNO3
p-chloromercuribenzoate
-
-
phenylhydrazine
-
-
phenylmercuric acetate
-
-
PMSF
decreases the enzyme activity by about 18% at 2 mM
putrescine
-
i.e. 1,4-diaminobutane
ribose
-
incubation of Aspergillus niger glucose oxidase with 1 mM ribose for up to 8 days results in 96% loss in activity
sodium bisulfate
-
-
sodium cholate
-
non-competitive inhibition in microemulsion
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Al3+
slight activation
N,N-dimethyl-4-nitrosoaniline
a redox mediator
Zn2+
slight activation
Ag2+
-
1 mM, 90-95% inhibition
Blue dextran
-
40% increase of activity as a result of the binding with the enzyme
-
Co2+
-
1 mM, about 90% inhibition
Hg2+
-
1 mM, about 85% inhibition
Ni2+
-
1 mM, about 75% inhibition
Pb2+
-
1 mM, about 25% inhibition
trehalose
-
trehalose does not affect Vmax but instead decreases Km and as a result enzyme efficiency is increased
Zn2+
-
1 mM, about 55% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.149 - 33.4
beta-D-glucose
3.33
1,4-benzoquinone
-
pH 5.5, 35°C
0.019 - 537
beta-D-glucose
25 - 26
D-glucose
0.19
di-(2,2'-bipyridinyl)ruthenium(III)dichloride
-
pH 7.3, 30°C
0.1107
ferrocinium-methanol
-
native enzyme, pH 6.5, 70°C
2.9 - 7
methyl-1,4-benzoquinone
0.18 - 0.2
O2
2.43
phenazine methosulfate
-
pH 4.7
0.694
[(1,10-phenanthroline)2(Cl)2Ru(III)]
-
pH 7.3, 30°C
0.019
[(1,8-dimethyl-4,5-phenanthroline)3Ru(II)]PF6-
-
pH 7.3, 30°C
0.52
[(2,2'-(4,4'dimethyl)bipyridine)2(Cl)2Ru(III)]
-
pH 7.3, 30°C
0.0313
[(2,2'-(4,4'dimethyl)bipyridine)2(Cl)2Ru(III)]PF6-
-
pH 7.3, 30°C
0.0922
[(2,2'-bipyridine)2(CO32-)1/2Ru(III)]
-
pH 7.3, 30°C
0.153
[(2,2'-bipyridine)2(H2O)2Ru(III)]PF6-
-
pH 7.3, 30°C
0.0513
[(2,2'-bipyridine)2(SCN-)2Ru(III)]
-
pH 7.3, 30°C
0.057
[(2,2'-bipyridine)3Ru(II)]PF6-
-
pH 7.3, 30°C
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
33.3 - 920
beta-D-glucose
0.00521 - 1938
beta-D-glucose
35.4
di-(2,2'-bipyridinyl)ruthenium(III)dichloride
-
pH 7.3, 30°C
10.5
[(1,10-phenanthroline)2(Cl)2Ru(III)]
-
-
50.3
[(1,8-dimethyl-4,5-phenanthroline)3Ru(II)]PF6-
-
pH 7.3, 30°C
10.5
[(2,2'-(4,4'dimethyl)bipyridine)2(Cl)2Ru(III)]
-
pH 7.3, 30°C
13.8
[(2,2'-(4,4'dimethyl)bipyridine)2(Cl)2Ru(III)]PF6-
-
pH 7.3, 30°C
38.6
[(2,2'-bipyridine)2(CO32-)1/2Ru(III)]
-
pH 7.3, 30°C
8.3
[(2,2'-bipyridine)2(H2O)2Ru(III)]PF6-
-
pH 7.3, 30°C
31.4
[(2,2'-bipyridine)2(SCN-)2Ru(III)]
-
pH 7.3, 30°C
158
[(2,2'-bipyridine)3Ru(II)]PF6-
-
pH 7.3, 30°C
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.997 - 30.7
beta-D-glucose
27 - 38
beta-D-glucose
0.017
ferrocinium-methanol
-
native enzyme, pH 6.5, 70°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000662
Ag+
Aspergillus niger
pH 4.0, 40°C
0.0126
Cu2+
Aspergillus niger
pH 4.0, 40°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
153.5
recombinant enzyme after 3.34fold purification, at 35°C
100
-
immobilized enzyme, pH 5.5, temperature not specified in the publication, high enzyme concentration
135
-
purified enzyme
155
purified recombinant enzyme, pH 6.0, 40°C
172
-
purified enzyme
189
-
GOD-His6 expressed in wild-type cells of Saccharomyces cerevisiae
194
-
GOD-His6 expressed in pmr1DELTA mutant cells of Saccharomyces cerevisiae
2.32
-
crude enzyme extract, pH not specified in the publication, 30°C
216
-
immobilized enzyme, pH 5.5, temperature not specified in the publication, low enzyme concentration
28.81
3.1
-
in the culture filtrate
6
-
after isolation from the fermenter liquid by gel filtration, lyophilized preparate
62
-
purified enzyme, pH not specified in the publication, 30°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
recombinant mutant B11
5 - 7
recombinant enzyme
5.5
recombinant enzyme
5.5 - 7.4
assay at
6.86
glucose oxidase-immobilized polypyrrole/alginate films used as enzyme electrodes to test response to glucose solutions, cyclic voltammetry applied, performed in a one-compartment three electrode cell in 0.025 M PBS
2 - 9
-
pH profile of soluble and insoluble enzyme complexes, overview
5 - 6
5.1
-
assay at
5.6 - 5.8
-
crystalline enzyme
5.9
-
soluble enzyme and immobilized enzyme in collagen
6.3
-
immobilized on activated carbon
6.5
-
native enzyme
7.2
-
enzyme-pentacyanoferrate(III)-nucleophilic ligands-complex interaction assay
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1 - 7.5
trend of the dependence of pH on peak current investigated in 0.1 M KCl solution, maximum amperometric response of hydrogen peroxide on the microelectrode dependent on pH over a range from 5.0 to 7.0
3.5 - 9
activity range of wild-type and mutant enzymes, profile overview
4 - 7
more than 90% of the maximum activity of glycosylated and deglycosylated enzyme form is observed between pH 4.0-7.0. Outside this range activity decreases rapidly
4 - 8
more than 88% of the maximum activity is observed between pH 4.0 and 8.0, outside this range the activity decreases dramatically
2 - 7
-
the activities of modified GOD are about 40-55% of those of native GOD in the pH range tested (pH 2.0-7.0)
2.5 - 8.5
-
activity range, profile overview. 85% of maximal activity at pH 5.0, 51% activity at pH 7.0
2.5 - 9
-
immobilized on activated carbon
3.4 - 7.5
-
soluble enzyme
3.5 - 6.5
-
-
4 - 7
4.5 - 10
-
pH 4.5: about 85% of maximal activity, natural GOD and pmr1DELTA-mutant-derived GOD, about 90% of maximal activity, hyperglycosylated GOD expressed in wild-type cells of Saccharomyces cerevisiae, pH 10: about 75% of maximal activity, natural GOD and pmr1DELTA-mutant-derived GOD, about 90% of maximal activity, hyperglycosylated GOD expressed in wild-type cells of Saccharomyces cerevisiae
4.5 - 6.5
-
over 60% activity within this range at 50°C
4.5 - 7
-
pH 4.5: about 60% of maximal activity, pH 7.0: about 50% of maximal activity
5.5 - 9
-
80% of the maximal activity is observed in the pH 5.5-9.0 range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 37
assay at
37
recombinant enzyme
22
-
assay at room temperature
35
-
assay at
50 - 80
-
temperature profile of soluble and insoluble enzyme complexes, overview
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 50
the activity of the glycosylated and deglycosylated enzyme increases 2fold from 25°C to 55°C
25 - 69
at each temperature in the study (25-69.1°C), the catalytic activity of the native, aniline-, or benzoate-modified enzyme increases with high hydrostatic pressure, and reaches a maximum at around 180 MPa. At 180 MPa and 69.1°C, aniline-modified enzyme produces the fastest catalytic rate, followed by benzoate-modified enzyme, and then native enzyme
15 - 60
-
activity within this range at pH 5.0
20 - 60
-
20°C: about 90% of maximal activity, 55°C: 90% of maximal activity, 60°C: 33% of maximal activity
20 - 70
-
activity range, profile overview. About 90% of maximal activity at 20°C, 90% at 55°C, rapid deactivation above
25 - 60
the activity gradually increases from 25°C to 40°C, but followed by a decrease at higher temperatures
70
-
pH 5.1, 75% loss of of activity of natural GOD and pmr1DELTA-mutant-derived GOD, 65% loss of activity of hyperglycosylated GOD
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.2
-
isoelectric focusing
additional information
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
12% of glucose oxidase activity in the stationary phase and 16% of glucose oxidase activity in the mid-exponential phase is localised in the cytoplasm
Manually annotated by BRENDA team
-
34% of glucose oxidase activity in the stationary phase and 26% of glucose oxidase activity in the mid-exponential phase is localised in the membrane
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
enzyme mutant M12 GOx (N2Y/K13E/T30V/I94V/K152R) shows a 3fold higher activity compared to the wild type at 5 mM glucose and two times higher activity at 200 mM glucose
physiological function
evolution
glucose oxidase (GO) belongs to the auxiliary activity family AA3_2
malfunction
comparison of the substrate profile and H2O2 inactivation of the wild-type glucose oxidase, EC 1.1.3.4, and the Y300A mutant variant of GOOX, the mutant shows a comparatively broad substrate range along with reduced substrate inhibition compared to glucose oxidase, overview
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GOX_ASPNG
605
0
65638
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
157000
PAGE under non-dissociating conditions, glycosylated enzyme
160000
80000
90000 - 130000
recombinant glycosylated Aga2–GOx fusion protein, native PAGE
136000
-
x * 136000 deglycosylated recombinant enzyme, SDS-PAGE
140000
-
native enzyme, gel filtration
146000
-
x * 146000, deglycosylated recombinant enzyme with PEG-350 reagent, SDS-PAGE
150000 - 153000
152000
-
SDS-PAGE
154000
-
crystalline enzyme
155000
-
x * 155000, wild-type enzyme, SDS-PAGE
158000 - 160000
-
gel filtration
160000
180000
-
native enzyme
182200
-
x * 182200, PEGylated enzyme, SDS-PAGE
211000
-
x * 211000, deglycosylated recombinant enzyme with PEG-5000 reagent, SDS-PAGE
320000
-
x * 320000, recombinant enzyme expressed in yeast, SDS-PAGE
669000
-
PEGylated enzyme, gel filtration
75000
-
x * 75000, SDS-PAGE
77000
-
2 * 77000, native enzyme, SDS-PAGE
79000
-
2 * 79000, SDS-PAGE
80000
-
2 * 80000
86400
-
2 * 86400, native enzyme, SDS-PAGE
87100
-
x * 87100, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
homodimer
dimer
homodimer
monomer
-
1 * 160000, SDS-PAGE
additional information
-
a stable secondary conformation with some degree of freedom at the active sites is essential for the bioelectrocatalytic activity of GOx
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
glycoprotein
additional information
-
endo-beta-N-acetylglucosaminidase from Flavobacterium sp. releases about 30% of the N-linked sugar chains from the enzyme
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure refined at 1.9 A resolution to an R value of 19.0%
tertiary structure determined by x-ray crystallography
vapor diffusion sitting drop method
of the partially deglycosylated enzyme, crystal structure determined by isomorphous replacement and refined to 2.3 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A173T/A332S
increased electron transfer (1.2fold)
A173T/F414L
increased electron transfer (1.2fold), 70% decrease in O2 sensitivity
A173V/A332S/F414I/V560T
increased electron transfer (6.4fold), decrease in O2 sensitivity
A332S/V560T
increased electron transfer (1.2fold), 70% decrease in O2 sensitivity
F414Y
increased electron transfer
I94V/T30S
increased O2 sensitivity, increased electron transfer (1.9fold)
N2Y/K13E/T30V/I94V/K152R
site-directed mutagenesis of mutant M12, pH optimum and sugar specificity of M12 mutant of GOx is similar to the wild-type enzyme, while thermostability is slightly decreased. Mutant M12 GOx expressed in Pichia pastoris shows three times higher activity compared to wild-type GOx towards redox mediators like N,N-dimethyl-nitroso-aniline used for glucose strips manufacturing. Mutant M12 GOx remains very specific for glucose but has higher activity for galactose compared to wild-type GOx
T110A
the mutant enzyme displays 12.3fold reduced O2 consumption
T110S
increased electron transfer
T110S/T34V
increased electron transfer
T110S/V20Y
increased O2 sensitivity
T30V/I94V/A162T
2.9fold increase in kcat/Km, decrease in t1/2(60°C) by 1.5°C
T30V/I94V/A162T/R537K/M556V
4.0fol2.6fold increase in kcat/Km, increase in t1/2(60°C) by 5.25°C
T56V/T132S
mutant enzyme displays better catalytic properties than the native enzyme
V20Y
increased electron transfer
A449C
-
site-directed mutagenesis, the mutation results in almost completely diminished activity compared to the wild-type enzyme
E84C
-
site-directed mutagenesis, the mutation does not affect enzyme activity. Attachment of gold nanoparticles to the purified proteins leads to an immediate and dramatic decrease in activity
H172K
site-directed mutagenesis, mutant H172K shows increased thermosensitivity compared to the wild-type enzyme
H172K/H220D
site-directed mutagenesis, mutant H172K/H220D does not show significant differences in thermal stability but about 70% increased initial activity compared to the wild-type enzyme
H220D
site-directed mutagenesis, mutant H220D shows increased thermosensitivity and reduced activity compared to the wild-type enzyme
H447C
-
site-directed mutagenesis, the mutation does not affect enzyme activity. Attachment of gold nanoparticles to the purified proteins leads to an immediate and dramatic decrease in activity
H447K
L500D
site-directed mutagenesis, inactive mutant
L569E
Q124R/L569E
site-directed mutagenesis, the mutation has no significant effect on stability but causes a twofold increase of the enzyme's specific activity
Q345K
Q469K
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q469K/L500D
Q90R
site-directed mutagenesis, the mutant shows increased sensitivity to thermal denaturation, with R1 and R2 values 60% and 80% lower than wild-type enzyme respectively
Q90R/Y509E
Q90R/Y509E/T554M
the triple mutant is a glucose oxidase with high stability
S307C
-
site-directed mutagenesis, the mutation does not affect enzyme activity. Attachment of gold nanoparticles to the purified proteins leads to an immediate and dramatic decrease in activity
T30S/I94V
T554M
random mutagenesis, the mutation generates a sulfur-pi interaction, the mutant shows 60% reduced activity and 40% increased thermal stability compared to the wild-type enzyme
T56V/T132S
-
site-directed mutagenesis, the mutant shows improved catalytic efficiency. The protein has three native cysteines, of which two are involved in a disulfide bond and the third is a free cysteine, Cys 521
T56V/T132S/C521S
-
site-directed mutagenesis, the mutant shows improved catalytic efficiency, mutation C521S does not alter enzyme activity, but the attachment of AuNPs to the native free thiol is prevented
Y435C
-
site-directed mutagenesis, the mutation does not affect enzyme activity. Attachment of gold nanoparticles to the purified proteins leads to an immediate and dramatic decrease in activity
Y509E
site-directed mutagenesis, the mutation does not cause a significant change in the thermal stability of the enzyme, but causes increased enzyme activity compared to the wild-type enzyme
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
deglycosylation has no marked effect on the stability of the enzyme above pH 5
727055
9
at alkaline pH, particularly at and above pH 9.0, the glycosylated and the declycosylated enzyme are relatively unstable
727055
1.9
-
stable for 1 h, when FAD is added, bound to Blue Dextran
389798
10
-
the native enzyme shows partial unfolding but the deglycosylated form shows a compaction of conformation
654358
2
-
acid-induced unfolding of both forms of enzyme, significant loss of FAD cofactor and secondary structure
654358
2.5
-
the BTL wild-type strain enzyme is slightly more stable than the commercially available enzyme
389831
3
-
the BTL wild-type strain enzyme is slightly more stable than the commercially available enzyme
389831
3 - 11
-
10% relative activity after 30 min at pH 3.0, 40% relative activity after 30 min at pH 4.0, 50% relative activity after 30 min at pH 5.0, 55% relative activity after 30 min at pH 6.0, 100% activity after 30 min at pH 7.0, 95% relative activity after 30 min at pH 8.0, 75% relative activity after 30 min at pH 9.0, 70% relative activity after 30 min at pH 10.0, 55% relative activity after 30 min at pH 11.0
710858
3 - 5
-
deglycosylated enzyme, 4°C, 4 months, 65-75% activity retained
389816
3 - 9
-
2 h, 25°C, cell debris, stable, no loss of activity in the range of pH 3.0-7.0, loss of 10% activity at pH 8.0-9.0
672763
4 - 9
purified recombinant enzyme, more than 80% of activity is retained after incubation for 1 h at pHs from 4.0 to 9.0 and the maximum activity remains at pH 5.0-8.0
743193
4.5 - 6
-
the enzyme shows a pH-dependent response to the high pressure homogenization treatment, with reduction or maintenance of activity at pH 4.5-6.0 and a remarkable activity increase (30-300%) at pH 6.5 at all tested temperatures. i.e. 15°C, 50°C and 75°C
743644
4.5 - 7.4
-
the poly(methyl methacrylate)-bovine serum albumin particle-adsorbed GOx has a higher catalytic activity at pH 7.4, close to the physiological environment, in comparison with that at pH 4.5
699922
5 - 8
-
native and deglycosylated form
389788
6 - 8
-
-
389789
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 40
50% of enzyme activity is maintained after 90 min incubation at 20-40°C
20 - 60
the activity of recombinant GOD increases slightly at the reaction temperature ranging from 20-40°C, and then falls moderately till 60°C. The recombinant enzyme retains more than 90% of activity within 40°C. Over 30% of activity is lost at 50°C, whereas almost no activity is detected above 60°C
30 - 50
purified recombinant free enzyme and immobilized enzyme, the enzyme activity remains rather unchanged from 30-45°C and then drops at higher temperatures. The thermal stability of immobilized GOx is only slightly higher than that of the free enzyme
50
stable up to. At 50°C the enzyme is inactivated by 30% over a period of 11 h. The thermal stability is unaffected by the depletion of carbohydrate
55
purified dimeric enzyme, pH 5.8, stable up to, rapid inactivation above, the enzyme forms aggregates at incubation temperatures above 55°C, overview
75
purified recombinant free enzyme, loss of 50% activity
15 - 70
-
the enzyme shows a pH-dependent response to the high pressure homogenization treatment, with reduction or maintenance of activity at pH 4.5-6.0 and a remarkable activity increase (30-300%) at pH 6.5 at all tested temperatures. i.e. 15°C, 50°C and 75°C. The enzyme's thermal tolerance is reduced due to high pressure homogenization treatment and the storage for 24 h at high temperatures of 50°C and 75°C also causes a reduction of activity
20
-
half-life: 29.64h
25 - 70
-
70% relative activity after 30 min at 25°C, 100% activity after 30 min at 30°C, 90% relative activity after 30 min at 37°C, 75% relative activity after 30 min at 50°C, 30% relative activity after 30 min at 70°C
35
-
half-life: 78.48 h
40 - 60
purified recombinant enzyme, more than 90% activity remaining after incubation for 30 min at 50°C and 54% at temperatures up to 55°C
50 - 60
-
at pH 6.0 and at 50°C, the half life of the enzyme is about 20 h, thermal denaturation is observed above 60°C
50 - 70
-
the half-life is diminished from 210 min at 50°C to 0.61 min at 70°C, the inactivation rate constant decreases by up to 50% at temperatures between 50 and 70°C in the presence of 0.6 M trehalose
55.8
-
transition temperature is independent of the protein concentration. The thermally denatured enzyme is a compact structure, a form of molten globule-like apoenzyme
56
-
half-life of native enzyme without additive: 86 min, half-life of enzyme in presence of lysozyme: 322 min, half-life of enzyme in presence of 1 M NaCl: 1806 min, half-life of enzyme in presence of 0.2 M K2SO4: 1446 min
59
-
midpoint for thermal inactivation of residual activity and dissocation of FAD
62
-
midpoint for loss of secondary and tertiary structure
63
-
half-life of native enzyme without additive: 7.5 min, half-life of enzyme in presence of lysozyme: 24 min, half-life of enzyme in presence of 1 M NaCl: 146 min, half-life of enzyme in presence of 0.2 M K2SO4: 62 min
67
-
half-life of native enzyme without additive: 4.5 min, half-life of enzyme in presence of lysozyme: 12 min, half-life of enzyme in presence of 1 M NaCl: 58 min, half-life of enzyme in presence of 0.2 M K2SO4: 27.5 min
72.4
-
denaturation point of native enzyme
72.8
-
denaturation point of periodate-oxidized enzyme
80
-
the pure enzyme is inactive at 80°C, thermal resistance is high only at pH 7.0
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
high hydrostatic pressure stabilizes the aniline-, and benzoate-modified glucose oxidase at 69.1-80°C compared to atmospheric pressure. At 240 MPa and 80.0°C, the first order rate constant of inactivation (k(inact)) of aniline-modified enzyme is 0.02/min, or 3.7 times smaller than for the native enzyme, while the k(inact) for benzoate-modified enzyme is 0.26/min, or 2.8times smaller than for the native enzyme at the same temperature. At 240 MPa and 80.0°C, the k(inact) of the aniline-modified enzyme is 69times smaller than the k(inact) of native enzyme (15.3/min) at 0.1 MPa and 80.0°C. The combination of high hydrostatic pressure and hydrophobic modification makes more thermostable
protein/water interfacial tension as a critical physicochemical attribute of excipients that is crucial for increasing enzyme kinetic stability
3°C, little loss of activity, 3 years
-
4.0 M urea, immunoaffinity-layered preparation retains 87% of original activity after 2 h and 40% of activity after 24 h of incubation, whereas the soluble enzyme loses all of its activity within 1 h of preincubation
-
after immobilization of the oxidized GOX with silver nanoparticles, the Km and Vmax of the immobilization enzyme remarkably reduce and increase, respectively. While the bioconjugate is stable in lower temperatures and also in neutral to basic pH, the enzymatic activity of the bioconjugate slightly decreases in higher temperature
-
Ca2+ and Mg2+ at 1 M induce compaction of the native conformation of the enzyme, and the enzyme shows a higher stability as compared to the native enzyme against urea denaturation, Ca2+ and Mg2+ at concentrations above 2 M induce dissociation of the native dimeric enzyme, resulting in stabilization of the enzyme monomer, 3 M Ca2+-stabilized monomer retains about 70% secondary structure present in the native enzyme dimer, however there is a complete loss of cooperative interactions between these secondary structural elements present in the enzyme
-
chemical denaturation by 6.67 M guanidine HCl is accompanied by dissociation of the homodimeric enzyme into monomers
-
comparative stability of insoluble complexes of enzyme obtained with concanavalin A and glycosyl-specific polyclonal antibodies, overview
-
comparison of stability immobilized on various materials
-
D2O stabilizes
-
divalent cations such as Ba2+, Ca2+ and Mg2+ have a slightly negative effect on stability
-
encapsulation of the enzyme in the liposomes composed of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine increases the enzyme stability through its decreased inhibition because of H2O2 produced in glucose oxidation
-
freezing/thawing, stable
-
K2SO4 enhances the thermal stability by primarily strengthening the hydrophobic interactions and makes the holoenzyme a more compact dimeric structure
-
KCl stabilizes
-
low temperature ultrasonic processing of GOx (23 kHz at 4°C) does not appreciably compromise bioactivity
-
most stable, highly active and high-yield glucose oxidase preparations are optained by assembling the enzyme on small amounts of immunoaffinity support using glycosyl-specific polyclonal antibodies
-
NaCl stabilizes
-
SDS, 1%, 30°C, pH 5.5, stable 30 h incubation
-
SDS, 1.5%, 2-mercaptoethanol, 55°C, residual activity: 24%
-
SDS, 5%, stable to
-
stabilita to 4 M urea of soluble and insoluble enzyme complexes, overview
-
the activity of glucose oxidase is retained for more than three days in the water pool of the microemulsion, while a 30% loss in activity of the enzyme occurs in aqueous medium during that period
-
the complexation between GOX, chitosan, and calcium alginate stabilizes the enzyme, GOX retains its integrity upon adsorption to calcium alginate gel beads during the coating and after release from alginate/chitosan microsphere
-
the enzyme shows a pH-dependent response to the high pressure homogenization treatment, with reduction or maintenance of activity at pH 4.5-6.0 and a remarkable activity increase (30-300%) at pH 6.5 at all tested temperatures. i.e. 15°C, 50°C and 75°C. The enzyme's thermal tolerance is reduced due to high pressure homogenization treatment and the storage for 24 h at high temperatures of 50°C and 75°C also causes a reduction of activity
-
the enzyme stability is not influenced by physiological concentration of sodium chloride (140 mM)
-
the maximum enzymatic activity of copolymer-conjugated GOD (poly(N-isopropylacrylamide-co-methacrylic acid-co-octadecylacrylate)-conjugated GOD) is about 40-55% of that of native GOD
-
the poly(methyl methacrylate)-bovine serum albumin particle-adsorbed GOx can retain at least 80% of the free enzyme activity
-
the stabilization of the enzyme by NaCl and lysozyme is primarily the result of charge neutralization
-
urea: 7 M, 5 min, activity fully restored
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetone
dimethylformamide
-
50%, 37°C, 6 h, immunoeffinity immobilized enzyme preparation retains 99% of the original activity, soluble enzyme retains 63% of the initial activity
dioxane
tetrahydrofuran
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
immobilized enzyme, 50°C, half of GOx activity is retained in 40% v/v MeOH/acetate buffer
743105
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, storage for 30 days with a retainment of 90% activity
50°C, purified recombinant immobilized GOx, up to 80% of initial activity is retained after 44 h 50°C, purified recombinant free GOx, loss of 90% of initial activity within 44 h, a further 120 h storage period at 9°C leads to partial denaturation and is not reversible
-20°C, lyophilised enzyme, minimum of 6 months, remains stable
-
-20°C, purified enzyme, 6 months without addition of additives, complete stable, no loss of activity
-
-20°C, purified thioaniline-functionalized enzyme, at least three months, no noticeable degradation in its activity
-
0°C, as a solid, stable for at least 2 years
-
3°C, purified enzyme, several years
-
4°C, immobilized, 11% loss of activity, 1 year
-
4°C, lyophilized enzyme, no loss of activity after 1 year, 10% loss of activity after 2 years
-
4°C, purified recombinant enzyme in 100 mM sodium phosphate, pH 5.1, several months, no loss of activity
-
lyophilized, over P2O5
-
native GOx retains 43% of its bioactivity after 10 days and completely loses activity within 30 days. The bioconjugates of GOx, i.e. GOx-PPEG-A, GOx-PAA, GOx-PMA and GOx-PTBA, still retain bioactivity of 57%, 53%, 59%, and 68%, respectively after 10 days. 27%, 26%, 39%, and 37% of their origin bioactivity are still maintained after 30 days, respectively. Their bioactivities are lost completely after 45 days, 50 days, 55 days, and 55 days for GOx-PPEG-A, GOx-PAA, and GOx-PMA and GOx-PTBA, respectively
-
reaction rate of free GOx in solution remained stable up to 50 days for all investigated pH values, followed by a dramatic decrease owing to enzyme deactivation
-
storage for 24 h at high temperatures of 50°C and 75°C causes a reduction of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation
one step purification
purification to homogeneity by hydrophobic interaction and ion-exchange chromatography
recombinant mutant enzyme B11 from Saccharomyces cerevisiae strain EBY100 cell walls by anion exchange chromatography and ultrafiltration
recombinant wild-type and mutant M12 from Pichia pastoris strain KM71H by cross-flow ultrafiltration and anion exchange chromatography
ammonium sulfate precipitation and anion exchange column chromatography
-
ammonium sulfate precipitation, ion exchange chromatography, and gel filtration
-
from BTL wild-type strain using ammonium sulfate precipitation, column chromatography on Q-Sepharose at pH 6 and pH 4.5 and gel filtration on SW-300
-
from commercial preparation
-
from commercial preparation using DEAE-cellulose chromatography and Sephadex G-200 gel filtration
-
G-25 column chromatography
-
HiTrap phenyl HP column chromatography and HiTrap Q FF column chromatography
-
native enzyme 26.4fold by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
-
native enzyme 9.5fold from strain PIL7 by ammonium sulfate fractionation, dialysis, anion exchange chromatography, and gel filtration
-
native enzyme by ammonium sulfate fractionation, ion exchange chromatography, and gel filtration
-
native enzyme by liquid-liquid cationic reversed micelles extraction, CTAB micelles, method evaluation, overview
-
phenyl Sepharose column chromatography, Q Sepharose column chromatography, gel filtration
-
purchased and further purified by DEAE-Toyopearl 650M column chromatography
-
recombinant extracellular enzyme 1.26fold from Pichia pastoris by anion exchange chromatography
Sephacryl 200 gel filtration
-
Sephadex G-50 gel filtration
-
using dialysis, ammonium sulfate fractionation and column chromatography on DEAE-cellulose
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris KM71H
expressed in Pichia pastoris strain SMD1168
expression in Pichia pastoris. Cloned into the expression vector, pPIC9 and screened by the alcohol oxidase promoter. The enzyme production increases at 28°C. Enzyme activity induced by 1.0% methanol and the highest level of enzyme production is the result of shaking rate at 225 rpm
expression in Yarrowia lipolytica. Yarrowia lipolytica is a suitable and efficient eukaryotic expression system to production of recombinant enzyme (GOX) and can be used to production of pure form of GOX for industrial applications
expression of wild-type and mutant enzyme in Pichia pastoris
gene gox, recombinant expression of wild-type and M12 mutant enzymes in Pichia pastoris strain KM71H or in Saccharomyces cerevisiae strain InvSc1
overexpression in Saccharomyces cerevisiae
recombinant expression of mutant enzyme B11 in Saccharomyces cerevisiae strain EBY100 cell wall
construction of a recombinant strain, the recombinant strain produces up to four times more extracellular enzyme than wild type under identical conditions
-
expressed in Nicotiana tabaccum cultivar SR1
-
expressed in Pichia pastoris strain GS115
-
expressed in Saccharomyces cerevisiae
-
expression in Pichia pastoris GS115
expression in Saccharomyces cerevisiae mutant deficient in PMR1 gene. GOD-His6 expressed in wild-type strain is hyperglycosylated, GOD-His6 expressed in pmr1DELTA strain is not hyperglycosylated
-
gene gox, recombinant expression of the extracellular enzyme in Pichia pastoris strain GS115
isolation of the gene encoding the enzyme, DNA sequence analysis of the coding region shows 80% identity to the sequence of a enzyme gene previously published
-
recombinant expression of His-tagged enzyme in Pichia pastoris strain KM71H
recombinant expression of wild-type and mutant enzymes in Saccharomyces cerevisiae strain BY4741 (MATa his3 leu2 met15 ura3) from plasmid pSSP-GOX, the GOX coding sequence is fused to the STA1 signal peptide from Saccharomyces cerevisiae var. diastaticus and is under the control of the galactose-inducible GAL10/CYC1 promoter
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
thermal denaturation of glucose oxidase is an irreversible transition to the compact denatured form with a defined oligomeric structure that is significantly different from the chemically denatured state of the enzyme, unfolded monomer
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
mutant glucose oxidase (B11-GOx) is obtained from directed protein evolution and wild-type enzyme. Higher glucose oxidation currents are obtained from B11-GOx both in solution and polymer electrodes compared to wild type enzyme. Improved electrocatalytic activity towards electrochemical oxidation of glucose from the mutant enzyme. The enzyme electrode with the mutant enzyme B11-GOx shows a faster electron transfer indicating a better electronic interaction with the polymer mediator. Promising application of enzymes developed by directed evolution tailored for the applications of biosensors and biofuel cells
biotechnology
the enzyme is used for a number of applications in biotechnology and clinical diagnostics
diagnostics
energy production
food industry
industry
the enzyme is used in clinical, pharmaceutical, food and chemical industries
synthesis
analysis
biofuel production
biotechnology
diagnostics
food industry
industry
synthesis
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Okuma, H.; Sekimukai, S.; Hoshi, M.; Toyama, K.; Watanabe, E.
Biosensor system for continuous flow determination of enzyme activities. I. Determination of glucose oxidase and lactic dehydrogenase activities
Enzyme Microb. Technol.
11
824-829
1989
Aspergillus niger
-
Manually annotated by BRENDA team
Takegawa, K.; Fujiwara, K.; Iwahara, S.; Yamamoto, K.; Tochikura, T.
Effect of deglycosylation of N-linked sugar chains on glucose oxidase from Aspergillus niger
Biochem. Cell Biol.
67
460-464
1989
Aspergillus niger
Manually annotated by BRENDA team
Rogalski, J.; Fiedurek, J.; Szczordrak, J.; Kapusta, K.; Leonowicz, A.
Optimization of glucose oxidase synthesis in submerged cultures of Aspergillus niger G-13 mutant
Enzyme Microb. Technol.
10
508-511
1988
Aspergillus niger
-
Manually annotated by BRENDA team
Ye, W.N.; Combes, D.; Monsan, P.
Influence of additives on the thermostability of glucose oxidase
Enzyme Microb. Technol.
10
498-502
1988
Aspergillus niger
-
Manually annotated by BRENDA team
Eriksson, K.O.; Kourteva, I.; Yao, K.; Liao, J.L.; Kilar, F.; Hjerten, S.
Application of high-performance chromatographic and electrophoretic methods to the purification and characterization of glucose oxidase and catalase from Penicillium chrysogenum
J. Chromatogr.
397
239-249
1987
Aspergillus niger, Penicillium amagasakiense, Penicillium chrysogenum, Penicillium janthinellum, Talaromyces purpureogenus
Manually annotated by BRENDA team
Szajani, B.; Molnar, A.; Klamar, G.; Kalman, M.
Preparation, characterization, and potential application of an immobilized glucose oxidase
Appl. Biochem. Biotechnol.
14
37-47
1987
Aspergillus niger
Manually annotated by BRENDA team
Fiedurek, J.; Rogalski, J.; Ilczuk, Z.; Leonowicz, A.
Screening and mutagenesis of moulds for the improvement of glucose oxidase production
Enzyme Microb. Technol.
8
734-736
1986
Aspergillus niger, Penicillium chrysogenum
-
Manually annotated by BRENDA team
Kunst, A.; Draeger, B.; Ziegenhorn, J.
Colorimetric methods with glucose oxidase and peroxidase
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
6
178-185
1984
Aspergillus niger
-
Manually annotated by BRENDA team
Alberti, B.N.; Klibanov, A.M.
Preparative production of hydroquinone from benzoquinone catalysed by immobilized D-glucose oxidase
Enzyme Microb. Technol.
4
47-49
1982
Aspergillus niger
-
Manually annotated by BRENDA team
Solomon, B.; Lotan, N.; Katchalski-Katzir, E.
Interaction of glucose oxidase with blue dextran
J. Chromatogr.
215
121-129
1981
Aspergillus niger
-
Manually annotated by BRENDA team
Cho, Y.K.; Bailey, J.E.
Immobilization of enzymes on activated carbon: Properties of immobilized glucoamylase, glucose oxidase, and gluconolactone
Biotechnol. Bioeng.
20
1651-1665
1978
Aspergillus niger
-
Manually annotated by BRENDA team
Nakamura, S.; Hayashi, S.; Koga, K.
Effect of periodate oxidation on the structure and properties of glucose oxidase
Biochim. Biophys. Acta
445
294-308
1976
Aspergillus niger
Manually annotated by BRENDA team
Tsuge, H.; Natsuaki, O.; Ohashi, K.
Purification, properties, and molecular features of glucose oxidase from Aspergillus niger
J. Biochem.
78
835-843
1975
Aspergillus niger
Manually annotated by BRENDA team
Bright, H.J.; Porter, D.J.T.
Flavoprotein oxidases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
12
421-505
1975
Aspergillus niger, Penicillium amagasakiense
-
Manually annotated by BRENDA team
Constantinides, A.; Vieth, W.R.; Fernandes, P.M.
Characterization of glucose oxidase immobilized on collagen
Mol. Cell. Biochem.
1
127-133
1973
Aspergillus niger
Manually annotated by BRENDA team
Pazur, J.H.
Glucose oxidase from Aspergillus niger
Methods Enzymol.
9
82-87
1966
Aspergillus niger
-
Manually annotated by BRENDA team
Bentley, R.
Glucose oxidase
The Enzymes, 2nd Ed. (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
7
567-586
1963
Aspergillus niger, Mycoderma aceti, Penicillium amagasakiense
-
Manually annotated by BRENDA team
Swoboda, B.E.P.; Massey, V.
Purification and properties of the glucose oxidase from Aspergillus niger
J. Biol. Chem.
240
2209-2215
1965
Aspergillus niger
Manually annotated by BRENDA team
VanDijken, J.P.; Veenhuis, M.
Cytochemical localization of glucose oxidase in peroxisomes of Aspergillus niger
Eur. J. Appl. Microbiol. Biotechnol.
9
275-283
1980
Aspergillus niger
-
Manually annotated by BRENDA team
Hayashi, S.; Nakamura, S.
Comparison of fungal glucose oxidases. Chemical, physicochemical and immunological studies
Biochim. Biophys. Acta
438
37-48
1976
Aspergillus niger, Penicillium amagasakiense
Manually annotated by BRENDA team
Kalisz, H.M.; Hecht, H.J.; Schomburg, D.; Schmid, R.D.
Crystallization and preliminary X-ray diffraction studies of a deglycosylated glucose oxidase from Aspergillus niger
J. Mol. Biol.
213
207-209
1990
Aspergillus niger
Manually annotated by BRENDA team
Degani, Y.; Heller, A.
Direct electrical communication between chemically modified enzymes and metal electrodes. 2. Methods for bonding electron-transfer relays to glucose oxidase and D-amino-acid oxidase
J. Am. Chem. Soc.
110
2615-2620
1988
Aspergillus niger
-
Manually annotated by BRENDA team
Sanner, C.; Macheroux, P.; Ruterjans, H.; Muller, F.; Bacher, A.
15N- and 13C-NMR investigations of glucose oxidase from Aspergillus niger
Eur. J. Biochem.
196
663-672
1991
Aspergillus niger
Manually annotated by BRENDA team
Voet, J.G.; Andersen, E.C.
Electrostatic control of enzyme reactions: the mechanism of inhibition of glucose oxidase by putrescine
Arch. Biochem. Biophys.
233
88-92
1984
Aspergillus niger
Manually annotated by BRENDA team
Chan, T.W.; Bruice, T.C.
One and two electron transfer reactions of glucose oxidase
J. Am. Chem. Soc.
99
2387-2389
1977
Aspergillus niger
Manually annotated by BRENDA team
Duke, F.R.; Weibel, M.; Page, D.S.; Bulgrin, V.G.; Luthy, J.
Glucose oxidase mechanism. Enzyme activation by substrate
J. Am. Chem. Soc.
91
3904-3909
1969
Aspergillus niger
-
Manually annotated by BRENDA team
Weibel, M.K.; Bright, H.J.
The glucose oxidase mechanism. Interpretation of the pH dependence
J. Biol. Chem.
246
2734-2744
1971
Aspergillus niger
Manually annotated by BRENDA team
Swoboda, B.E.P.
The mechanism of binding of flavin-adenine dinucleotide to the apoenzyme of glucose oxidase and evidence for the involvement of multiple bonds
Biochim. Biophys. Acta
175
380-387
1969
Aspergillus niger
Manually annotated by BRENDA team
Hecht, H.J.; Kalisz, H.M.; Hendle, J.; Schmid, R.D.; Schomburg, D.
Crystal structure of glucose oxidase from Aspergillus niger refined at 2.3 A resolution
J. Mol. Biol.
229
153-172
1993
Aspergillus niger
Manually annotated by BRENDA team
Hellmuth, K.; Pluschkell, S.; Jung, J.K.; Ruttkowski, E.; Rinas, U.
Optimization of glucose oxidase production by Aspergillus niger using genetic- and process-engineering techniques
Appl. Microbiol. Biotechnol.
43
978-984
1995
Aspergillus niger
Manually annotated by BRENDA team
Hatzinikolaou, D.G.; Hansen, O.C.; Macris, B.J.; Tingey, A.; Kekos, D.; Goodenough, P.; Stougaard, P.
A new glucose oxidase from Aspergillus niger: characterization and regulation studies of enzyme and gene
Appl. Microbiol. Biotechnol.
46
371-381
1996
Aspergillus niger
Manually annotated by BRENDA team
Huwel, S.; Haalck, L.; Conrath, N.; Spener, F.
Maltose phosphorylase from Lactobacillus brevis: purification, characterization, and application in a biosensor for ortho-phosphate
Enzyme Microb. Technol.
21
413-420
1997
Aspergillus niger
Manually annotated by BRENDA team
Haouz, A.; Twist, C.; Zentz, C.; Tauc, P.; Alpert, B.
Dynamic and structural properties of glucose oxidase enzyme
Eur. Biophys. J.
27
19-25
1998
Aspergillus niger
Manually annotated by BRENDA team
Akhtar, M.S.; Ahmad, A.; Bhakuni, V.
Divalent cation induced changes in structural properties of the dimeric enzyme glucose oxidase: dual effect of dimer stabilization and dissociation with loss of cooperative interactions in enzyme monomer
Biochemistry
41
7142-7149
2002
Aspergillus niger
Manually annotated by BRENDA team
Trytek, M.; Fiedurek, J.
Biotransformation of D-limonene to carvone by means of glucose oxidase and peroxidase
Acta Microbiol. Pol.
51
57-62
2002
Aspergillus niger
Manually annotated by BRENDA team
Zhang, W.; Huang, Y.; Dai, H.; Wang, X.; Fan, C.; Li, G.
Tuning the redox and enzymatic activity of glucose oxidase in layered organic films and its application in glucose biosensors
Anal. Biochem.
329
85-90
2004
Aspergillus niger
Manually annotated by BRENDA team
Akhtar, M.S.; Bhakuni, V.
Alkaline treatment has contrasting effects on the structure of deglycosylated and glycosylated forms of glucose oxidase
Arch. Biochem. Biophys.
413
221-228
2003
Aspergillus niger
Manually annotated by BRENDA team
Seymour, S.L.; Klinman, J.P.
Comparison of rates and kinetic isotope effects using PEG-modified variants and glycoforms of glucose oxidase: the relationship of modification of the protein envelope to C-H activation and tunneling
Biochemistry
41
8747-8758
2002
Aspergillus niger
Manually annotated by BRENDA team
Ivanova, E.V.; Ershov, A.Y.; Laurinavicius, V.; Meskus, R.; Ryabov, A.D.
Comparative kinetic study of D-glucose oxidation by ruthenium(III) compounds catalyzed by FAD-dependent glucose oxidase and PQQ-dependent glucose dehydrogenase
Biochemistry
68
407-415
2003
Aspergillus niger
Manually annotated by BRENDA team
Yoshimoto, M.; Miyazaki, Y.; Sato, M.; Fukunaga, K.; Kuboi, R.; Nakao, K.
Mechanism for high stability of liposomal glucose oxidase to inhibitor hydrogen peroxide produced in prolonged glucose oxidation
Bioconjug. Chem.
15
1055-1061
2004
Aspergillus niger
Manually annotated by BRENDA team
Jan, U.; Husain, Q.
Preparation of a highly stable, very active and high-yield multilayered assembly of glucose oxidase using carbohydrate-specific polyclonal antibodies
Biotechnol. Appl. Biochem.
39
233-239
2004
Aspergillus niger
Manually annotated by BRENDA team
Gupta, S.; Mukhopadhyay, L.; Moulik, S.P.
Kinetics in microemulsion V. Glucose oxidase catalyzed oxidation of beta-D-glucose in aqueous, micellar and water-in-oil microemulsion media
Indian J. Biochem. Biophys.
40
340-349
2003
Aspergillus niger
Manually annotated by BRENDA team
Gouda, M.D.; Singh, S.A.; Rao, A.G.; Thakur, M.S.; Karanth, N.G.
Thermal inactivation of glucose oxidase. Mechanism and stabilization using additives
J. Biol. Chem.
278
24324-24333
2003
Aspergillus niger
Manually annotated by BRENDA team
Zoldak, G.; Zubrik, A.; Musatov, A.; Stupak, M.; Sedlak, E.
Irreversible thermal denaturation of glucose oxidase from Aspergillus niger is the transition to the denatured state with residual structure
J. Biol. Chem.
279
47601-47609
2004
Aspergillus niger
Manually annotated by BRENDA team
Brahim, S.; Narinesingh, D.; Guiseppi-Elie, A.
Kinetics of glucose oxidase immobilized in p(HEMA)-hydrogel microspheres in a packed-bed bioreactor
J. Mol. Catal. B
18
69-80
2002
Aspergillus niger
-
Manually annotated by BRENDA team
Wohlfahrt, G.; Trivic, S.; Zeremski, J.; Pericin, D.; Leskovac, V.
The chemical mechanism of action of glucose oxidase from Aspergillus niger
Mol. Cell. Biochem.
260
69-83
2004
Aspergillus niger
Manually annotated by BRENDA team
Ko, J.H.; Hahm, M.S.; Kang, H.A.; Nam, S.W.; Chung, B.H.
Secretory expression and purification of Aspergillus niger glucose oxidase in Saccharomyces cerevisiae mutant deficient in PMR1 gene
Protein Expr. Purif.
25
488-493
2002
Aspergillus niger
Manually annotated by BRENDA team
Tetianec, L.; Kulys, J.
Study of kinetics of Aspergillus niger glucose oxidase reaction with pentacyanoferrates containing nucleophilic ligands
Biologija (Vilnius)
4
43-47
2005
Aspergillus niger
-
Manually annotated by BRENDA team
Ferreira, L.F.; Taqueda, M.E.; Converti, A.; Vitolo, M.; Pessoa, A.
Purification of glucose oxidase from Aspergillus niger by liquid-liquid cationic reversed micelles extraction
Biotechnol. Prog.
21
868-874
2005
Aspergillus niger
Manually annotated by BRENDA team
Bhatti, H.N.; Madeeha, M.; Asgher, M.; Batool, N.
Purification and thermodynamic characterization of glucose oxidase from a newly isolated strain of Aspergillus niger
Can. J. Microbiol.
52
519-524
2006
Aspergillus niger, Aspergillus niger NFCCP
Manually annotated by BRENDA team
Rost, D.; Welker, A.; Welker, J.; Millonig, G.; Berger, I.; Autschbach, F.; Schuppan, D.; Mueller, S.
Liver-homing of purified glucose oxidase: A novel in vivo model of physiological hepatic oxidative stress (H(2)O(2))
J. Hepatol.
46
482-491
2006
Aspergillus niger
Manually annotated by BRENDA team
Jan, U.; Khan, A.A.; Husain, Q.
A study on the comparative stability of insoluble complexes of glucose oxidase obtained with concanavalin A and specific polyclonal antibodies
World J. Microbiol. Biotechnol.
22
1033-1039
2006
Aspergillus niger
-
Manually annotated by BRENDA team
Li, J.; Yu, J.
Fabrication of Prussian Blue modified ultramicroelectrode for GOD imaging using scanning electrochemical microscopy
Bioelectrochemistry
72
102-106
2008
Aspergillus niger (P13006)
Manually annotated by BRENDA team
Burchardt, M.; Wittstock, G.
Kinetic studies of glucose oxidase in polyelectrolyte multilayer films by means of scanning electrochemical microscopy (SECM)
Bioelectrochemistry
72
66-76
2008
Aspergillus niger (P13006)
Manually annotated by BRENDA team
Chen, S.; Chen, W.; Xue, G.
Electrogeneration of polypyrrole/alginate films for immobilization of glucose oxidase
Macromol. Biosci.
8
478-483
2008
Aspergillus niger (P13006)
Manually annotated by BRENDA team
Kumar, J.; DSouza, S.F.
Preparation of PVA membrane for immobilization of GOD for glucose biosensor
Talanta
75
183-188
2008
Aspergillus niger (P13006)
Manually annotated by BRENDA team
Bahshi, L.; Frasconi, M.; Tel-Vered, R.; Yehezkeli, O.; Willner, I.
Following the biocatalytic activities of glucose oxidase by electrochemically cross-linked enzyme-Pt nanoparticles composite electrodes
Anal. Chem.
80
8253-8259
2008
Aspergillus niger
Manually annotated by BRENDA team
Yu, J.H.; Kang, S.G.; Jung, U.Y.; Jun, C.H.; Kim, H.
Effects of omega-3 fatty acids on apoptosis of human gastric epithelial cells exposed to silica-immobilized glucose oxidase
Ann. N. Y. Acad. Sci.
1171
359-364
2009
Aspergillus niger
Manually annotated by BRENDA team
Guo, Y.; Lu, F.; Zhao, H.; Tang, Y.; Lu, Z.
Cloning and heterologous expression of glucose oxidase gene from Aspergillus niger Z-25 in Pichia pastoris
Appl. Biochem. Biotechnol.
162
498-509
2010
Aspergillus niger (P13006), Aspergillus niger Z-25 (P13006), Aspergillus niger Z-25
Manually annotated by BRENDA team
Wong, C.M.; Wong, K.H.; Chen, X.D.
Glucose oxidase: natural occurrence, function, properties and industrial applications
Appl. Microbiol. Biotechnol.
78
927-938
2008
Aspergillus niger
Manually annotated by BRENDA team
Miron, J.; Vazquez, J.; Gonzalez, M.; Murado, M.
Joint effect of nitrogen and phosphorous on glucose oxidase production by Aspergillus niger: Discussion of an experimental design with a risk of co-linearity
Biochem. Eng. J.
40
54-63
2008
Aspergillus niger
-
Manually annotated by BRENDA team
Jairajpuri, D.S.; Fatima, S.; Saleemuddin, M.
Complexing of glucose oxidase with anti-glucose oxidase antibodies or the F(ab)(2)/F(ab) fragments derived therefrom protects both the enzyme and antibody/antibody fragments against glycation
Biochemistry
73
1235-1241
2008
Aspergillus niger
Manually annotated by BRENDA team
Tao, Z.; Raffel, R.A.; Souid, A.K.; Goodisman, J.
Kinetic studies on enzyme-catalyzed reactions: oxidation of glucose, decomposition of hydrogen peroxide and their combination
Biophys. J.
96
2977-2988
2009
Aspergillus niger
Manually annotated by BRENDA team
Gao, F.; Courjean, O.; Mano, N.
An improved glucose/O2 membrane-less biofuel cell through glucose oxidase purification
Biosens. Bioelectron.
25
356-361
2009
Aspergillus niger
Manually annotated by BRENDA team
Bankar, S.B.; Bule, M.V.; Singhal, R.S.; Ananthanarayan, L.
Glucose oxidase - an overview
Biotechnol. Adv.
27
489-501
2009
Aspergillus niger
Manually annotated by BRENDA team
Johnstone-Robertson, M.; Clarke, K.; Harrison, S.
Characterization of the distribution of glucose oxidase in Penicillium sp. CBS 120262 and Aspergillus niger NRRL-3 cultures and its effect on integrated product recovery
Biotechnol. Bioeng.
99
910-918
2008
Aspergillus niger, Penicillium canescens, Penicillium canescens CBS 120262, Aspergillus niger NRRL-3
Manually annotated by BRENDA team
Jo, S.M.; Lee, H.Y.; Kim, J.C.
Glucose-sensitivity of liposomes incorporating conjugates of glucose oxidase and poly(N-isopropylacrylamide-co-methacrylic acid-co-octadecylacrylate)
Int. J. Biol. Macromol.
45
421-426
2009
Aspergillus niger
Manually annotated by BRENDA team
Paz-Alfaro, K.J.; Ruiz-Granados, Y.G.; Uribe-Carvajal, S.; Sampedro, J.G.
Trehalose-mediated thermal stabilization of glucose oxidase from Aspergillus niger
J. Biotechnol.
141
130-136
2009
Aspergillus niger
Manually annotated by BRENDA team
Guiseppi-Elie, A.; Choi, S.; Geckeler, K.
Ultrasonic processing of enzymes: Effect on enzymatic activity of glucose oxidase
J. Mol. Catal. B
58
118-123
2009
Aspergillus niger
-
Manually annotated by BRENDA team
Wu, X.; Zhao, B.; Wu, P.; Zhang, H.; Cai, C.
Effects of ionic liquids on enzymatic catalysis of the glucose oxidase toward the oxidation of glucose
J. Phys. Chem. B
113
13365-13373
2009
Aspergillus niger
Manually annotated by BRENDA team
He, C.; Liu, J.; Xie, L.; Zhang, Q.; Li, C.; Gui, D.; Zhang, G.; Wu, C.
Activity and thermal stability improvements of glucose oxidase upon adsorption on core-shell PMMA-BSA nanoparticles
Langmuir
25
13456-13460
2009
Aspergillus niger
Manually annotated by BRENDA team
Kumar, S.; Sitasawad, S.L.
N-acetylcysteine prevents glucose/glucose oxidase-induced oxidative stress, mitochondrial damage and apoptosis in H9c2 cells
Life Sci.
84
328-336
2009
Aspergillus niger
Manually annotated by BRENDA team
Liu, Q.; Rauth, A.M.; Liu, J.; Babakhanian, K.; Wang, X.; Bendayan, R.; Wu, X.Y.
Characterization of a microsphere formulation containing glucose oxidase and its in vivo efficacy in a murine solid tumor model
Pharm. Res.
26
2343-2357
2009
Aspergillus niger
Manually annotated by BRENDA team
Hashemifard, N.; Mohsenifar, A.; Ranjbar, B.; Allameh, A.; Lotfi, A.S.; Etemadikia, B.
Fabrication and kinetic studies of a novel silver nanoparticles-glucose oxidase bioconjugate
Anal. Chim. Acta
675
181-184
2010
Aspergillus niger
Manually annotated by BRENDA team
Altikatoglu, M.; Basaran, Y.; Arioz, C.; Ogan, A.; Kuzu, H.
Glucose oxidase-dextran conjugates with enhanced stabilities against temperature and pH
Appl. Biochem. Biotechnol.
160
2187-2197
2010
Aspergillus niger
Manually annotated by BRENDA team
Courjean, O.; Mano, N.
Recombinant glucose oxidase from Penicillium amagasakiense for efficient bioelectrochemical applications in physiological conditions
J. Biotechnol.
151
122-129
2011
Aspergillus niger, Penicillium amagasakiense
Manually annotated by BRENDA team
Wang, Q.; Xu, W.; Wu, P.; Zhang, H.; Cai, C.; Zhao, B.
New insights into the effects of thermal treatment on the catalytic activity and conformational structure of glucose oxidase studied by electrochemistry, IR spectroscopy, and theoretical calculation
J. Phys. Chem. B
114
12754-12764
2010
Aspergillus niger
Manually annotated by BRENDA team
Maruthasalam, S.; Liu, Y.L.; Sun, C.M.; Chen, P.Y.; Yu, C.W.; Lee, P.F.; Lin, C.H.
Constitutive expression of a fungal glucose oxidase gene in transgenic tobacco confers chilling tolerance through the activation of antioxidative defence system
Plant Cell Rep.
29
1035-1048
2010
Aspergillus niger
Manually annotated by BRENDA team
Cao, X.; Li, Y.; Zhang, Z.; Yu, J.; Qian, J.; Liu, S.
Catalytic activity and stability of glucose oxidase/horseradish peroxidase co-confined in macroporous silica foam
Analyst
137
5785-5791
2012
Aspergillus niger
Manually annotated by BRENDA team
Ritter, D.W.; Roberts, J.R.; McShane, M.J.
Glycosylation site-targeted PEGylation of glucose oxidase retains native enzymatic activity
Enzyme Microb. Technol.
52
279-285
2013
Aspergillus niger
Manually annotated by BRENDA team
Kagan, M.; Kivirand, K.; Rinken, T.
Modulation of enzyme catalytic properties and biosensor calibration parameters with chlorides: Studies with glucose oxidase
Enzyme Microb. Technol.
53
278-282
2013
Aspergillus niger
Manually annotated by BRENDA team
Holland, J.T.; Lau, C.; Brozik, S.; Atanassov, P.; Banta, S.
Engineering of glucose oxidase for direct electron transfer via site-specific gold nanoparticle conjugation
J. Am. Chem. Soc.
133
19262-19265
2011
Aspergillus niger
Manually annotated by BRENDA team
Seehuber, A.; Dahint, R.
Conformation and activity of glucose oxidase on homogeneously coated and nanostructured surfaces
J. Phys. Chem. B
117
6980-6989
2013
Aspergillus niger
Manually annotated by BRENDA team
Zhang, Y.; Rochefort, D.
Activity, conformation and thermal stability of laccase and glucose oxidase in poly(ethyleneimine) microcapsules for immobilization in paper
Process Biochem.
46
993-1000
2011
Aspergillus niger
-
Manually annotated by BRENDA team
Wohlfahrt, G.; Witt, S.; Hendle, J.; Schomburg, D.; Kalisz, H.M.; Hecht, H.J.
1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes
Acta Crystallogr. Sect. D
55
969-977
1999
Aspergillus niger (P13006), Aspergillus niger, Penicillium amagasakiense (P81156), Penicillium amagasakiense
Manually annotated by BRENDA team
Kalisz, H.M.; Hecht, H.J.; Schomburg, D.; Schmid, R.D.
Effects of carbohydrate depletion on the structure, stability and activity of glucose oxidase from Aspergillus niger
Biochim. Biophys. Acta
1080
138-142
1991
Aspergillus niger (P13006), Aspergillus niger
Manually annotated by BRENDA team
Hecht, H.J.; Schomburg, D.; Kalisz, H.; Schmid, R.D.
The 3D structure of glucose oxidase from Aspergillus niger. Implications for the use of GOD as a biosensor enzyme
Biosens. Bioelectron.
8
197-203
1993
Aspergillus niger (P13006), Aspergillus niger
Manually annotated by BRENDA team
Meyer, M.; Wohlfahrt, G.; Knblein. J.; Schomburg, D.
Aspects of the mechanism of catalysis of glucose oxidase: a docking, molecular mechanics and quantum chemical study
J. Comput. Aided Mol. Des.
12
425-440
1998
Aspergillus niger (P13006)
Manually annotated by BRENDA team
Mecheri, B.; De Porcellinis, D.; Campana, P.T.; Rainer, A.; Trombetta, M.; Marletta, A.; Oliveira, O.N.; Licoccia, S.
Tuning structural changes in glucose oxidase for enzyme fuel cell applications
ACS Appl. Mater. Interfaces
7
28311-28318
2015
Aspergillus niger
Manually annotated by BRENDA team
Ansari, Z.; Karimi, A.; Ebrahimi, S.; Emami, E.
Improvement in ligninolytic activity of Phanerochaete chrysosporium cultures by glucose oxidase
Biochem. Eng. J.
105
332-338
2016
Aspergillus niger (P13006)
-
Manually annotated by BRENDA team
Yu, J.; Zhang, Y.; Liu, S.
Enzymatic reactivity of glucose oxidase confined in nanochannels
Biosens. Bioelectron.
55
307-312
2014
Aspergillus niger
Manually annotated by BRENDA team
Halalipour, A.; Duff, M.R.; Howell, E.E.; Reyes-De-Corcuera, J.I.
Glucose oxidase stabilization against thermal inactivation using high hydrostatic pressure and hydrophobic modification
Biotechnol. Bioeng.
114
516-525
2017
Aspergillus niger (P13006)
Manually annotated by BRENDA team
Zia, M.; Riaz, A.; Rasul, S.; Abbas, R.
Evaluation of antimicrobial activity of glucose oxidase from Aspergillus niger EBL-A and Penicillium notatum
Braz. Arch. Biol. Technol.
56
956-961
2013
Aspergillus niger, Penicillium chrysogenum (K9L4P7), Aspergillus niger EBL-A
-
Manually annotated by BRENDA team
Balistreri, N.; Gaboriau, D.; Jolivalt, C.; Launay, F.
Covalent immobilization of glucose oxidase on mesocellular silica foams Characterization and stability towards temperature and organic solvents
J. Mol. Catal. B
127
26-33
2016
Aspergillus niger (P13006)
-
Manually annotated by BRENDA team
Xu, G.; Xu, Y.; Li, A.; Chen, T.; Liu, J.
Enzymatic bioactivity investigation of glucose oxidase modified with hydrophilic or hydrophobic polymers via in situ RAFT polymerization
J. Polym. Sci. A
55
1289-1293
2017
Aspergillus niger
-
Manually annotated by BRENDA team
Meng, Y.; Zhao, M.; Yang, M.; Zhang, Q.; Hao, J.; Meng, Y.
Production and characterization of recombinant glucose oxidase from Aspergillus niger expressed in Pichia pastoris
Lett. Appl. Microbiol.
58
393-400
2014
Aspergillus niger (Q0PGS3), Aspergillus niger, Aspergillus niger ATCC 9029 (Q0PGS3)
Manually annotated by BRENDA team
Kovacevic, G.; Blazic, M.; Draganic, B.; Ostafe, R.; Gavrovic-Jankulovic, M.; Fischer, R.; Prodanovic, R.
Cloning, heterologous expression, purification and characterization of M12 mutant of Aspergillus niger glucose oxidase in yeast Pichia pastoris KM71H
Mol. Biotechnol.
56
305-311
2014
Aspergillus niger (P13006), Aspergillus niger
Manually annotated by BRENDA team
Sim, H.J.; Kim, J.H.; Kook, S.H.; Lee, S.Y.; Lee, J.C.
Glucose oxidase facilitates osteogenic differentiation and mineralization of embryonic stem cells through the activation of Nrf2 and ERK signal transduction pathways
Mol. Cell. Biochem.
419
157-163
2016
Aspergillus niger (P13006)
Manually annotated by BRENDA team
Marin-Navarro, J.; Roupain, N.; Talens-Perales, D.; Polaina, J.
Identification and structural analysis of amino acid substitutions that increase the stability and activity of Aspergillus niger glucose oxidase
PLoS ONE
10
e0144289
2015
Aspergillus niger (A0A068CB13), Aspergillus niger, Aspergillus niger CECT 2775 (A0A068CB13)
Manually annotated by BRENDA team
Tribst, A.A.; Cota, J.; Murakami, M.T.; Cristianini, M.
Effects of high pressure homogenization on the activity, stability, kinetics and three-dimensional conformation of a glucose oxidase produced by Aspergillus niger
PLoS ONE
9
e103410
2014
Aspergillus niger
Manually annotated by BRENDA team
Blazic, M.; Kovacevic, G.; Prodanovic, O.; Ostafe, R.; Gavrovic-Jankulovic, M.; Fischer, R.; Prodanovic, R.
Yeast surface display for the expression, purification and characterization of wild-type and B11 mutant glucose oxidases
Protein Expr. Purif.
89
175-180
2013
Aspergillus niger (P13006), Aspergillus niger
Manually annotated by BRENDA team
Jithendar, T.; Sairam, K.; Verma, V.
Research journal of pharmaceutical, biological and chemical sciences purification, characterization, thermostability and shelf life studies of glucose oxidase from Aspergillus niger PIL7
Res. J. Pharm. Biol. Chem. Sci.
6
1666-1678
2015
Aspergillus niger, Aspergillus niger PIL7
-
Manually annotated by BRENDA team
Vuong, T.V.; Foumani, M.; MacCormick, B.; Kwan, R.; Master, E.R.
Direct comparison of gluco-oligosaccharide oxidase variants and glucose oxidase substrate range and H2O2 stability
Sci. Rep.
6
37356
2016
Aspergillus niger (Q9HFQ1)
Manually annotated by BRENDA team
Sattari, Z.; Pourfaizi, H.; Dehghan, G.; Amani, M.; Moosavi-Movahedi, A.
Thermal inactivation and conformational lock studies on glucose oxidase
Struct. Chem.
24
1105-1110
2013
Aspergillus niger (P13006)
-
Manually annotated by BRENDA team
Yu, E.; Prodanovic, R.; Gven, G.; Ostafe, R.; Schwaneberg, U.
Electrochemical oxidation of glucose using mutant glucose oxidase from directed protein evolution for biosensor and biofuel cell applications
Appl. Biochem. Biotechnol.
165
1448-1457
2011
Aspergillus niger (P13006)
Manually annotated by BRENDA team
Won, K.; Kim, Y.; An, S.; Lee, H.; Park, S.; Choi, Y.; Kim, J.; Hwang, H.; Kim, H.; Kim, H.; Lee, S.
Glucose oxidase/cellulose-carbon nanotube composite paper as a biocompatible bioelectrode for biofuel cells
Appl. Biochem. Biotechnol.
171
1194-1202
2013
Aspergillus niger (P13006)
Manually annotated by BRENDA team
Zhao, X.; Jia, H.; Kim, J.; Wang, P.
Kinetic limitations of a bioelectrochemical electrode using carbon nanotube-attached glucose oxidase for biofuel cells
Biotechnol. Bioeng.
104
1068-1074
2009
Aspergillus niger (P13006)
Manually annotated by BRENDA team
Fischback, M.; Kwon, K.; Lee, I.; Shin, S.; Park, H.; Kim, B.; Kwon, Y.; Jung, H.; Kim, J.; Ha, S.
Enzyme precipitate coatings of glucose oxidase onto carbon paper for biofuel cell applications
Biotechnol. Bioeng.
109
318-324
2012
Aspergillus niger (P13006)
Manually annotated by BRENDA team
La Rotta H., C.; Ciniciato, G.; Gonzalez, E.
Triphenylmethane dyes, an alternative for mediated electronic transfer systems in glucose oxidase biofuel cells
Enzyme Microb. Technol.
48
487-497
2011
Aspergillus niger (P13006)
Manually annotated by BRENDA team
Yamamoto, K.; Matsumoto, T.; Shimada, S.; Tanaka, T.; Kondo, A.
Starchy biomass-powered enzymatic biofuel cell based on amylases and glucose oxidase multi-immobilized bioanode
New Biotechnol.
30
531-535
2013
Aspergillus niger (P13006)
Manually annotated by BRENDA team
Petrovic, D.; Frank, D.; Kamerlin, S.C.L.; Hoffmann, K.; Strodel, B.
Shuffling active site substate populations affects catalytic activity the case of glucose oxidase
ACS Catal.
7
6188-6197
2017
Aspergillus niger (P13006)
Manually annotated by BRENDA team
Mano, N.
Engineering glucose oxidase for bioelectrochemical applications
Bioelectrochemistry
128
218-240
2019
Aspergillus niger (P13006), Penicillium amagasakiense (P81156)
Manually annotated by BRENDA team
Halalipour, A.; Duff, M.R.; Howell, E.E.; Reyes-De-Corcuera, J.I.
Catalytic activity and stabilization of phenyl-modified glucose oxidase at high hydrostatic pressure
Enzyme Microb. Technol.
137
109538
2020
Aspergillus niger (P13006)
Manually annotated by BRENDA team
Belyad, F.; Karkhanei, A.A.; Raheb, J.
Expression, characterization and one step purification of heterologous glucose oxidase gene from Aspergillus niger ATCC 9029 in Pichia pastoris
EuPA Open Proteom.
19
1-5
2018
Aspergillus niger (P13006), Aspergillus niger ATCC 9029 (P13006), Aspergillus niger ATCC 9029
Manually annotated by BRENDA team
Gau, E.; Flecken, F.; Ksiazkiewicz, A.; Pich, A.
Enzymatic synthesis of temperature-responsive poly(N-vinylcaprolactam) microgels with glucose oxidase
Green Chem.
20
431-439
2018
Aspergillus niger (P13006)
-
Manually annotated by BRENDA team
Jiang, P.; Liu, H.; Zhao, X.; Ding, Q.
Physicochemical properties of soybean protein isolate affected by the cross-linking with horseradish peroxidase, glucose oxidase and glucose
J. Food Meas. Charact.
11
1196-1202
2017
Aspergillus niger (P13006)
-
Manually annotated by BRENDA team
Sedlak, E.; Sedlakova, D.; Marek, J.; Hancar, J.; Garajova, K.; Zoldak, G.
Ion-specific protein/water interface determines the Hofmeister effect on the kinetic stability of glucose oxidase
J. Phys. Chem. B
123
7965-7973
2019
Aspergillus niger (P13006), Aspergillus niger
Manually annotated by BRENDA team
Khadivi Derakshan, F.; Darvishi, F.; Dezfulian, M.; Madzak, C.
Expression and characterization of glucose oxidase from Aspergillus niger in Yarrowia lipolytica
Mol. Biotechnol.
59
307-314
2017
Aspergillus niger (P13006), Aspergillus niger, Aspergillus niger ATCC 9202 (P13006)
Manually annotated by BRENDA team
Wang, Y.; Wang, J.; Leng, F.; Ma, J.; Bagadi, A.
Expression of Aspergillus niger glucose oxidase in Pichia pastoris and its antimicrobial activity against Agrobacterium and Escherichia coli
PeerJ
8
e9010
2020
Aspergillus niger (E3VW38), Aspergillus niger, Aspergillus niger ZM-8 (E3VW38)
Manually annotated by BRENDA team
Jagathy, K.; Kalpana, K.; Rajeshkumar, S.
Production, optimization, characterization and immobilization of glucose oxidase from Aspergillus species
Res. J. Pharm. Technol.
10
1924-1928
2017
Aspergillus niger, Aspergillus niger PIL7
-
Manually annotated by BRENDA team
Kang, Z.; Jiao, K.; Yu, C.; Dong, J.; Peng, R.; Hu, Z.; Jiao, S.
Direct electrochemistry and bioelectrocatalysis of glucose oxidase in CS/CNC film and its application in glucose biosensing and biofuel cells
RSC Adv.
7
4572-4579
2017
Aspergillus niger (P13006)
-
Manually annotated by BRENDA team
Wu, Y.; Chu, L.; Liu, W.; Jiang, L.; Chen, X.; Wang, Y.; Zhao, Y.
The screening of metal ion inhibitors for glucose oxidase based on the peroxidase-like activity of nano-Fe3O4
RSC Adv.
7
47309-47315
2017
Aspergillus niger (P13006)
-
Manually annotated by BRENDA team