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Information on EC 1.1.3.4 - glucose oxidase
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1.1.3.4 glucose oxidaseIUBMB Comments
A flavoprotein (FAD).
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Word Map
- 1.1.3.4
-
electrode
-
biosensors
-
electrochemical
-
fabric
-
amperometric
- nanoparticles
-
film
- gold
- horseradish
-
biosensing
-
voltammetry
-
nanotube
- niger
-
electrocatalytic
-
biocompatibility
-
glassy
-
gluconic
-
entrap
- hydrogel
- platinum
-
nanostructures
-
layer-by-layer
-
graphene
-
electroactive
-
nanocomposite
-
electrochemistry
-
multiwalled
-
immunosensors
-
co-immobilized
-
sol-gel
-
polypyrrole
-
mesoporous
-
prussian
-
peroxidase-like
-
nafion
-
electrodeposition
- ferrocene
-
bioelectrocatalytic
-
screen-printed
- synthesis
-
biocomposite
- diagnostics
- biotechnology
-
polyaniline
- biofuel production
- industry
- pharmaceutical industry
- analysis
-
metal-organic
-
paper-based
-
nanozymes
- food industry
-
nanosheets
- energy production
-
microa
- agriculture
-
glucose-responsive
- 3,3',5,5'-tetramethylbenzidine
-
as-prepared
-
photoelectrochemical
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
glucose oxidase, d-glucose oxidase, microcid, goxp5, cngoxa, beta-d-glucose oxidase, ygoxpenag, notatin, glucose aerodehydrogenase, beta-d-glucose oxygen 1-oxidoreductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AldO
beta-D-glucose oxidase
-
-
-
-
beta-D-glucose/oxygen 1-oxidoreductase
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-1-oxidoreductase
beta-D-glucose:quinone oxidoreductase
-
-
-
-
CngoxA
corylophyline
-
-
-
-
D-glucose oxidase
-
-
-
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D-glucose-1-oxidase
-
-
-
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deoxin-1
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-
-
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glucose aerodehydrogenase
-
-
-
-
glucose oxyhydrase
-
-
-
-
GO-2
GOD
GOX
microcid
-
-
-
-
notatin
-
-
-
-
oxidase, glucose
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-
-
-
penatin
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-
-
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additional information
GOD
-
-
-
-
GOX
-
-
GOX
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2
stereochemistry
-
beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2
catalytic mechanism and stereoselectivity, substrate binding occurs through a lock-and-key mechanism and does not induce conformational changes with respect to the ligand-free protein, overview
-
beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2
proposed mechanism for the oxidation of 1,2-diols to the alpha-hydroxy acids, overview
-
beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2
catalytic mechanism and stereoselectivity, substrate binding occurs through a lock-and-key mechanism and does not induce conformational changes with respect to the ligand-free protein, overview
-
-
beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2
proposed mechanism for the oxidation of 1,2-diols to the alpha-hydroxy acids, overview
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-
beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
beta-D-glucose:oxygen 1-oxidoreductase
A flavoprotein (FAD).
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CAS REGISTRY NUMBER
COMMENTARY
9001-37-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-1-phenyl-1,2-ethanediol + O2
(2R)-hydroxy(phenyl)ethanoic acid + H2O2
-
-
product identification by NMR
-
?
1,2-pentanediol + O2
2-hydroxypentanoate + H2O2
-
-
product identification by NMR
-
?
1,3-butanediol + O2
2-hydroxypropanal + H2O2
-
-
product identification by GC-MS
-
?
1-phenyl-1,2-ethanediol + O2
hydroxy(phenyl)ethanoic acid + H2O2
-
-
-
-
r
2-deoxy-6-fluoro-D-glucose + O2 + H2O
2-deoxy-6-fluoro-D-glucono-1,5-lactone + H2O2
-
1.85% relative activity to beta-D-glucose
-
?
2-deoxy-D-glucose + O2
?
19.6% of the activity with D-glucose for the native enzyme, 5.9 for the recombinant enzyme
-
-
?
3,6-methyl-D-glucose + O2 + H2O
3,6-methyl-D-glucono-1,5-lactone + H2O2
-
1.85% relative activity to beta-D-glucose
-
?
3-deoxy-D-glucose + O2 + H2O
3-deoxy-D-glucono-1,5-lactone + H2O2
-
1% relative activity to D-glucose
-
?
4,6-methyl-D-glucose + O2 + H2O
4,6-methyl-D-glucono-1,5-lactone + H2O2
-
1.22% relative activity to beta-D-glucose
-
?
4-deoxy-d-glucose + O2
? + H2O2
-
7% of the activity compared to beta-D-glucose
-
-
?
4-deoxy-D-glucose + O2 + H2O
4-deoxy-D-glucono-1,5-lactone + H2O2
-
2% relative activity to D-glucose
-
?
4-O-methy-D-glucose + O2 + H2O
4-O-methyl-D-glucono-1,5-lactone + H2O2
-
15% relative activity to D-glucose
-
?
4-O-methyl-D-glucose + O2
4-O-methyl-D-glucono-1,5-lactone + H2O2
-
8% activity compared to beta-D-glucose
-
-
?
4-O-methyl-D-glucose + O2
? + H2O2
-
8% of the activity compared to beta-D-glucose
-
-
?
6-deoxy-6-fluoro-D-glucose + O2 + H2O
6-deoxy-6-fluoro-D-glucono-1,5-lactone + H2O2
-
3% relative activity to beta-D-glucose, when determined with an unspecified enzyme at 0.5 M substrate concentration
-
?
6-deoxy-D-glucose + O2
6-deoxy-D-glucono-1,5-lactone + H2O2
-
12% activity compared to beta-D-glucose
-
-
?
6-deoxy-d-glucose + O2
? + H2O2
-
12% of the activity compared to beta-D-glucose
-
-
?
6-deoxy-D-glucose + O2 + H2O
6-deoxy-D-glucono-1,5-lactone + H2O2
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10% relative activity to D-glucose
-
?
6-O-methyl-D-glucose + O2 + H2O
6-O-methyl-D-glucono-1,5-lactone + H2O2
-
1% relative activity to D-glucose
-
?
alpha-methyl-D-glucoside + O2 + H2O
? + H2O2
-
13% relative activity to D-glucose
-
?
beta-D-glucose + 1,2-naphthoquinone-4-sulfonic acid
D-glucono-1,5-lactone + ?
-
-
-
-
?
beta-D-glucose + 4-benzoquinone
D-glucono-1,5-lactone + 4-benzoquinol
-
-
-
-
r
beta-D-glucose + benzoquinone
D-glucono-1,5-lactone + hydroquinone
-
enzyme immobilized onto alumina
immobilized enzyme, yield of conversion: 100%
?
beta-D-glucose + methyl-1,4-benzoquinone
D-glucono-1,5-lactone + ?
-
-
-
-
?
beta-D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + ?
-
-
-
-
?
beta-D-glucose + potassium ferricyanide
D-glucono-1,5-lactone + ?
-
-
-
-
?
cellobiose + O2 + H2O
? + H2O2
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13% relative activity to D-glucose
-
?
D-fructose + O2
?
4.9% of the activity with D-glucose for the native enzyme, no activity with the recombinant enzyme
-
-
?
D-fructose + O2 + H2O
? + H2O2
-
4.9% relative activity to D-glucose
-
?
D-glucono-1,5-lactone + O2 + H2O
? + H2O2
-
80% relative activity to D-glucose
-
?
D-glucose + di-(2,2'-bipyridinyl)ruthenium(III)dichloride
D-glucono-1,5-lactone + di-(2,2'-bipyridinyl)ruthenium(II)dichloride
-
-
-
-
?
D-glucose + [(1,10-phenanthroline)2(Cl)2Ru(III)]
D-glucono-1,5-lactone + [(1,10-phenanthroline)2(Cl)2Ru(II)]
-
-
-
-
?
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-
-
-
-
-
?
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)]
-
-
-
-
?
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-
-
-
-
-
?
D-glucose + [(2,2'-bipyridine)2(CO32-)1/2Ru(III)]
D-glucono-1,5-lactone + [(2,2'-bipyridine)2(CO32-)1/2Ru(II)]
-
-
-
-
?
D-glucose + [(2,2'-bipyridine)2(H2O)2Ru(III)]PF6-
D-glucono-1,5-lactone + [(2,2'-bipyridine)2(H2O)2Ru(II)]PF6-
-
-
-
-
?
D-glucose + [(2,2'-bipyridine)2(SCN-)2Ru(III)]
D-glucono-1,5-lactone + [(2,2'-bipyridine)2(SCN-)2Ru(II)]
-
-
-
-
?
D-glucose + [(2,2'-bipyridine)3Ru(II)]PF6-
D-glucono-1,5-lactone + [(2,2'-bipyridine)3Ru(III)]PF6-
-
-
-
-
?
D-glucosone + O2 + H2O
? + H2O2
-
30% relative activity to beta-D-glucose
-
?
galactose + O2 + H2O
D-galactono-1,5-lactone + H2O2
-
18% of the activity with beta-D-glucose
-
-
?
L-gulono-gamma-lactone + O2 + H2O
? + H2O2
-
62% relative activity to D-glucose
-
?
maltose + O2
?
21.3% of the activity with D-glucose for the native enzyme, 42.2% for the recombinant enzyme
-
-
?
2-deoxy-D-glucose + O2
2-deoxy-D-glucono-1,5-lactone + H2O2
-
10% activity compared to beta-D-glucose
-
-
?
2-deoxy-D-glucose + O2
2-deoxy-D-glucono-1,5-lactone + H2O2
-
10% activity compared to beta-D-glucose
-
-
?
2-deoxy-d-glucose + O2
? + H2O2
-
10% of the activity compared to beta-D-glucose
-
-
?
2-deoxy-d-glucose + O2
? + H2O2
-
10% of the activity compared to beta-D-glucose
-
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
-
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
20% relative activity to D-glucose
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
30% relative activity to beta-D-glucose
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
25% relative activity to beta-D-glucose
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
low GOD activity
-
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
recombinant enzyme
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
25% relative activity to beta-D-glucose, when determined with a commercial preparation of the enzyme at 0.1 M substrate concentration, 12% relative activity to beta-D-glucose, when determined with a commercial preparation of glucose oxidase, containing catalase, at 0.05 M substrate concentration
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
38% relative activity to D-glucose
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
36% of the activity with beta-D-glucose
-
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
36% of the activity with beta-D-glucose
-
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
19.6% relative activity to D-glucose
-
?
3,6-methyl-D-glucose + O2
3-O,6-O-dimethyl-D-glucono-1,5-lactone + H2O2
-
10% activity compared to beta-D-glucose
-
-
?
3,6-methyl-D-glucose + O2
3-O,6-O-dimethyl-D-glucono-1,5-lactone + H2O2
-
10% activity compared to beta-D-glucose
-
-
?
3,6-methyl-D-glucose + O2
? + H2O2
-
10% of the activity compared to beta-D-glucose
-
-
?
3,6-methyl-D-glucose + O2
? + H2O2
-
10% of the activity compared to beta-D-glucose
-
-
?
4-deoxy-D-glucose + O2
4-deoxy-D-glucono-1,5-lactone + H2O2
-
7% activity compared to beta-D-glucose
-
-
?
4-deoxy-D-glucose + O2
4-deoxy-D-glucono-1,5-lactone + H2O2
-
7% activity compared to beta-D-glucose
-
-
?
alpha-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
0.64% relative activity to beta-D-glucose
-
?
alpha-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
very slow reaction
-
?
beta-D-glucose + 1,4-benzoquinone
D-glucono-1,5-lactone + hydroquinone
-
-
-
-
?
beta-D-glucose + 1,4-benzoquinone
D-glucono-1,5-lactone + hydroquinone
-
-
-
-
?
beta-D-glucose + 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
beta-D-glucose + 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
beta-D-glucose + 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
electrocatalytical reduction of hydrogen peroxide derived from glucose oxidase, biochemical reactivity of glucose oxidase imaged by Scanning electrochemical microscopy, Prussian Blue film modified disk ultramicroelectrode
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
glucose oxidase used as a model protein for immobilization on a conducting polymer surface bearing abundant carboxyl groups, cyclic voltammetry applied to probe response to glucose
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
immobilization of biocatalysts in a membranous form, glucose oxidase as a model protein for biosensor analysis
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
multilayer films of glucose oxidase (GOX) and poly(dimethyl diallyl ammonium chloride, PDDA) prepared by layer-by-layer deposition and analyzed by Scanning electrochemical microscopy
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
GOx enzyme catalyzes the oxidation of glucose to gluconolactone via reduction of the FAD cofactor to FADH2. The reoxidation of FADH2 in the ping-pong mechanism is normally achieved using oxygen as the electron acceptor
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
D-glucose is oxidised at a much faster rate than 2-deoxy-D-glucose and D-mannose, whereas L-glucose, D-galactose, D-arabinose, D-xylose are not oxidised
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
cofactor FAD is transiently reduced along the reaction mechanism
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
enzymatic oxidation by glucose oxidase reduces FAD to FADH2, releasing H2O2 in the presence of O2
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
enzyme assay using the ABTS/horseradish peroxidase system
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
the enzyme is highly specific for D-glucose
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
the reaction can be divided into reductive and oxidative step. In the reductive half of the reaction, beta-D-glucose is oxidized to D-glucono-1,5-lactone, subsequently hydrolyzed to gluconic acid, with simultaneous reduction of FAD to FADH2. In the oxidative half of the reaction, FADH2 in GOx is re-oxidized by oxygen to yield H2O2
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
the addition of ferrous ions (Fe2+) induces the formation of hydroxyl radicals from the hydrogen peroxide, which act as initiating species for the microgel synthesis
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
cofactor FAD is transiently reduced along the reaction mechanism
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
enzymatic oxidation by glucose oxidase reduces FAD to FADH2, releasing H2O2 in the presence of O2
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
activities toward 2-deoxy-D-glucose, galactose and maltose are negligible when compared to the beta-D-glucose. The enzyme (GOD) does not show any activity toward arabinose, lactose, fructose, xylose and sucrose
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Aspergillus tubingensis CTM 507
-
activities toward 2-deoxy-D-glucose, galactose and maltose are negligible when compared to the beta-D-glucose. The enzyme (GOD) does not show any activity toward arabinose, lactose, fructose, xylose and sucrose
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
kinetic studies on the oxidation of beta-D-glucose combined with molecular modelling show the side chain of Arg516, which forms two hydrogen bonds with the 3-OH group of beta-D-glucose, to be absolutely essential for the efficient binding of beta-D-glucose. Of the residues forming the active site of glucose oxidase, Arg516 is the most critical amino acid for the efficient binding of beta-D-glucose by the enzyme, whereas aromatic residues at positions 73, 418 and 430 are important for the correct orientation and maximal velocity of glucose oxidation
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
kinetic studies on the oxidation of beta-D-glucose combined with molecular modelling show the side chain of Arg516, which forms two hydrogen bonds with the 3-OH group of beta-D-glucose, to be absolutely essential for the efficient binding of beta-D-glucose. Of the residues forming the active site of glucose oxidase, Arg516 is the most critical amino acid for the efficient binding of beta-D-glucose by the enzyme, whereas aromatic residues at positions 73, 418 and 430 are important for the correct orientation and maximal velocity of glucose oxidation
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
enzymatic oxidation by glucose oxidase reduces FAD to FADH2, releasing H2O2 in the presence of O2
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
via cofactor FAD reduction to FADH2, reaction cycles, FADH2 reduces O2, overview
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
via cofactor FAD reduction to FADH2, reaction cycles, FADH2 reduces O2, overview
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
the beta-D-glucose serves as a donor of electrons and hydrogen ions, on other side of this complex reaction, oxygen dissolved in water-based reaction media is as an acceptor. Coenzyme FAD acts as electron shuttle during catalytic action of the enzyme, FAD is converted to FADH2
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
the beta-D-glucose serves as a donor of electrons and hydrogen ions, on other side of this complex reaction, oxygen dissolved in water-based reaction media is as an acceptor. Coenzyme FAD acts as electron shuttle during catalytic action of the enzyme, FAD is converted to FADH2
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
654185, 654659, 656782, 695600, 696068, 696777, 696864, 696884, 699078, 699771, 699922, 699941, 700599, 710858, 710908, 712533, 712857, 713259
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
highly specific
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
soluble enzyme and immobilized enzyme on collagen
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
kinetic mechanism
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
glucose is the primary substrate for the enzyme
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
glucose is the primary substrate for the enzyme
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
glucose is the primary substrate for the enzyme
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
native enzyme and enzyme immobilized on activated carbon
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
the enzyme can use 2,6-dichlorophenolindophenol as hydrogen acceptor in addition to oxygen, the rate of glucose oxidation in the presence of 2,6-dichlorophenolindophenol is only 3.3% of that in the presence of oxygen
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
hydrogel microspheres of crosslinked poly(hydroxyethyl methylacrylate-co-dimethylaminoethyl methacrylate) are used for physical and covalent immobilization. Matrix entrapment (physical immobilization) affords the higher loading capacity and higher specific activity of the immobilized enzyme. The substrate has almost solution-like access to the immobilized enzyme within the microsphere and the hydrogel presents no significant diffusional barrier to enzyme-substrate reaction. Two functional groups, imidazolium and sulfhydryl, of His and Cys respectively, may be involved at the active site for the oxidation of glucose
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
GOD is highly specific for the beta-anomer of D-glucose
-
-
ir
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
native enzyme and enzyme immobilized on mycelium pellets
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
native enzyme and enzyme immobilized on mycelium pellets
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
in a subsequent step D-glucono-1,5-lactone is nonenzymatically hydrolyzed to D-gluconic acid
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
kinetic mechanism
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
glucose is the primary substrate, recombinant enzyme
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
the enzyme can use 2,6-dichlorophenolindophenol as hydrogen acceptor in addition to oxygen, the rate of glucose oxidation in the presence of 2,6-dichlorophenolindophenol is only 3.3% of that in the presence of oxygen
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
highly specific
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
highly specific
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
in a subsequent step D-glucono-1,5-lactone is nonenzymatically hydrolyzed to D-gluconic acid
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
glucose is the primary substrate for the enzyme
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
glucose is the primary substrate for the enzyme
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
2,6-dichloroindophenol, N,N,N',N'-tetramethyl-1,4-phenylenediamine, and 4-benzoquinone can function as electron acceptors
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
glucose is the primary substrate for the enzyme
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
specific for D-glucose, 2,6-dichloroindophenol can act as artificial electron acceptor
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
highly specific
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
highly specific
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
highly specific
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
glucose is the primary substrate for the enzyme
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
highly substrate specific enzyme
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
highly substrate specific enzyme
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
the enzyme is involved in apple fruit tissue browning
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
best substrate
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
best substrate
-
-
?
D-maltose + O2 + H2O
? + H2O2
-
22% of the activity with beta-D-glucose
-
-
?
D-maltose + O2 + H2O
? + H2O2
-
22% of the activity with beta-D-glucose
-
-
?
D-maltose + O2 + H2O
? + H2O2
-
21.3% relative activity to D-glucose
-
?
D-mannose + O2
?
7.2% of the activity with D-glucose for the native enzyme, 13.4 for the recombinant enzyme
-
-
?
D-mannose + O2
?
7.2% of the activity with D-glucose for the native enzyme, 13.4 for the recombinant enzyme
-
-
?
D-xylose + O2
?
3.0% of the activity with D-glucose for the native enzyme, 5.8 for the recombinant enzyme
-
-
?
D-xylose + O2
?
3.0% of the activity with D-glucose for the native enzyme, 5.8 for the recombinant enzyme
-
-
?
D-xylose + O2 + H2O
? + H2O2
-
11% of the activity with beta-D-glucose
-
-
?
D-xylose + O2 + H2O
? + H2O2
-
11% of the activity with beta-D-glucose
-
-
?
L-sorbose + O2
? + H2O2
-
15% of the activity compared to beta-D-glucose
-
-
?
L-sorbose + O2
? + H2O2
-
15% of the activity compared to beta-D-glucose
-
-
?
mannose + O2
? + H2O2
-
9% of the activity compared to beta-D-glucose
-
-
?
mannose + O2
? + H2O2
-
9% of the activity compared to beta-D-glucose
-
-
?
mannose + O2 + H2O
? + H2O2
-
9% relative activity to D-glucose
-
?
mannose + O2 + H2O
? + H2O2
-
7.2% relative activity to D-glucose
-
?
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
-
-
?
additional information
?
-
-
analysis of interaction of the enzyme with complexes of pentacyanoferrate(III) and nucleophilic ligands ammonia, imidazole or pyrazole, overview
-
-
?
additional information
?
-
-
the enzyme binds to concanavalin A forming insoluble complexes, overview
-
-
?
additional information
?
-
-
alpha-D-glucose is not a suitable substrate
-
-
?
additional information
?
-
His516 plays an important role in the reductive and oxidative half reaction
-
-
?
additional information
?
-
-
construction of a nanodevice coupled with an integrated real-time detection system for evaluation of the function of biomolecules in biological processes, and enzymatic reaction kinetics occurring at the confined space or interface. A nanochannel-enzyme system in which the enzymatic reaction is coupled with an electrochemical method is constructed. The model system is established by covalently linking glucose oxidase (GOD) onto the inner wall of the nanochannels of the porous anodic alumina (PAA)membrane. An gold disc is attached at the end of the nanochannel of the PAA membrane as the working electrode for detection of H2O2 product of enzymatic reaction. The effects of ionic strength, amount of immobilized enzyme and pore diameter of the nanochannels on the enzymatic reaction kinetics are analysed, method evaluation, overview
-
-
?
additional information
?
-
-
no activity with 2-deoxy-6-fluoro-D-glucose, 4,6-dimethyl-D-glucose, beta-deoxy-D-glucose, 6-O-methyl-D-glucose, D-glucono-delta-lactone, L-gulono-gamma-lactone, D-gulono-gamma-lactone, D-glucuronolactone, altrose, galactose, xylose, idose, cellobiose, D-kabinose, L-arabinose, or D-fructose
-
-
?
additional information
?
-
the enzyme is specific for D-glucose, it shows less than 10% activity with trehalose, D-galactose, melibiose, and raffinose compared to D-glucose, no activity with L-mannomethylose, D-fructose, D-xylose, lactose, and sucrose
-
-
?
additional information
?
-
-
the enzyme is specific for D-glucose, it shows less than 10% activity with trehalose, D-galactose, melibiose, and raffinose compared to D-glucose, no activity with L-mannomethylose, D-fructose, D-xylose, lactose, and sucrose
-
-
?
additional information
?
-
the enzyme oxidizes the anomeric carbon of beta-D-glucose using molecular oxygen as an electron acceptor, producing H2O2 and D-glucono-delta-lactone, which in the presence of water spontaneously hydrolyzes to gluconic acid. Poor activity with xylose, maltose, cellobiose, cellotetraose, and xylo-oligosaccharides
-
-
?
additional information
?
-
usage of the nitroso-aniline assay for determination of GOx activity
-
-
?
additional information
?
-
-
usage of the nitroso-aniline assay for determination of GOx activity
-
-
?
additional information
?
-
the enzyme is specific for D-glucose, it shows less than 10% activity with trehalose, D-galactose, melibiose, and raffinose compared to D-glucose, no activity with L-mannomethylose, D-fructose, D-xylose, lactose, and sucrose
-
-
?
additional information
?
-
-
no activity with 2-deoxy-6-fluoro-D-glucose, 4,6-dimethyl-D-glucose, beta-deoxy-D-glucose, 6-O-methyl-D-glucose, D-glucono-delta-lactone, L-gulono-gamma-lactone, D-gulono-gamma-lactone, D-glucuronolactone, altrose, galactose, xylose, idose, cellobiose, D-kabinose, L-arabinose, or D-fructose
-
-
?
additional information
?
-
-
Rab8, Cdc42, Rho1, and Rho4 are associated with enriched vesicles carrying GOX activity
-
-
?
additional information
?
-
-
Rab8, Cdc42, Rho1, and Rho4 are associated with enriched vesicles carrying GOX activity
-
-
?
additional information
?
-
-
characterization of the allergen Mala s12, sequence similarity to glucose-methanol-choline (GMC) oxidoreductase enzyme superfamily, no enzyme activity of the recombinant protein in oxidase or dehydrogenase assay determined
-
-
?
additional information
?
-
-
the enzyme is the predominant source of H2O2 in ligninolytic cultures, H2O2 plays a central role in lignin biodegradation, it is obligately required for the activity of ligninases, a family of lignin peroxidases that is important in the oxidative depolymerization of lignin
-
-
?
additional information
?
-
-
the enzyme is the predominant source of H2O2 in ligninolytic cultures, H2O2 plays a central role in lignin biodegradation, it is obligately required for the activity of ligninases, a family of lignin peroxidases that is important in the oxidative depolymerization of lignin
-
-
?
additional information
?
-
-
AldO catalyzes the C1 oxidation of several polyols
-
-
?
additional information
?
-
-
substrate specificity,besides alditols, 1,2-diols are reasonable substrates indicating that two adjacent hydroxy groups at C-1 and C-2 seem to be a minimal requirement for a compound in order to be effectively oxidized by AldO, overview
-
-
?
additional information
?
-
-
AldO catalyzes the C1 oxidation of several polyols
-
-
?
additional information
?
-
-
substrate specificity,besides alditols, 1,2-diols are reasonable substrates indicating that two adjacent hydroxy groups at C-1 and C-2 seem to be a minimal requirement for a compound in order to be effectively oxidized by AldO, overview
-
-
?
additional information
?
-
-
less than 2.5% of the activity with beta-D-glucose with arabinose, lactose, mannitol, sucrose and fructose
-
-
?
additional information
?
-
-
the enzyme interacts with redox mediators, e.g. 9,10-phenantroline-5,6-dione, 9,10-phenanthrenequinone, N-methylphenazonium methyl sulfate, ferrocene, ferrocenecarboxylic acid, alpha-methylferrocenemethanol, ferrocenecarboxaldehyde. 9,10-phenantroline-5,6-dione and 9,10-phenanthrenequinone are the best redox mediators or electron acceptors for this type of GOx. The redox mediators in a reaction mixture containing glucose, GOx and 1,4-benzoquinone lead to a 1.4-7.9fold rise of the 1,4-benzoquinone reduction rate, method evaluation
-
-
?
additional information
?
-
-
the enzyme interacts with redox mediators, e.g. 9,10-phenantroline-5,6-dione, 9,10-phenanthrenequinone, N-methylphenazonium methyl sulfate, ferrocene, ferrocenecarboxylic acid, alpha-methylferrocenemethanol, ferrocenecarboxaldehyde. 9,10-phenantroline-5,6-dione and 9,10-phenanthrenequinone are the best redox mediators or electron acceptors for this type of GOx. The redox mediators in a reaction mixture containing glucose, GOx and 1,4-benzoquinone lead to a 1.4-7.9fold rise of the 1,4-benzoquinone reduction rate, method evaluation
-
-
?
additional information
?
-
-
less than 2.5% of the activity with beta-D-glucose with arabinose, lactose, mannitol, sucrose and fructose
-
-
?
additional information
?
-
no activity with L-arabinose and D-galactose with the native and recombinant enzyme
-
-
?
additional information
?
-
no activity with L-arabinose and D-galactose with the native and recombinant enzyme
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
GOx enzyme catalyzes the oxidation of glucose to gluconolactone via reduction of the FAD cofactor to FADH2. The reoxidation of FADH2 in the ping-pong mechanism is normally achieved using oxygen as the electron acceptor
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
in a subsequent step D-glucono-1,5-lactone is nonenzymatically hydrolyzed to D-gluconic acid
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
in a subsequent step D-glucono-1,5-lactone is nonenzymatically hydrolyzed to D-gluconic acid
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
the enzyme is involved in apple fruit tissue browning
-
-
?
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
-
-
?
additional information
?
-
-
Rab8, Cdc42, Rho1, and Rho4 are associated with enriched vesicles carrying GOX activity
-
-
?
additional information
?
-
-
Rab8, Cdc42, Rho1, and Rho4 are associated with enriched vesicles carrying GOX activity
-
-
?
additional information
?
-
-
the enzyme is the predominant source of H2O2 in ligninolytic cultures, H2O2 plays a central role in lignin biodegradation, it is obligately required for the activity of ligninases, a family of lignin peroxidases that is important in the oxidative depolymerization of lignin
-
-
?
additional information
?
-
-
the enzyme is the predominant source of H2O2 in ligninolytic cultures, H2O2 plays a central role in lignin biodegradation, it is obligately required for the activity of ligninases, a family of lignin peroxidases that is important in the oxidative depolymerization of lignin
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
flavin
-
both the thermal and chemical denaturation of the enzyme cause dissociation of the flavin cofactor
FAD
-
-
389792, 389802, 389804, 389827, 389836, 389837, 654780, 695790, 696864, 696865, 699078, 699600, 699771, 710858, 712533, 712857, 725199, 741479, 742213, 743644, 743775
FAD
-
defined as flavoprotein oxidase, two very tightly bound FAD molecules per dimer, kinetic behavior
FAD
-
defined as flavoprotein oxidase, two very tightly bound FAD molecules per dimer, kinetic behavior
FAD
-
electron transfer between FAD centers and metal electrodes after chemical modification of enzyme
FAD
-
dissociation of FAD from the holoenzyme is responsible for the thermal inaction of the enzyme
FAD
-
covalently bound to the recombinant protein of Mala s12, flavin content per monomer of protein calculated
FAD
-
a flavoprotein, the flavin cofactor is covalently linked to the polypeptide chain, covalent anchoring of the FAD cofactor is an autocatalytic process and that only occurs upon correct folding of the polypeptide chain
FAD
-
flavin-dependent oxidase with covalently linked FAD which is located at the bottom of a funnel-shaped pocket that forms the active site
FAD
-
each subunit of dimeric GOD contains one tightly bound FAD as cofactor
FAD
dimerization is only possible with the proper incorporation of the cofactor in the FAD-binding pocket
FAD
semiempirical quantum chemical calculations are used to investigate the role of FAD in the catalytic oxidation of glucose. Only the hydride ion is transferred to the FAD coenzyme
FAD
a flavoenzyme with a tightly but non-covalently bound FAD cofactor
FAD
-
coenzyme FAD acts as electron shuttle during catalytic action of the enzyme. The FAD extinction is used for enzyme quantification
FAD
dependent on, the FAD cofactor is not covalently but tightly bound to the enzyme domain, that consists of a five-stranded beta-sheet sandwiched between a three-stranded beta-sheet and three alpha-helices
FAD
each monomer has one co-enzyme molecule of FAD, which acts as an electron receptor during catalysis
FAD
enzyme pen-GOx contains one mol of tightly but not covalently bound FAD cofactor at the active site of each subunit. The FAD-binding domain of GOx is formed by a beta-sheet lid. The lid prevents the release of FAD from the dimer. Loosening of tertiary structure leads to opening of this lid, causing FAD loss anddissociation of the dimer. Loss of FAD from GOx is concurrent with tertiary structure loss. FAD, especially isoalloxazine, is important for the catalytic activity for beta-D-glucose. The binding of FAD cofactor also plays a key role on the catalytic activity of flavoproteins for the correct folding, assembly and protein stability. The three-dimensional structure of the glucose oxidase is stabilized by FAD, which can act as a redox carrier in catalysis
FAD
the active site holds the tightly, non-covalently bound FAD cofactor
additional information
-
specification of the relative contribution of structure and dynamics to the catalytic activity, using infrared absorption spectroscopy of the amide I' band, tryptophan fluorescence quenching and hydrogen isotopic exchange on the oxidized and reduced enzymes
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CuCl2
KCN
Mn2+
5 mM and 10 mM, enzymatic activity of wild-type enzyme is above 100%
additional information
additional information
the enzyme activity is not significantly affected by 2 mM of Mg2+, Ca2+, Mn2+, Ni2+, Al3+, and Zn2+
additional information
-
the enzyme activity is not significantly affected by 2 mM of Mg2+, Ca2+, Mn2+, Ni2+, Al3+, and Zn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
AlCl3
-
inhibits the enzyme at low concentrations of 5 mM, and inhibits it completely at higher salt concentrations over 0.1 M
ammonium chloride
-
mixed-type inhibitor, inhibits glucose oxidase in the culture fluid, glucose oxidase activity decreases by 1.7-1.8times in the presence of 1 M ammonium chloride
Fe3+
10 mM, wild-type enzyme retains approximately 80% of its activity, mutant enzyme Y169C/A211C retains 50-60% activity
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
ribose
-
incubation of Aspergillus niger glucose oxidase with 1 mM ribose for up to 8 days results in 96% loss in activity
Ag+
-
inhibits oxidation of the reduced FAD moiety competing with molecular oxygen as a hydrogen acceptor
Ag+
-
inhibition is explained by the high reactivity of this ion for thiol groups essential for enzymic activity
H2O2
-
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. The glucose oxidase-containing liposomes are completely free of the inhibition even in the complete conversion of 10 mM glucose at 25°C because the H2O2 concentration is kept negligible low both outside and inside liposomes throughout the reaction
Mn2+
5 mM and 10 mM, enzymatic activity of wild-type enzyme is above 100%, mutant enzyme Y169C/A211C retains 50-60% activity
Na+
-
the inhibiting effect of Na+ions is reduced at Na+concentrations over 0.5 M
additional information
-
2.5 or 5 mM N-acetylcysteine prevents glucose/glucose oxidase-induced oxidative stress, mitochondrial damage and apoptosis in H9c2 cells
-
additional information
diethyl dicarbonate, dimethylaminobenzaldehyde, and EDTA do not cause any inhibition at 2 mM. SDS, Tween-20, Tween-80, Triton X-100, NP40, benzalkonium bromide, and sodium cholate do not exhibit a significant effect on the enzyme activity at 2%
-
additional information
-
diethyl dicarbonate, dimethylaminobenzaldehyde, and EDTA do not cause any inhibition at 2 mM. SDS, Tween-20, Tween-80, Triton X-100, NP40, benzalkonium bromide, and sodium cholate do not exhibit a significant effect on the enzyme activity at 2%
-
additional information
a colorimetric method is proposed based on the peroxidase-like activity of Fe3O4 magnetic nanoparticles for screening metal ion inhibitors for glucose oxidase activity. This assay is economical, time-saving and highly-effective with definitely significant reference for the screening of metal ions as glucose oxidase inhibitors
-
additional information
-
glycoprotein from Dioscorea batatas protects mouse thymocytes from glucose/glucose oxidase-induced cell death
-
additional information
-
ammonium sulfate does not inhibit glucose oxidase
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
beta-D-glucose
GOX protein expression levels and GOX enzymatic activities increase with dietary glucose
Blue dextran
-
40% increase of activity as a result of the binding with the enzyme
-
CaCl2
-
immobilized enzyme, activating factor, considerable increase in activity
casein
-
immobilized enzyme, activating factor, considerable increase in activity
CuCl2
-
stimulation of activity, 123% relative activity to no addition
NaF
-
weak stimulation of activity, 111% relative activity to no addition
trehalose
-
trehalose does not affect Vmax but instead decreases Km and as a result enzyme efficiency is increased
KCN
-
stimulation of activity, 135% relative activity to no addition
additional information
-
after fifth-instar plant-fed caterpillars are transferred to an artificial diet, their labial salivary GOX activity increases quickly, sugars and secondary metabolites are the possible causes of induction of GOX activity. Chlorogenic acid, rutin, and quercetin (0.2%, dry weight) in the diets have no effect on GOX activity of labial salivary glands.
-
additional information
-
the enzyme interacts with redox mediators, e.g. 9,10-phenantroline-5,6-dione, 9,10-phenanthrenequinone, N-methylphenazonium methyl sulfate, ferrocene, ferrocenecarboxylic acid, alpha-methylferrocenemethanol, ferrocenecarboxaldehyde. 9,10-phenantroline-5,6-dione and 9,10-phenanthrenequinone are the best redox mediators or electron acceptors for this type of GOx. The redox mediators in a reaction mixture containing glucose, GOx and 1,4-benzoquinone lead to a 1.4-7.9fold rise of the 1,4-benzoquinone reduction rate, method evaluation
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.019
beta-D-glucose
-
native enzyme in solution, pH 5.5, temperature not specified in the publication
0.149
beta-D-glucose
immobilized enzyme, pH and temperature not specified in the publication
1.51 - 3.4
beta-D-glucose
-
depending on O2-concentration, comparison of values with enzyme immobilized on various materials
1.9
beta-D-glucose
-
purified enzyme under argon, in 20 mM phosphate buffer pH 7.4 at 37°C
2.5
beta-D-glucose
-
non-purified enzyme under argon, in 20 mM phosphate buffer pH 7.4 at 37°C
2.5
beta-D-glucose
-
recombinant wild-type enzyme, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme
2.6
beta-D-glucose
-
recombinant mutant K424E, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme
3.2
beta-D-glucose
-
recombinant mutant K424E, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme
3.4
beta-D-glucose
-
recombinant mutant K424I, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme
3.8
beta-D-glucose
-
recombinant wild-type enzyme, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme
4
beta-D-glucose
-
immobilized enzyme, immobilized membrane with ratio stretching 1.25
5.4
beta-D-glucose
-
immobilized enzyme, immobilized membrane with ratio stretching 3
6.3
beta-D-glucose
-
wild-type enzyme conjugated to gold nanoparticles, pH and temperature not specified in the publication
8
beta-D-glucose
-
enzyme adsorbed on 11-(1H-pyrol-11-(1H-pyrol-1-yl)undecane-1-thiol) coated matrix, high enzyme concentration, pH 5.5, temperature not specified in the publication
8.2
beta-D-glucose
-
mutant H447C conjugated to gold nanoparticles, pH and temperature not specified in the publication
10.5
beta-D-glucose
-
in 50 mM sodium acetate buffer (pH 5.4). at 45°C
11.43
beta-D-glucose
recombinant mutant M12 expressed in Pichia pastoris, pH 7.4, 25°C
11.7
beta-D-glucose
-
recombinant enzyme yGOXpenag, using O2 as cosubstrate, pH 6.0, 50°C
11.9
beta-D-glucose
-
purified enzyme under O2, in 20 mM phosphate buffer pH 7.4 at 37°C
12
beta-D-glucose
-
enzyme adsorbed on 11-amino-1-undecanethiol coated matrix, pH 5.5, temperature not specified in the publication
13.33
beta-D-glucose
recombinant mutant M12 enzyme expressed in Pichia pastoris, pH 5.5, 25°C
14.98
beta-D-glucose
pH 5.5, temperature not specified in the publication, mutant enzyme T30V/I94V/A162T
15
beta-D-glucose
-
mutant H447C, pH and temperature not specified in the publication
16.95
beta-D-glucose
recombinant enzyme, in 0.1 M sodium phosphate buffer, pH 6.0, at 35°C
18.1
beta-D-glucose
recombinant mutant M12 enzyme expressed in Saccharomyces cerevisiae, pH 5.5, 25°C
18.2
beta-D-glucose
-
recombinant enzyme yGOXpenag, using ferrocinium-methanol as cosubstrate, pH 6.0, 50°C
18.54
beta-D-glucose
pH 5.5, temperature not specified in the publication, mutant enzyme T30V/I94V/A162T/R537K/M556V
19.76
beta-D-glucose
pH 5.5, temperature not specified in the publication, mutant enzyme T30V/R37K/I94V/V106I/A162T/M556V
22
beta-D-glucose
-
enzyme adsorbed on 11-(1H-pyrol-11-(1H-pyrol-1-yl)undecane-1-thiol) coated matrix, low enzyme concentration, pH 5.5, temperature not specified in the publication
22
beta-D-glucose
-
recombinant mutant K424I, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme
22
beta-D-glucose
recombinant wild-type enzyme expressed in Saccharomyces cerevisiae, pH 5.5, 25°C
23.19
beta-D-glucose
recombinant wild-type enzyme expressed in Pichia pastoris, pH 7.4, 25°C
27.9
beta-D-glucose
recombinant enzyme mutant B11 in fusion with Aga2, pH 5.5, 25°C
28.26
beta-D-glucose
recombinant wild-type enzyme expressed in Pichia pastoris, pH 5.5, 25°C
28.26
beta-D-glucose
pH 5.5, temperature not specified in the publication, wild-type enzyme
33.4
beta-D-glucose
recombinant wild-type enzyme in fusion with Aga2, pH 5.5, 25°C
69
beta-D-glucose
pH 7.0, 20-25°C, mutant enzyme Y169C/A211C
71.2
beta-D-glucose
-
native enzyme, using ferrocinium-methanol as cosubstrate, pH 6.5, 70°C
96.4
beta-D-glucose
-
wild-type enzyme, pH and temperature not specified in the publication
103
beta-D-glucose
pH 7.0, 20-25°C, wild-type enzyme
0.0638
ferrocinium-methanol
-
recombinant enzyme yGOXpenag, pH 6.0, 50°C
additional information
additional information
-
values for glyco-enzyme and aglyco-enzyme
-
additional information
additional information
-
KM-value of immunoaffinity-layered glucose oxidase preparations remains unaltered
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
kinetics of enzyme-pentacyanoferrate(III)-nucleophilic ligands-complex interactions, detailed overview
-
additional information
additional information
-
steady-state kinetics, overview
-
additional information
additional information
-
choline, glucose, myo-inositol, methanol, ethanol, 1-pentanol, benzyl alcohol, 2-phenylethanol, cholesterol or lauryl alcohol tested as potential substrates, recombinant protein devoid of either oxidase or dehydrogenase activity
-
additional information
additional information
-
substrate specificity and steady state kinetics, overview
-
additional information
additional information
-
enzyme thermodynamics and kinetics
-
additional information
additional information
Michaelis-Menten kinetics of immobilized enzyme GOx and free enzyme GOx
-
additional information
additional information
kinetic limitations of a bioelectrochemical electrode using carbon nanotube-attached glucose oxidase for biofuel cells. Carbon nanotube-supported glucose oxidase is examined in the presence of 1,4-benzoquinone. The intrinsic Michaelis parameters of the reaction catalyzed by carbon nanotube-glucose-oxidase are very close to those of native enzyme. However, the Nafion entrapment of carbon nanotube-glucose-oxidase for an electrode results in a much lower activity due to the limited availability of the embedded enzyme. Kinetic studies reveal that the biofuel cell employing such an enzyme electrode only generate a power density equivalent to less than 40% of the reaction capability of the enzyme on electrode. Factors such as electron and proton transfer resistances can be more overwhelming than the heterogeneous reaction kinetics in limiting the power generation of such biofuel cells
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.168
beta-D-glucose
-
pH 7, 30°C, 2-ethylhexylsulfosuccinate medium or polyethylene glycol p-tert octyl phenyl ether medium
5.2
beta-D-glucose
-
pH 9.0, 33°C, deglycosylated recombinant enzyme with PEG-5000 reagent
5.5
beta-D-glucose
-
pH 9.0, 33°C, deglycosylated recombinant enzyme with PEG-350 reagent
22.8
beta-D-glucose
-
wild-type enzyme conjugated to gold nanoparticles, pH and temperature not specified in the publication
33.3
beta-D-glucose
recombinant wild-type enzyme in fusion with Aga2, pH 5.5, 25°C
54.8
beta-D-glucose
recombinant wild-type enzyme expressed in Saccharomyces cerevisiae, pH 5.5, 25°C
55.3
beta-D-glucose
-
mutant H447C conjugated to gold nanoparticles, pH and temperature not specified in the publication
61.3
beta-D-glucose
recombinant enzyme mutant B11 in fusion with Aga2, pH 5.5, 25°C
97
beta-D-glucose
pH 7.0, 20-25°C, wild-type enzyme
130.2
beta-D-glucose
recombinant wild-type enzyme expressed in Pichia pastoris, pH 7.4, 25°C
150
beta-D-glucose
recombinant mutant M12 enzyme expressed in Saccharomyces cerevisiae, pH 5.5, 25°C
152
beta-D-glucose
-
wild-type enzyme, pH and temperature not specified in the publication
164
beta-D-glucose
pH 7.0, 20-25°C, mutant enzyme Y169C/A211C
189.38
beta-D-glucose
pH 5.5, temperature not specified in the publication, wild-type enzyme
189.4
beta-D-glucose
recombinant wild-type enzyme expressed in Pichia pastoris, pH 5.5, 25°C
238
beta-D-glucose
-
recombinant wild-type enzyme, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme
245
beta-D-glucose
-
recombinant mutant K424I, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme
250
beta-D-glucose
-
recombinant mutant K424E, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme
257.1
beta-D-glucose
recombinant mutant M12 expressed in Pichia pastoris, pH 7.4, 25°C
291.82
beta-D-glucose
pH 5.5, temperature not specified in the publication, mutant enzyme T30V/I94V/A162T
345.16
beta-D-glucose
pH 5.5, temperature not specified in the publication, mutant enzyme T30V/R37K/I94V/V106I/A162T/M556V
352
beta-D-glucose
recombinant mutant M12 enzyme expressed in Pichia pastoris, pH 5.5, 25°C
425
beta-D-glucose
-
mutant H447C, pH and temperature not specified in the publication
433
beta-D-glucose
-
recombinant mutant K424I, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme
446
beta-D-glucose
pH 5.1, 37°C, unmodified enzyme and aniline-modified enzyme
458
beta-D-glucose
-
recombinant wild-type enzyme, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme
464
beta-D-glucose
-
recombinant mutant K424E, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme
484.3
beta-D-glucose
recombinant enzyme, in 0.1 M sodium phosphate buffer, pH 6.0, at 35°C
498.34
beta-D-glucose
pH 5.5, temperature not specified in the publication, mutant enzyme T30V/I94V/A162T/R537K/M556V
1695
beta-D-glucose
-
recombinant enzyme yGOXpenag, using ferrocinium-methanol as cosubstrate, pH 6.0, 50°C
1808
beta-D-glucose
-
recombinant enzyme yGOXpenag, using O2 as cosubstrate, pH 6.0, 50°C
1938
beta-D-glucose
-
native enzyme, using ferrocinium-methanol as cosubstrate, pH 6.5, 70°C
additional information
additional information
-
in microemulsion medium (water/2-ethylhexylsulfosuccinate/decane) turnover-number values exhibit a deformed W-shaped profile with omega (the water/surfactant mol ratio). At pH 7, a maximum value of turnover-number is observed at omega = 10.6. The turnover numbers are higher in microemulsion medium than in aqueous medium at both pHs 7 and 8
-
additional information
additional information
native enzyme and recombinant enzyme at pH 5.0, 28°C
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.997
beta-D-glucose
recombinant wild-type enzyme in fusion with Aga2, pH 5.5, 25°C
2.2
beta-D-glucose
recombinant enzyme mutant B11 in fusion with Aga2, pH 5.5, 25°C
2.49
beta-D-glucose
recombinant wild-type enzyme expressed in Saccharomyces cerevisiae, pH 5.5, 25°C
5.61
beta-D-glucose
recombinant wild-type enzyme expressed in Pichia pastoris, pH 7.4, 25°C
6.7
beta-D-glucose
recombinant wild-type enzyme expressed in Pichia pastoris, pH 5.5, 25°C
6.7
beta-D-glucose
pH 5.5, temperature not specified in the publication, wild-type enzyme
8.29
beta-D-glucose
recombinant mutant M12 enzyme expressed in Saccharomyces cerevisiae, pH 5.5, 25°C
17.5
beta-D-glucose
pH 5.5, temperature not specified in the publication, mutant enzyme T30V/R37K/I94V/V106I/A162T/M556V
19.5
beta-D-glucose
pH 5.5, temperature not specified in the publication, mutant enzyme T30V/I94V/A162T
22.48
beta-D-glucose
recombinant mutant M12 expressed in Pichia pastoris, pH 7.4, 25°C
26.41
beta-D-glucose
recombinant mutant M12 enzyme expressed in Pichia pastoris, pH 5.5, 25°C
26.9
beta-D-glucose
pH 5.5, temperature not specified in the publication, mutant enzyme T30V/I94V/A162T/R537K/M556V
27
beta-D-glucose
-
native enzyme, using ferrocinium-methanol as cosubstrate, pH 6.5, 70°C
93
beta-D-glucose
-
recombinant enzyme yGOXpenag, using ferrocinium-methanol as cosubstrate, pH 6.0, 50°C
95.2
beta-D-glucose
-
recombinant wild-type enzyme, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme
96
beta-D-glucose
-
recombinant mutant K424E, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme
120
beta-D-glucose
-
recombinant wild-type enzyme, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme
122
beta-D-glucose
-
recombinant mutant K424I, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme
127
beta-D-glucose
-
recombinant mutant K424I, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme
145
beta-D-glucose
-
recombinant mutant K424E, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme
155
beta-D-glucose
-
recombinant enzyme yGOXpenag, using O2 as cosubstrate, pH 6.0, 50°C
0.027
ferrocinium-methanol
-
recombinant enzyme yGOXpenag, pH 6.0, 50°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
39.8
ammonium chloride
-
pH and temperature not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
-
immobilized enzyme, pH 5.5, temperature not specified in the publication, high enzyme concentration
194
-
GOD-His6 expressed in pmr1DELTA mutant cells of Saccharomyces cerevisiae
216
-
immobilized enzyme, pH 5.5, temperature not specified in the publication, low enzyme concentration
28.81
5.53
crude enzyme extract, pH not specified in the publication, 30°C
59.37
purified enzyme, pH not specified in the publication, 30°C
6
-
after isolation from the fermenter liquid by gel filtration, lyophilized preparate
additional information
additional information
electrochemical deposition technique, cyclic voltammetry and Prussian Blue deposition experiments performed, cyclic voltammetry curves of hydrogen peroxide in KCl solution, response curve of hydrogen peroxide on Prussian Blue film modified microelectrode, voltammetric curves and activity image of glucose oxidase by Scanning electrochemical microscopy shown, comparison diagram of bare and Prussian Blue film modified microelectrode, images of glucose oxidase spot activity and its topographic graph
additional information
immobilization of glucose oxidase in a membranous form using polyvinyl alcohol, membrane composition analyzed on the basis of swelling index, Fourier transform infrared study and Scanning electron microscopy, membrane tested for biosensor reading by association with dissolved oxygen probe, detection range estimated, 32 reactions without significant loss of activity determined
additional information
kinetic investigations using Scanning electrochemical microscopy, influence of glucose concentration and of layer number, covering layers and time dependence, kinetic information as a function of layer number, film termination, inert covering layers and enzyme substrate concentration after fitting to numerical models shown, enzymatic conversion by electrochemical measurements at Scanning electrochemical microscopy feedback experiments
additional information
protonated sodium alginate used as a dopant for electrogeneration of polypyrrole/alginate functionalized films, glucose oxidase attached to electrode surface, enzyme linkage to the conductive surface characterized by attenuated total reflection spectroscopy and scanning electron microscopy, bioactivity of the enzyme toward glucose shown to be retained in phosphate buffer solution containing p-benzoquinone as a mediator under an argon atmosphere
additional information
-
sequence similarity to the glucose-methanol-choline (GMC) oxidoreductase enzyme superfamily, biophysical properties shown, function as an electron transport protein, no enzyme activity of the recombinant protein, major allergen in Atopic eczema patients
additional information
-
1.08 U/mg dry weight for the intracellular enzyme, and 6.9U/ml for the extracellular enzyme
additional information
-
effect of culture conditions on enzyme activity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6
5.1
5.5
5.5 - 6
5.6
5.8
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
7.2
-
enzyme-pentacyanoferrate(III)-nucleophilic ligands-complex interaction assay
7.5
5
-
the maximum enzymatic activity of copolymer-conjugated GOD (poly(N-isopropylacrylamide-co-methacrylic acid-co-octadecylacrylate)-conjugated GOD) is observed around pH 5.0 and the value is about 40% of that of native GOD
6
-
natural GOD, pmr1DELTA-mutant-derived GOD,hyperglycosylated GOD expressed in wild-type cells of Saccharomyces cerevisiae
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
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
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
3 - 8
3 - 9
3.5 - 9
activity range of wild-type and mutant enzymes, profile overview
4 - 7
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
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 - 7
-
pH 4.5: about 60% of maximal activity, pH 7.0: about 50% of maximal activity
5 - 10
pH 5.0: about 60% of maximal activity, pH 10.0: about 40% of maximal activity, recombinant wild-type enzyme
additional information
-
the pH correlation of enzyme activity and catalytic characteristics in various buffer systems (phosphate (pH 5.09.0), citrate (pH 3.05.0), citrate-phosphate (pH 3.09.0), and universal (pH 3.0-9.0)) are determined. The GOx is the most efficiently interacting with substrate (glucose) in phosphate buffer at pH 7.0
3 - 8
pH-profiles, 54% of maximal activity at pH 3.0, 20% of maximal activity at pH 8.0 for the recombinant enzyme, 50% for the native enzyme, overview
3 - 9
-
pH 3.0: about 45% of maximal activity, pH 9.0: about 40% of maximal activity, 10 min oxidation-assay of beta-D-glucose
3 - 9
-
low activity at pH 3.0 and pH 9.0, high activity at pH 4.0-7.0 depending on the buffer system used
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
35
37
40
45
50
50 - 80
-
temperature profile of soluble and insoluble enzyme complexes, overview
55
25
-
enzyme-pentacyanoferrate(III)-nucleophilic ligands-complex interaction assay
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 40
0°C: about 70% of maximal activity, 40°C: about 80% of maximal activity, recombinant wild-type enzyme
0 - 50
0°C: about 75% of maximal activity, 40°C: about 75% of maximal activity, mutant enzyme Y169C/A211C
10 - 74
-
10°C: 13% of maximal activity, 30°C: 28% of maximal activity, 74°C: about 60% of maximal activity
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 - 50
the activity of the glycosylated and deglycosylated enzyme increases 2fold from 25°C to 55°C
25 - 60
the activity gradually increases from 25°C to 40°C, but followed by a decrease at higher temperatures
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
4 - 30
Penicillium sp. MX3343
4°C: about 72% of maximal activity, 30°C: maximal activity, recombinant enzyme
70
-
pH 5.1, 75% loss of of activity of natural GOD and pmr1DELTA-mutant-derived GOD, 65% loss of activity of hyperglycosylated GOD
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
sequence with exchanges at V167T and K282E
UniProt
brenda
-
389787, 389788, 389790, 389792, 389793, 389794, 389796, 389797, 389798, 389799, 389801, 389802, 389803, 389804, 389805, 389806, 389807, 389813, 389815, 389816, 389817, 389819, 389821, 389822, 389823, 389824, 389825, 389827, 389829, 389834, 389836, 389837, 654143, 654185, 654358, 654659, 654780, 654909, 655079, 655711, 656254, 656562, 656782, 657249, 672872, 675186, 677260
-
-
brenda
-
695790, 696068, 696369, 696777, 696864, 696865, 696884, 698321, 699078, 699600, 699771, 699922, 699941, 700599, 710858, 710908, 712533, 712857, 713259, 723947, 724880, 724884, 725199, 725789, 726413
-
-
brenda
-
743857, 746771, 746773, 747341, 747343, 747675, 748768, 762536, 762774, 762986, 762993, 763123, 763332, 763385, 763464
SwissProt
brenda
larvae collected from the cotton fields in Zhengzhou, Henan Province of China, gene HaGox
UniProt
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
-
389796, 389797, 389798, 389801, 389802, 389804, 389816, 389821, 389834, 389837, 677260, 723947, 724884, 725789, 726413, 741479
brenda
-
brenda
additional information
activity of wild-type and mutant M12 GOx during fermentation, overview
brenda
additional information
-
activity of wild-type and mutant M12 GOx during fermentation, overview
brenda
additional information
transcript levels of HaGox in larval labial salivary glands are significantly higher than those in midgut and hemolymph, respectively, and those of caterpillars reared on tobacco
brenda
additional information
-
transcript levels of HaGox in larval labial salivary glands are significantly higher than those in midgut and hemolymph, respectively, and those of caterpillars reared on tobacco
brenda
additional information
-
poor growth of the organism in medium containing glucose as sole carbon source, in this culture gluconate accumulates
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
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
brenda
-
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
-
brenda
-
22% of glucose oxidase activity in the stationary phase and 35% of glucose oxidase activity in the mid-exponential phase is localised in the cytoplasm
brenda
-
22% of glucose oxidase activity in the stationary phase and 35% of glucose oxidase activity in the mid-exponential phase is localised in the cytoplasm
-
brenda
-
38% of glucose oxidase activity in the stationary phase and 46% of glucose oxidase activity in the mid-exponential phase is localised in the extracellular fluid
-
brenda
-
38% of glucose oxidase activity in the stationary phase and 46% of glucose oxidase activity in the mid-exponential phase is localised in the extracellular fluid
-
-
brenda
-
59% of glucose oxidase activity in the stationary phase and 30% of glucose oxidase activity in the mid-exponential phase is localised in the extracellular fluid
-
brenda
-
59% of glucose oxidase activity in the stationary phase and 30% of glucose oxidase activity in the mid-exponential phase is localised in the extracellular fluid
-
-
brenda
-
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
brenda
-
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
-
brenda
-
10% of glucose oxidase activity in the stationary phase and 18% of glucose oxidase activity in the mid-exponential phase is localised in the membrane
brenda
-
10% of glucose oxidase activity in the stationary phase and 18% of glucose oxidase activity in the mid-exponential phase is localised in the membrane
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
glucose oxidase (GO) belongs to the auxiliary activity family AA3_2
malfunction
physiological function
additional information
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
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
caterpillar labial salivary enzyme glucose oxidase plays an important role in plant-insect interactions by suppressing the caterpillar-induced nicotine production in tobacco plants
physiological function
glucose oxidase (GOx) addition induces the expression and enzymatic activity of manganese peroxidase (MnP) and lignin peroxidase (LiP) from Phanerochaete chrysosporium strain ATCC 24725 cultures. Daily supplementation with GOx-glucose as compared with control cultures causes a remarkable increase in stability of MnP productivity in fungi cultures. Neither H2O2 nor gluconic acid produced by GOx is responsible for improvement of peroxidase activity in nitrogen-limited cultures. GOx increases MnP and LiP activity in the presence of manganese ions
physiological function
glucose oxidase facilitates osteogenic differentiation and mineralization of embryonic stem cells through the activation of nuclear factor (erythroid-derived 2)-like 2, Nrf2, and ERK signal transduction pathways. Glucose oxidase treatment at relatively low concentrations does not change the viability of embryonic stem cells, whereas it enhances osteogenic differentiation and mineralization in the cells. The enzyme induces heme oxygenase-1 and Nrf2 expression via production of H2O2. Glucose oxidase-mediated acceleration of Runx2 expression and mineralization is inhibited either by Nrf2 knockdown or by treating with 5 lM PD98059, an inhibitor of phospho-extracellular signal-regulated kinase (p-ERK). The glucose oxidase-stimulated mineralization is also suppressed by treating the cells with reduced glutathione or catalase, but not by superoxide dismutase or N-acetylcysteine. Viability of the stem cells is not changed by treatment with glucose oxidase within the ranges from 1-10 mU/ml, while it is reduced significantly by adding 20 mU/ml glucose oxidase into the cultures
physiological function
-
glucose oxidase from Aspergillus niger shows anti-bacterial activity, but no fungicidal effects
physiological function
glucose oxidase from Penicillium notatum shows no fungicidal effects
physiological function
hydrogen peroxide generated by GOX action has anti-microbial effect
physiological function
-
hydrogen peroxide generated by GOX action has anti-microbial effect
-
physiological function
-
glucose oxidase from Aspergillus niger shows anti-bacterial activity, but no fungicidal effects
-
additional information
-
424 is a key position for enzyme activity of the immobilized enzyme on electrode surfaces, overview
additional information
-
a stable secondary conformation with some degree of freedom at the active sites is essential for the bioelectrocatalytic activity of GOx
additional information
-
enzyme denaturing process analysis by molecular dynamics simulations, overview
additional information
enzyme structure and structure-activity relationship analysis and molecular dynamic simulations, detailed overview. Active-site residues of pen-GOx are two histidines, His520 and His563, which act as general base and general acid in the reductive half-reaction and the oxidative half-reaction, respectively
additional information
identification and analysis of structural motifs of the protein which are critical for its stability
additional information
-
identification and analysis of structural motifs of the protein which are critical for its stability
additional information
-
identification and analysis of structural motifs of the protein which are critical for its stability
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GOX_ASPNG
605
0
65638
Swiss-Prot
Secretory Pathway (Reliability: 2)
GOX_PENAG
587
0
63965
Swiss-Prot
other Location (Reliability: 1)
GOX_TALFL
605
0
65769
Swiss-Prot
Secretory Pathway (Reliability: 1)
A0A218N0E8_MYTSE
606
0
66406
TrEMBL
other Location (Reliability: 3)
K9L4P7_PENCH
604
0
66342
TrEMBL
Secretory Pathway (Reliability: 1)
A2I7K9_9EURO
605
0
65778
TrEMBL
Secretory Pathway (Reliability: 1)
Q9HFQ1_ASPNG
604
0
65200
TrEMBL
Secretory Pathway (Reliability: 3)
A0A0K0Q058_9EURO
251
0
27258
TrEMBL
other Location (Reliability: 2)
A0A3G2S2X3_9BASI
983
1
106833
TrEMBL
other Location (Reliability: 2)
A0A0F8CXS8_CERFI
566
0
60975
TrEMBL
other Location (Reliability: 3)
A0A7L7T1A0_PENSQ
Penicillium sp
605
0
65267
TrEMBL
Secretory Pathway (Reliability: 2)
Q0PGS3_ASPNG
581
0
62804
TrEMBL
other Location (Reliability: 1)
G3XZX6_ASPNA
Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7)
596
0
64223
TrEMBL
Secretory Pathway (Reliability: 3)
E3VW38_ASPNG
583
0
63261
TrEMBL
other Location (Reliability: 1)
A2QZ31_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
655
0
73135
TrEMBL
Secretory Pathway (Reliability: 1)
Q9U8X6_APIME
615
0
67938
TrEMBL
other Location (Reliability: 3)
A2QM15_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
596
0
64195
TrEMBL
Secretory Pathway (Reliability: 3)
A0A3G2SBT7_9BASI
614
0
67363
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5Q2UVJ5_9PEZI
613
0
66530
TrEMBL
Secretory Pathway (Reliability: 2)
M5BNG8_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
619
0
65952
TrEMBL
Secretory Pathway (Reliability: 2)
A0A221SAG9_AURPU
589
0
63724
TrEMBL
Secretory Pathway (Reliability: 2)
V9SH09_ASPCA
605
0
65518
TrEMBL
Secretory Pathway (Reliability: 3)
M4VR58_ASPNG
605
0
65564
TrEMBL
Secretory Pathway (Reliability: 2)
D8QJE7_SCHCM
Schizophyllum commune (strain H4-8 / FGSC 9210)
602
0
63598
TrEMBL
Mitochondrion (Reliability: 3)
A0A0Y0IDS5_9EURO
601
0
65535
TrEMBL
Secretory Pathway (Reliability: 2)
B8MDS4_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
636
0
69555
TrEMBL
other Location (Reliability: 4)
A2QBC3_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
605
0
65624
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8J8VZR3_9EURO
592
0
64714
TrEMBL
Secretory Pathway (Reliability: 2)
Q5Q041_ASPNG
581
0
63049
TrEMBL
other Location (Reliability: 1)
A0A1V0E5A9_9PEZI
Aureobasidium sp
607
0
65136
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5Q2USS5_9PEZI
568
0
61578
TrEMBL
Secretory Pathway (Reliability: 1)
D9ZFI1_SPOEX
608
0
67501
TrEMBL
other Location (Reliability: 3)
I6VCW8_ASPNG
586
0
63591
TrEMBL
other Location (Reliability: 1)
Q70FC9_TALVA
605
0
65670
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0F4YPS7_TALEM
573
0
61772
TrEMBL
Secretory Pathway (Reliability: 2)
A0A142I707_9NEOP
607
0
67048
TrEMBL
other Location (Reliability: 3)
M5BN50_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
199
0
21474
TrEMBL
other Location (Reliability: 3)
MNCO_MICNN
495
0
54679
Swiss-Prot
other Location (Reliability: 3)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
120000
146000
-
x * 146000, deglycosylated recombinant enzyme with PEG-350 reagent, SDS-PAGE
148000
150000 - 153000
158000 - 160000
159000
-
calculated value based on Stokes' radius and sedimentation coefficient
160000
167000
-
glycosylated enzyme, PAGE under non-dissociating conditions
175000 - 180000
180000
211000
-
x * 211000, deglycosylated recombinant enzyme with PEG-5000 reagent, SDS-PAGE
45000
-
4 * 45000, 2 polypeptide chains linked by disulfide bond, sedimentation equilibrium centrifugation, treatment with guanidine-HCl and 2-mercaptoethanol
60000
70000
72000
77700
-
2 * 77700, SDS-PAGE, confirmed by electron-microscopic examinations
80000
90000 - 130000
recombinant glycosylated Aga2GOx fusion protein, native PAGE
120000
SDS-PAGE, wild-type and mutant enzyme Y169C/A211C
180000
-
gel filtration, overestimation may be due to hydrodynamic properties of the enzyme
80000
2 * 80000, PAGE under dissociating conditions, glycosylated enzyme
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
oligomer
tetramer
additional information
?
-
x * 146000, deglycosylated recombinant enzyme with PEG-350 reagent, SDS-PAGE
?
-
x * 211000, deglycosylated recombinant enzyme with PEG-5000 reagent, SDS-PAGE
?
x * 120000, SDS-PAGE, wild-type and mutant enzyme Y169C/A211C
?
-
x * 120000, SDS-PAGE, wild-type and mutant enzyme Y169C/A211C
-
dimer
-
for both native and deglycosylated GOD at pH 6 and 10 only the dimeric configuration is observed
dimer
2 * 80000, PAGE under dissociating conditions, glycosylated enzyme
dimer
-
each unit in the dimer is composed of two polypeptide chains connected by a disulfide bond
dimer
-
2 * 77700, SDS-PAGE, confirmed by electron-microscopic examinations
homodimer
2 * 100000-140000, recombinant glycosylated Aga2-GOx fusion protein, SDS-PAGE, 2 * 74500, about, recombinant Aga2-GOx fusion protein, sequence calculation, 2 * 65000, about, native GOx, sequence calculation
homodimer
each monomer contains two domains, one consists of a five-stranded beta-sheet sandwiched between a three-stranded beta-sheet and three alpha-helices, and the other is composed by a large six-stranded antiparallel beta-sheet supported by six alpha-helices. The two units of the dimer are connected through hydrophobic and hydrophilic contacts, the latter including salt bridges and hydrogen bonds
homodimer
-
each monomer contains two domains, one consists of a five-stranded beta-sheet sandwiched between a three-stranded beta-sheet and three alpha-helices, and the other is composed by a large six-stranded antiparallel beta-sheet supported by six alpha-helices. The two units of the dimer are connected through hydrophobic and hydrophilic contacts, the latter including salt bridges and hydrogen bonds
-
homodimer
2 * 66700, SDS-PAGE and crystal structure analysis
tetramer
-
4 * 45000, 2 polypeptide chains linked by disulfide bond, sedimentation equilibrium centrifugation, treatment with guanidine-HCl and 2-mercaptoethanol
additional information
-
a stable secondary conformation with some degree of freedom at the active sites is essential for the bioelectrocatalytic activity of GOx
additional information
enzyme structure and structure-activity relationship analysis and molecular dynamic simulations, detailed overview. The three-dimensional structure of the glucose oxidase is stabilized by FAD, which can act as a redox carrier in catalysis
additional information
-
the monomers of GOx-pa contain 587 amino acids each, and one prosthetic group, flavin adenine dinucleotide (FAD). Dimer interface analysis
additional information
-
AldO shares the same folding topology of the members of the vanillyl-alcohol oxidase family of flavoenzymes, three-dimensional structure analysis, overview
additional information
-
AldO shares the same folding topology of the members of the vanillyl-alcohol oxidase family of flavoenzymes, three-dimensional structure analysis, overview
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
no glycoprotein
additional information
-
endo-beta-N-acetylglucosaminidase from Flavobacterium sp. releases about 30% of the N-linked sugar chains from the enzyme
glycoprotein
-
the enzyme contains 74% protein, 16.4% neutral sugar and 2.4% amino sugar, major component: mannose
glycoprotein
-
native enzyme contains 12% carbohydrate by weight, main component: mannose, the carbohydrate moiety plays a role in increasing the stability of the protein moiety, but does not directly participate in the catalytic activity, in the immunological reactivity, or in maintaining the conformation of the enzyme protein, periodate treatment decreases the carbohydrate content to about 40% of its original value
glycoprotein
-
carbohydrate content between 10.7 and 16.5%, major component: mannose
glycoprotein
-
N- and O-linked sugar chains, the enzyme contains 15.2% carbohydrates
glycoprotein
-
GOD-His6 expressed in wild-type strain of Saccharomyces cerevisiae is hyperglycosylated, GOD-His6 expressed in pmr1DELTA strain of Saccharomyces cerevisiae is not hyperglycosylated. The catalytic efficiency and physical properties of pmr1DELTA mutant-derived GOD-His6 are very similar to those of natural GOD
glycoprotein
-
the enzyme binds to concanavalin A forming insoluble complexes, overview
glycoprotein
approx. 95% of the carbohydrate moiety is cleaved from the protein by incubation of glucose oxidase with endoglycosidase H and alpha-mannosidase. Cleavage of the carbohydrate moiety effects a 23-30% decrease in the molecular weight and a reduction in the number of isoforms of glucose oxidase. No significant changes were observed in the circular dichroism spectra of the deglyeosylated enzyme. Other properties, such as thermal stability, pH and temperature optima of glucose oxidase activity and substrate specificity are not affected. However, removal of the carbohydrate moiety marginally affect the kinetics of glucose oxidation and stability at low pH. From these results it appears that the carbohydrate chain of glucose oxidase does not contribute significantly to the structure, stability and activity of glucose oxidase
glycoprotein
the enzyme is around 15% glycosylated with mostly mannose-type glycosylation
glycoprotein
eight potential N-glycosylation at N43, N89, N161, N168, N258, N355, N388, and N473
glycoprotein
-
the enzyme consists of 13% carbohydrate comprising 95 residues of mannose, 12 residues of glucosamine and 5 residues of galactose per molecule of enzyme, six N-glycosylation sites estimated for the dimer
glycoprotein
-
no significant differences in catalytic properties of glyco- and aglyco-GOD
glycoprotein
-
carbohydrate content between 10.7 and 16.5%, major component: mannose
glycoprotein
-
the enzyme has four N-glycosylation sites at positions ASN93, ASN165, ASN357, and ASN392, respectively. Three different sugars are bound at these positions: N-acetyl-D-glucosamine, beta-D-mannose, and alpha-D-mannose
glycoprotein
the recombinant enzyme from Pichia pastoris is higher glycosylated, 17%, compared to the native enzyme, 14%
glycoprotein
-
the recombinant enzyme from Pichia pastoris is higher glycosylated, 17%, compared to the native enzyme, 14%
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
of the partially deglycosylated enzyme, crystal structure determined by isomorphous replacement and refined to 2.3 A resolution
-
deglycosylation and purification to isoelectric homogeneity are important prerequisite steps to obtain crystals suitable for X-ray investigations. Crystals of the deglycosylated enzyme are reproducibly grown using ammonium sulfate as precipitant at pH 7.4 to 7.5. Crystals diffract to at least 2.0 A resolution and belong to the orthorhombic space group P2(1)2(1)2(1), with refined lattice constants of a = 59.3 A, b = 136.3 A and c = 156.7 A. Crystallized as a complex with the coenzyme FAD
the enzyme crystallizes from 1.3 M ammonium sulfate, 100 mM citrate/phosphate buffer pH 7.4 in the orthorhombic space group P212121, with unit-cell dimensions a = 57.6, b = 132.1, c = 151.3 A and one dimeric molecule per asymmetric unit. The structure is determined by molecular replacement and refined at 1.8 A resolution to an R value of 16.4%
native wild-type enzyme, hanging-drop vapor diffusion method at 4 °C by mixing equal volumes of 14 mg/mL AldO solution in 50 mM potassium phosphate buffer, pH 7.5, with reservoir solutions containing 0.1 M MES/HCl, pH 6.5, 0.2 M MgCl2 and 18-20% w/v PEG4000, 3-4 days, substrate incorporation by soaking the wild-type AldO crystals in a solution consisting of 0.1 M MES/HCl, pH 6.5, 0.2 M MgCl2, 25% w/v PEG 4000, 17.5% sucrose, and 25 mM substrate for 3 h, X-ray diffraction structure determination and analysis at 1.1-1.9 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
I94V/T30S
increased O2 sensitivity, increased electron transfer (1.9fold)
L569E
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
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
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
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
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
H220D
-
site-directed mutagenesis, mutant H220D shows increased thermosensitivity and reduced activity compared to the wild-type enzyme
-
Q124R/L569E
-
site-directed mutagenesis, the mutation has no significant effect on stability but causes a twofold increase of the enzyme's specific activity
-
Q90R/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
-
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
-
Y169C/A211C
G423D
K424E
K424I
-
site-directed mutagenesis, the mutation does not significantly affect the enzyme activity
R516K
the mutant enzyme whose side chain forms only one hydrogen bond with the 3-OH group of beta-D-glucose, exhibits an 80fold higher apparent Km (513 mM) but a Vmax only 70% lower than the wild type
R516Q
the complete elimination of a hydrogen-bond interaction between residue 516 and the 3-OH group of beta-D-glucose through the substitution R516Q effects a 120fold increase in the apparent Km for glucose (to 733 mM) and a decrease in the Vmax to 1/30
S114A/F355L
increased electron transfer, 88% decrease in O2 sensitivity
V464A/K424E
2.4fold increase in electron transfer, 95% decrease in O2 sensitivity
V564S
1.1fold increase in electron transfer, 88% decrease in O2 sensitivity
R516K
-
the mutant enzyme whose side chain forms only one hydrogen bond with the 3-OH group of beta-D-glucose, exhibits an 80fold higher apparent Km (513 mM) but a Vmax only 70% lower than the wild type
-
R516Q
-
the complete elimination of a hydrogen-bond interaction between residue 516 and the 3-OH group of beta-D-glucose through the substitution R516Q effects a 120fold increase in the apparent Km for glucose (to 733 mM) and a decrease in the Vmax to 1/30
-
additional information
H447K
site-directed mutagenesis, introduction of two symmetrical, intermolecular salt bridges at the dimer interface, between K447 and D70
H447K
site-directed mutagenesis, the shows similar initial activity but higher thermal sensitivity compared to the wild-type enzyme
L569E
site-directed mutagenesis, the mutant shows about 50% increased initial activity compared to the wild-type enzyme
L569E
site-directed mutagenesis, the thermal stability of the mutant is similar to the wild-type enzyme, but the initial activity is increased compared to the wild-type enzyme
Q345K
site-directed mutagenesis, introduction of the mutation to create a salt bridge with D177
Q345K
site-directed mutagenesis, the mutant shows highly reduced thermal stability and about 50% increased initial activity compared to the wild-type enzyme
Q469K/L500D
site-directed mutagenesis, the mutant shows strongly reduced activity compared to the wild-type enzyme
Q469K/L500D
site-directed mutagenesis, the thermal stability of the mutant is similar to the wild-type enzyme, but the initial activity is reduced compared to the wild-type enzyme
Q90R/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
Q90R/Y509E
site-directed mutagenesis, the mutation introduces a new salt bridge near the interphase of the dimeric protein structure, 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
T30S/I94V
site-directed mutagenesis, the mutant shows reduced activity 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
mutant enzyme displays better catalytic properties than the native enzyme
Y169C/A211C
compared with wild-type enzyme, the half-life of the mutant, at 40 °C increases approximately 48fold. The kcat and catalytic efficiency are enhanced 0.7fold and 1.6fold, respectively
Y169C/A211C
-
compared with wild-type enzyme, the half-life of the mutant, at 40 °C increases approximately 48fold. The kcat and catalytic efficiency are enhanced 0.7fold and 1.6fold, respectively
-
G423D
-
site-directed mutagenesis, the mutant shows no activity compared to the wild-type enzyme
G423D
-
site-directed mutagenesis, the mutants containing the mutation G423D leads to quadruple mutants that are not able to reconstitute. The mutant enzymes displays a dramatic decrease in activity compared to thré wild-type enzyme
K424E
-
site-directed mutagenesis, the single mutation results in a significant increase in the current density which becomes 2.4 fold higher than the current obtained for the wild-type
K424E
increased electron transfer (2.4fold), 20% decrease in O2 sensitivity
additional information
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preparation of surface variants that contain artificial polymer poylethylene glycol. All surface modifications of glucose oxidase beyond that of the wild-type enzyme give rise to altered behavior for hydrogen transfer in the active site such that the kinetic isotope effect becomes more temperature-dependent upon perturbation
additional information
-
engineering of glucose oxidase by site-specific attachment of a maleimide-modified gold nanoparticle to the enzyme for enabling direct electrical communication between the conjugated enzyme and an electrode required for using the enzyme as biosensor, evaluation, overview
additional information
-
enzyme adsorption on different particles with homogeneous or nanostructured surfaces and coated with different compounds, i.e. 11-amino-1-undecanethiol, 12-mercaptododecanoic acid, 1-dodecanethiol, and 11-(1H-pyrol-11-(1H-pyrol-1-yl)undecane-1-thiol), only 9% of the activity of the native protein is preserved on 11-(1H-pyrol-11-(1H-pyrol-1-yl)undecane-1-thiol), but the substrate affinity of the adsorbed GOx is best on 11-(1H-pyrol-11-(1H-pyrol-1-yl)undecane-1-thiol) where its catalytic activity is worst, secondary structure of thhe enzyme is altered compared to enzyme in solution, overview
additional information
-
laccase and glucose oxidase in poly(ethyleneimine) microcapsules for immobilization in paper, activity, conformation and thermal stability, overview. The KM for GOx does not change after microencapsulation. Microencapsulation improves the thermal stability of GOx at temperatures up to 60°C due to stabilization of its active conformation but reduces the thermal stability of laccase because of the increased coordination between PEI and copper atoms in the enzyme's active site
additional information
-
macroporous silica foam is used as a nanoreactor to co-confine glucose oxidase and horseradish peroxidase with enzymatic cascade reactions, which act in tandem inside nanoreactors, for oxidation of glucose and 3,3',5,5'-tetramethylbenzidine, the catalytic activity of the co-confined enzymes is reduced, but stabilities of co-confined enzymes in denaturing agents, such as guanidinium chloride (GdmCl) and urea, are higher than those of free enzymes in solution compared to that of free enzymes in solution at room temperature. Adsorption amounts of glucose oxidase and horseradish peroxidase into macropores under different conditions, overview
additional information
-
modulation of calibration parameters of biosensors, in which glucose oxidase is used for biorecognition, in the presence of different chlorides by following the transient phase dynamics ofoxygen concentration with an oxygen optrode, mechanism, overview. the maximum calculated signal change was amplifiedfor about 20% in the presence of sodium and magnesium chlorides. The value of the kinetic parameter decreases along with the addition of salts and increases only at sodium chloride concentrations over 0.5 mM, MgCl2 causes a 1.3fold essential increase of the maximum signal change parameter A in a salt concentration, ranging from 0.1 to 0.4 M. AlCl3 inhibits the enzyme at 5 mM, and at higher salt concentrations over 0.1 M, the catalytic activity is completely inhibited
additional information
-
PEGylation of GOx provides stability against denaturation or hydrolytic cleavage, glycosylation site-targeted PEGylation of glucose oxidase retains native enzymatic activity, bioconjugate's potential of the enzyme in an optical biosensing assay, overview. The bioconjugate is entrapped within a poly(2-hydroxyethyl methacrylate) hydrogel containing an oxygen-sensitive phosphor, and the construct is shown to respond approximately linearly over the physiologically-relevant glucose range, overview
additional information
-
construction of a nanodevice coupled with an integrated real-time detection system for evaluation of the function of biomolecules in biological processes, and enzymatic reaction kinetics occurring at the confined space or interface. A nanochannel-enzyme system in which the enzymatic reaction is coupled with an electrochemical method is constructed. The model system is established by covalently linking glucose oxidase (GOD) onto the inner wall of the nanochannels of the porous anodic alumina (PAA)membrane. For enzyme assembling, the PAA membranes are first treated with silane to form epoxy groups modified inner surface of PAA nanochannels. Then GOD is assembled onto the membrane and the inner wall of the nanochannels through a ring-opening reaction. An gold disc is attached at the end of the nanochannel of the PAA membrane as the working electrode for detection of H2O2 product of enzymatic reaction. The effects of ionic strength, amount of immobilized enzyme and pore diameter of the nanochannels on the enzymatic reaction kinetics are analysed, method evaluation, overview
additional information
construction of enzyme mutant B11 with a C-terminal fusion with Saccharomyces cerevisiae Aga2 protein, the fusion proteins display on the surface of yeast EBY100 cells and show 2fold increased activity compared to the wild-type enzyme at pH 5.5 Aga2-GOx fusion proteins in the yeast cell wall can also be used as immobilized catalysts for the production of gluconic acid. The yeast surface display is developed for the directed evolution of antibodies in Saccharomyces cerevisiae, and involves the fusion of antibody variable domains to Aga2p, the adhesion subunit of the yeast agglutinin protein. Aga2p binds via disulfide bonds to the membrane protein Aga1p, which is embedded in the membrane via a glycosylphosphatidylinositol (GPI) anchor. The Aga2-antibody fusion gene is cloned in the vector pCTCON, whereas the Aga1p gene is integrated into the yeast genome, but both are under the control of galactose-inducible promoters. The surface display system is used for the directed evolution of horseradish peroxidase and expression of GOx for applications in biofuel cells. The kcat of the wild-type and B11 fusion enzymes are 1.65fold and 1.30fold lower than of the non-fusion enzymes, respectively, and the Km values of the wild-type and B11 fusion enzymes are 1.52fold and 1.74fold higher than of the non-fusion enzymes, respectively
additional information
-
construction of enzyme mutant B11 with a C-terminal fusion with Saccharomyces cerevisiae Aga2 protein, the fusion proteins display on the surface of yeast EBY100 cells and show 2fold increased activity compared to the wild-type enzyme at pH 5.5 Aga2-GOx fusion proteins in the yeast cell wall can also be used as immobilized catalysts for the production of gluconic acid. The yeast surface display is developed for the directed evolution of antibodies in Saccharomyces cerevisiae, and involves the fusion of antibody variable domains to Aga2p, the adhesion subunit of the yeast agglutinin protein. Aga2p binds via disulfide bonds to the membrane protein Aga1p, which is embedded in the membrane via a glycosylphosphatidylinositol (GPI) anchor. The Aga2-antibody fusion gene is cloned in the vector pCTCON, whereas the Aga1p gene is integrated into the yeast genome, but both are under the control of galactose-inducible promoters. The surface display system is used for the directed evolution of horseradish peroxidase and expression of GOx for applications in biofuel cells. The kcat of the wild-type and B11 fusion enzymes are 1.65fold and 1.30fold lower than of the non-fusion enzymes, respectively, and the Km values of the wild-type and B11 fusion enzymes are 1.52fold and 1.74fold higher than of the non-fusion enzymes, respectively
additional information
glucose oxidase is chemically modified to increase the stability of GOx using N-(3-dimethylaminopropyl)-N'-ethylcarbodiimide hydrochloride and sodium benzoate or aniline. The modification forms an amide bond between benzoate and lysines or aniline with glutamate and aspartate residues. The labeling of primary amines (lysines and the N-terminus) by benzoate is measured through a trinitrobenzene sulfonic acid (TNBS) assay
additional information
glucose oxidase is immobilized on mesoporous SBA-15 silica and two mesocellular foams (MCF) characterized by similar surface area and pore volumes but different pore/cell dimensions, covalent grafting of the enzyme through amide bonds, overview. The immobilized protein activity is significantly higher for the mesocellular foam with both cells and windows size larger than the enzyme dimensions. Enzyme GOx exhibits higher thermal stability when immobilized on the mesocellular foam compared to thefree enzyme
additional information
-
in situ RAFT polymerization of four different monomers including acrylic acid (AA), methyl acrylate (MA), poly (ethylene glycol) acrylate (PEG-A) and tert-butyl acrylate (TBA) are polymerized directly on the surface of enzyme GOx to afford GOx-poly (PEG-A)(GOx-PPEG-A), GOx-poly(MA)(GOx-PMA), GOx-poly(AA)(GOx-PAA), and GOx-poly(TBA)(GOx-PTBA) conjugates, respectively. PAA and PPEG-A represent the hydrophilic polymers, while PMA and PTBA stand for the hydrophobic ones. Higher bioactivity is obtained for GOx modified with hydrophilic polymers compared with that modified with hydrophobic ones. All the tested polymers can enhance the stability of the GOx, while the hydrophobic GOx-polymers conjugates exhibit much better stability than the hydrophilic ones. Method overview
additional information
-
the enzyme adopts a stable secondary conformation with some degree of freedom at active sites under acidic-neutral pH values, when either free in solution or immobilized on Nafion. Immobilization on Nafion actually increases the amount of active enzyme (Vmax) and affinity for glucose (inversely proportional to Km) at pH 6.0
additional information
usage of a strategy that combined random and rational approaches to isolate uncharacterized mutations of Aspergillus niger glucose oxidase with improved properties. GOX library construction in Saccharomyces cerevisiae and random mutagenesis and screening for mutants with improved thermal stability
additional information
-
usage of a strategy that combined random and rational approaches to isolate uncharacterized mutations of Aspergillus niger glucose oxidase with improved properties. GOX library construction in Saccharomyces cerevisiae and random mutagenesis and screening for mutants with improved thermal stability
additional information
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
additional information
-
usage of a strategy that combined random and rational approaches to isolate uncharacterized mutations of Aspergillus niger glucose oxidase with improved properties. GOX library construction in Saccharomyces cerevisiae and random mutagenesis and screening for mutants with improved thermal stability
-
additional information
the removal of aromatic or bulky residues at positions 73, 418 or 430 result in decreases in the maximum rates of glucose oxidation to less than 1/90
additional information
-
the removal of aromatic or bulky residues at positions 73, 418 or 430 result in decreases in the maximum rates of glucose oxidation to less than 1/90
additional information
-
for use on electrode surfaces, the key amino acid at the entrance of the active site of glucose oxidase from Penicilium amagasakiense, Lys424, Gln75, Gln184, and Gly423, are redesign by nonactive site mutations, leading to enzymatic anodes with 2.4fold higher current densities, making the biosensor more effective. 424 is the key position
additional information
-
the removal of aromatic or bulky residues at positions 73, 418 or 430 result in decreases in the maximum rates of glucose oxidation to less than 1/90
-
additional information
-
construction of a Penicillium funiculosum highly active strain 46.1 from parental strain BIM F-15 as a producer of extracellular GOx by induced mutagenesis technique. The GOx from Penicillium funiculosum strain 46.1 differs from GOx purified from the parent strain BIM F-15 by reduced Michaelis constant, higher efficiency of glucose oxidation, pH dependence, and thermal stability, but it has similar thermal optimum. The enzyme-encoding gene has no special mutation
additional information
-
construction of a Penicillium funiculosum highly active strain 46.1 from parental strain BIM F-15 as a producer of extracellular GOx by induced mutagenesis technique. The GOx from Penicillium funiculosum strain 46.1 differs from GOx purified from the parent strain BIM F-15 by reduced Michaelis constant, higher efficiency of glucose oxidation, pH dependence, and thermal stability, but it has similar thermal optimum. The enzyme-encoding gene has no special mutation
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
11
-
at 4°C, 7 months, glycine/NaOH buffer, residual activity of the glycosylated enzyme: less than 1%, residual activity of the deglycosylated enzyme: less than 1%
389832
12
-
at 4°C, 7 months, glycine/NaOH buffer, residual activity of the glycosylated enzyme: less than 1%, residual activity of the deglycosylated enzyme: less than 1%
389832
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 - 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 - 9
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 - 5.2
-
recombinant enzyme, exhibits more than 80% of the maximum activity
389835
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 - 7
5 - 8
5.5
6.2 - 6.5
-
recombinant enzyme, exhibits more than 80% of the maximum activity
389835
additional information
10
-
the native enzyme shows partial unfolding but the deglycosylated form shows a compaction of conformation
654358
10
-
at 4°C, 7 months, glycine/NaOH buffer, residual activity of the glycosylated enzyme: less than 1%, residual activity of the deglycosylated enzyme: less than 1%
389832
3
-
the BTL wild-type strain enzyme is slightly more stable than the commercially available enzyme
389831
3
-
at 4°C, 7 months, glycine/HCl buffer, residual activity of the glycosylated enzyme: 34%, residual activity of the deglycosylated enzyme: 10%
389832
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
-
both the BTL wild-type strain enzyme and the commercially available enzyme are stable for at least 48 h
389831
4
-
at 4°C, 7 months, glycine/HCl buffer, residual activity of the glycosylated enzyme: 58%, residual activity of the deglycosylated enzyme: 30%
389832
4
-
at 4°C, 7 months, acetate buffer, residual activity of the glycosylated enzyme: 65%, residual activity of the deglycosylated enzyme: 59%
389832
5
-
both the BTL wild-type strain enzyme and the commercially available enzyme are stable for at least 48 h
389831
5
deglycosylation has no marked effect on the stability of the enzyme above pH 5
727055
5
-
at 4°C, 7 months, acetate buffer, residual activity of the glycosylated enzyme: 81%, residual activity of the deglycosylated enzyme: 60%
389832
5
-
extremely stable, no loss of activity detected after 300 days at 4°C and 30°C
389833
5 - 7
-
recombinant enzyme, more than 90% of the residual activity retained after 72 h incubation at room temperature
389835
6
-
both the BTL wild-type strain enzyme and the commercially available enzyme are stable for at least 48 h
389831
6
-
at 4°C, 7 months, acetate buffer, residual activity of the glycosylated enzyme: 76%, residual activity of the deglycosylated enzyme: 70%
389832
6
-
at 4°C, 7 months, phosphate buffer, residual activity of the glycosylated enzyme: 80%, residual activity of the deglycosylated enzyme: 75%
389832
6
-
at pH 6.0 and at 50°C, the half life of the enzyme is about 20 h
712533
7
-
above, the recombinant enzyme is slightly less stable than native and deglycosylated enzyme
389835
7
-
at 4°C, 7 months, Tris/HCl buffer, residual activity of the glycosylated enzyme: 71%, residual activity of the deglycosylated enzyme: 70%
389832
7
-
at 4°C, 7 months, phosphate buffer, residual activity of the glycosylated enzyme: 88%, residual activity of the deglycosylated enzyme: 87%
389832
8
-
at 4°C, 7 months, phosphate buffer, residual activity of the glycosylated enzyme: 7%, residual activity of the deglycosylated enzyme: 5%
389832
8
-
at 4°C, 7 months, TRIS/HCl buffer, residual activity of the glycosylated enzyme: 20%, residual activity of the deglycosylated enzyme: 16%
389832
9
at alkaline pH, particularly at and above pH 9.0, the glycosylated and the declycosylated enzyme are relatively unstable
727055
9
-
at 4°C, 7 months, glycine/NaOH buffer, residual activity of the glycosylated enzyme: less than 5%, residual activity of the deglycosylated enzyme: less than 5%
389832
9
-
at 4°C, 7 months, Tris/HCl buffer, residual activity of the glycosylated enzyme: less than 2%, residual activity of the deglycosylated enzyme: less than 2%
389832
additional information
the deglycosylated enzyme is less stable at low pH
727055
additional information
-
the deglycosylated enzyme is less stable at low pH
727055
additional information
-
comparison of soluble and immobilized enzyme
389791
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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 - 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
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
30
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
35
37
40
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
45
45 - 65
-
at 45°C the enzyme half-life is 99 min and at 65°C it is 20.38 min under similar conditions
50
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
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
60
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
65
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
70
80
additional information
37
-
GOD has half-life of approximately 30 min at 37°C, immobilized GOD is more effective for applications at 37°C
37
-
at 37°C and in pH 7.5 buffer, the half life of the native enzyme is 48 h
37
-
loss in specific activity of PEGylated GOx and native GOx in the absence of glucose and at 37°C, the PEGylated enzyme is more stable and retains 62.6% after 24 h and about 40% after 30 days, the native enzyme retains 67.3% after 24 h and about 20% after 30 days, overview
37
-
at 37°C and in pH 7.5 buffer, the half life of the recombinant enzyme yGOXpenag is 6 h
40
-
at or below both the BTL wild-type strain enzyme and the commercially available enzyme are stable for at least 48 h
40
1 h, no loss of activity, mutant enzyme Y169C/A211C. Half-life of mutant enzyme Y169C/A211C: 720 min. Half-life of wild-type enzyme: 15 min
40
half-life native enzyme: 103 min, half-life recombinant enzyme: 26 min
45
-
bound to Blue Dextran, in the absence of added FAD, 60% activity retained after 3 h
45
1 h, complete loss of activity, recombinant enzyme. 30 min, 60% loss of activity, mutant enzyme Y169C/A211C
45
half-life native enzyme: 23 min, half-life recombinant enzyme: 3 min
50
-
both native and carbonhydrate-depleted enzyme retain full activity below
50
-
the poly(methyl methacrylate)-bovine serum albumin particle-adsorbed GOx only loses 28% of its activity in comparison with a 64% activity loss of free GOx when it is incubated at 50°C for 35 h
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
50
the purified recombinant enzyme retains 90% activity at 50°C for 30 min
50
-
the activity of the free enzyme decreases to 30% of the original value, the activity of the immobilized enzyme scarcely decreases
50
-
at pH 6.0 and at 50°C, the half life of the enzyme is about 20 h, thermal denaturation is observed above 50°C
55
-
bound to Blue Dextran, in the absence of added FAD, 20% activity retained after 3 h
55
-
the commercially available enzyme is more stable than the BTL wild-type strain enzyme
55
purified dimeric enzyme, pH 5.8, stable up to, rapid inactivation above, the enzyme forms aggregates at incubation temperatures above 55°C, overview
60
-
affinity-layered preparation retains 55% of the original activity after 2 h of preincubation, soluble enzyme loses almost 80% activity in 15 min
60
-
half-life of native enzyme without additive: 13 min, half-life of enzyme in presence of lysozyme: 46 min, half-life of enzyme in presence of 1 M NaCl: 434 min, half-life of enzyme in presence of 0.2 M K2SO4: 308 min
60
purified enzyme, residual activity after 10 min is 32.9% for the wild-type enzyme and 14.7% for enzyme mutant M12
60
t1/2: 10.5 min (wild-type enzyme), 9.0 (mutant enzyme T30V/I94V/A162T), 11.74 (mutant enzyme T30V/I94V/A162T/R537K/M556V), 15.75 (mutant enzyme T30V/R37K/I94V/V106I/A162T/M556V)
65
-
the commercially available enzyme is more stable than the BTL wild-type strain enzyme
70
-
native GOx retains 48% activity after 10 min, the bioactivity is completely lost after 1 h at 70°C. The bioactivity of the enzyme-polymer conjugates (GOx-PPEG-A, GOx-PAA, GOx-PMA and GOx-PTBA) only slowly declines, GOx-PPEG-A, GOx-PAA, GOx-PMA and GOx-PTBA retain about 61%, 67%, 79%, and 73%, after 10 min and 28%, 24%, 35%, and 37% after 1 h, respectively, at 70°C. The four polymers, hydrophilic or hydrophobic, improve the thermal stability of enzyme GOx. Enzyme modified by hydrophobic polymers (PMA and PTBA) exhibit better thermal stability than that modified by hydrophilic ones (PPEG-A and PAA)
70
-
completely inactivated after 15 min in the absence of glucose and 50% inactivated in the presence of glucose
80
-
the pure enzyme is inactive at 80°C, thermal resistance is high only at pH 7.0
80
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
additional information
-
comparison of stability of enzyme from different sources
additional information
-
native and carbohydrate-depleted enzyme, no decrease of activity after 100 freeze-thaw cycles
additional information
-
the irreversible nature of thermal inactivation is caused by a change in the state of association of apoenzyme. The dissociation of FAD results in the loss of secondary and tertiary structure, leading the unfolding and nonspecific aggregation of the enzyme molecule because of hydrophobic interactions of side chains
additional information
-
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
additional information
-
inactivation of the free enzyme within 10 min. Microencapsulation improves the thermal stability of GOx at temperatures up to 60°C due to stabilization of its active conformation but reduces the thermal stability of laccase because of the increased coordination between poly(ethyleneimine) and copper atoms in the enzyme's active site, 70% remaining activity after 60 min
additional information
analysis of thermal inactivation kinetics of enzyme GOD
additional information
glucose oxidase stabilization against thermal inactivation using high hydrostatic pressure and hydrophobic modification, method development, evaluation, and kinetics of thermal inactivation, detailed overview. Determination of the effect of temperature on the rate constant of inactivation of GOx at each of the selected pressures, and of the pressure effects on the rate constant of inactivation of GOx
additional information
-
thermal inactivation thermodynamic parameters of GOx, overview
additional information
wild-type and mutant enzyme Y169C/A211C are cold adapted
additional information
-
wild-type and mutant enzyme Y169C/A211C are cold adapted
additional information
-
comparison of stability of enzyme from different sources
additional information
-
enzyme denaturing process at different temperatures, localization of breaking points, analysis by molecular dynamics simulations, overview. Identification of the transition state of protein folding/unfolding, overview
additional information
-
glucose stabilizes against heat inactivation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
-
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
-
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
K2SO4 enhances the thermal stability by primarily strengthening the hydrophobic interactions and makes the holoenzyme a more compact dimeric structure
-
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
-
protein/water interfacial tension as a critical physicochemical attribute of excipients that is crucial for increasing enzyme kinetic stability
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
-
the enzyme stability is not influenced by physiological concentration of sodium chloride (140 mM)
-
the enzyme stability is not influenced by physiological concentration of sodium chloride (140 mM)
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
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
SDS
tetrahydrofuran
Acetone
-
50%, 37°C, 6 h, immunoeffinity immobilized enzyme preparation retains 72% of the original activity, soluble enzyme retains 18% of the initial activity
Acetone
-
2h, 37°C, 10-50%, inactivation of insoluble enzyme complexes, 50% acetone reduces the activity of the soluble enzyme by 62%, reduction of the activity of the soluble antibody-Con A-enzyme complex by 14-34%, overview
dioxane
-
50%, 37°C, 6 h, immunoeffinity immobilized enzyme preparation retains 99% of the original activity, soluble enzyme retains 63% of the initial activity
dioxane
-
2h, 37°C, 10-50%, effects on soluble and insoluble enzyme complexes, overview
SDS
wild-type and mutant enzyme Y169C/A211C are highle resistant
SDS
-
wild-type and mutant enzyme Y169C/A211C are highle resistant
-
tetrahydrofuran
-
50%, 37°C, 6 h, immunoeffinity immobilized enzyme preparation retains 87% of the original activity, soluble enzyme retains 1% of the initial activity
tetrahydrofuran
-
2h, 37°C, 10-50%, effects on soluble and insoluble enzyme complexes, overview
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
immobilized enzyme, 50°C, half of GOx activity is retained in 40% v/v MeOH/acetate buffer
743105
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-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
-
0C, as a solid, stable for at least 2 years
4°C, lyophilized enzyme, no loss of activity after 1 year, 10% loss of activity after 2 years
-
4°C, more than 90% activity retained, 100 mM phosphate buffer, pH 7, immobilized, 4 months
-
4C, purified recombinant enzyme in 100 mM sodium phosphate, pH 5.1, several months, no loss of 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
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
-
the lyophilized purified enzyme is stable at -20 °C for a minimum of 6 months.
-
4C, purified recombinant enzyme in 100 mM sodium phosphate, pH 5.1, several months, no loss of activity
-
4C, purified recombinant enzyme in 100 mM sodium phosphate, pH 5.1, several months, no loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
all reconstituted variants are purified to homogeneity by mild acidification and ion-exchange chromatography
ammonium sulfate precipitation, DEAE cellulose column chromatography, and Sephadex G-100 gel filtration
-
ammonium sulfate precipitation, ion exchange chromatography, and gel filtration
-
from a partially purified sample, using column chromatography on DEAE-cellulose
-
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
-
HiTrap phenyl HP column chromatography and HiTrap Q FF column chromatography
-
isolation and purification of the extracellular enzyme by precipitation with Mg(OH)2, Zn(OH)2, aluminium oxide, zinc phosphate, or calcium phosphate, method evaluation, two fractions, overview
-
isolation of glyco-GOD and aglyco-GOD from tunicamycin containing growth medium
-
native enzyme 10.7fold by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
native enzyme 26.4fold by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
-
native enzyme 63fold by ammonium sulfate fractionation, ultrafiltration, anion exchange chromatography, and gel filtration, to 93% purity
-
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
-
of the reactivated recombinant enzyme, using mild acidification and anion-exchange chromatography on Q-Sepharose
-
partial
phenyl Sepharose column chromatography and Q Sepharose column chromatography
-
phenyl Sepharose column chromatography, Q Sepharose column chromatography, gel filtration
-
purchased and further purified by DEAE-Toyopearl 650M column chromatography
-
purification to homogeneity by hydrophobic interaction and ion-exchange chromatography
recombinant enzyme 2.4fold from Pichia pastoris culture supernatant by ultrafiltration, anion exchange chromatography, and gel filtration
recombinant extracellular enzyme 1.26fold from Pichia pastoris by anion 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
ultrafiltration, combined treatment with salts and Triton X-100 is followed by a significant increase in the effectiveness of ultrafiltration purification of the culture fluid
-
using ammonium sulfate precipitation, gel filtration, anion-exchange and hydrophobic-interaction chromatography
-
using an extraction step of the mycelium mass at pH 3.0, cation exchange chromatography on S-Sepharose and gel filtration on Sephacryl S-300
-
using column chromatography on DEAE-Sephadex, Sephacryl S-300 and DEAE-Sepharose
-
using dialysis, ammonium sulfate fractionation and column chromatography on DEAE-cellulose
-
using high performance hydrophobic-interaction chromatography on a pentylagarose column
-
using ion-exchange chromatography on DEAE-Sepharose and gel filtration chromatography on Sephacryl S-300
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of the gene encoding the enzyme and expression in Escherichia coli
-
construction of a recombinant strain, the recombinant strain produces up to four times more extracellular enzyme than wild type under identical conditions
-
expressed in Pichia pastoris strain GS115
expression in Escherichia coli, expression of all enzyme variants leads to the formation of insoluble inclusion bodies. Refolding of most variants can be followed by measuring increases in enzyme activity
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 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
-
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
gene GOX, DNA sequence determination and analysis, expression in a larger scale in Pichia pastoris strain X33 using the methanol inducible AOX1 promoter, the enzyme is secreted
gene gox, recombinant expression of the extracellular enzyme in Pichia pastoris strain GS115
gene gox, recombinant expression of wild-type and M12 mutant enzymes in Pichia pastoris strain KM71H or in Saccharomyces cerevisiae strain InvSc1
gene HaGox, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real time-PCR expression analysis
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
-
overexpressed either in Escherichia coli or in Pichia pastoris
recombinant enzyme expression in the periplasm or on the cell surface of Escherichia coli cells of different strains. The enzyme is differently tagged, i.e. expressed as Tat-AldO or INP-AldO, and exported to the periplasm or to the cell surface of the transformed cells, overview. AldO is successfully displayed at the surface of E. coli using a truncated INP variant, it contains covalently bound FAD, thus has attained a correctly folded and active conformation
-
recombinant expression of His-tagged enzyme in Pichia pastoris strain KM71H
recombinant expression of mutant enzyme B11 in Saccharomyces cerevisiae strain EBY100 cell wall
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
recombinant protein, expressed in Escherichia coli strain BL21, pET17b expression vector
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
GOX protein expression levels and GOX enzymatic activities increase with dietary glucose
transcript level of GOX increases with dietary carbohydrate levels, regardless of protein concentrations. GOX enzymatic activity increases with increasing dietary carbohydrates when caterpillars are fed protein-rich diets, but not when caterpillars are fed protein-poor diets, transcript levels increase over 2fold when caterpillars are fed carbohydrate-rich diets
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
refolding after treatment with 8 M urea and 30 mM dithiothreitol and subsequent dilution in a buffer containing reduced glutathione, FAD and glycerol
-
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
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
analysis
biofuel production
biotechnology
diagnostics
energy production
food industry
industry
medicine
-
analysis of the chronic inflammatory skin disorder Atopic eczema (AE)
pharmaceutical industry
-
enzyme immobilized both independently and together with catalase in gel of polyvinylalcohol in the form of membranes on cotton base, employment in food and pharmaceutical industries
synthesis
additional information
agriculture
-
the enzyme can be used as pest control agent against Ephestia kuehniella. The enzyme shows approximately similar damage on the Ephestia kuehniella midgut including rupture and disintegration of the epithelial layer and cellular vacuolization
agriculture
-
the enzyme shows antifungal activity. It could become a natural alternative to synthetic fungicides to control certain important plant microbial diseases. The enzyme displays a wide inhibitory spectrum toward different fungi at a concentration of 20 AU. It has a strong inhibitor effect on mycelia growth and spore germination of Pythium ultimum
agriculture
Aspergillus tubingensis CTM 507
-
the enzyme can be used as pest control agent against Ephestia kuehniella. The enzyme shows approximately similar damage on the Ephestia kuehniella midgut including rupture and disintegration of the epithelial layer and cellular vacuolization
-
agriculture
Aspergillus tubingensis CTM 507
-
the enzyme shows antifungal activity. It could become a natural alternative to synthetic fungicides to control certain important plant microbial diseases. The enzyme displays a wide inhibitory spectrum toward different fungi at a concentration of 20 AU. It has a strong inhibitor effect on mycelia growth and spore germination of Pythium ultimum
-
analysis
-
coupling of the enzyme with Fenton's reagent used for the determination of glucose produced as a result of the hydrolysis of cellobiose catalyzed by beta-glucosidase
analysis
-
phosphate sensor consisting of glucose oxidase coimmobilized with glutaraldehyde with maltose phosphorylase and bovine serum albumin
analysis
-
enzyme immobilized in Bombyx mori silk fibroin membrane applied to glucose sensor
analysis
-
immobilized enzyme on polyacrylamide employed for the determination of glucose concentration in blood sera
analysis
-
biosensor system prepared for continuous flow analysis of enzyme activity
analysis
-
application in glucose biosensors. An unmediated, reagentless glucose biosensor is prepared with two polyethylenimine/glucose oxidase bilayers-modified pyrolytic graphite electrodes. A calibration linear range of glucose is 0.5-8.9 mM with a detection limit of 0.05 mM and sensitivity of 0.76 microA per mM
analysis
-
the enzym eis used in a model system to study physiological effects of hepatic H2O2 release on rat liver
analysis
the enzyme finds wide application in food industry and clinical analysis
analysis
-
the enzyme is useful in designing of biosensors for use in clinical, biochemical, and diagnostic assays
analysis
-
the enzyme might by useful in designing of biosensors for use in clinical, biochemical, and diagnostic assays
analysis
-
co-confined glucose oxidase and horseradish peroxidase bienzyme system as a biosensor for the detection of glucose gives a wider linear range of glucose than for free enzymes in solution
analysis
-
the enzyme is useful as biosensor for glucose detection
analysis
-
GOx is the main component in glucose biosensors for determination of glucose in industrial solutions and in body fluids such as blood and urine
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
analysis
-
the enzyme finds wide application in food industry and clinical analysis
-
analysis
-
the enzyme might by useful in designing of biosensors for use in clinical, biochemical, and diagnostic assays
-
analysis
-
GOx is the main component in glucose biosensors for determination of glucose in industrial solutions and in body fluids such as blood and urine
-
analysis
-
the enzyme is useful in designing of biosensors for use in clinical, biochemical, and diagnostic assays
-
biofuel production
-
glucose oxidase is typically used in the anode of biofuel cells to oxidise glucose
biofuel production
-
used in miniature membrane-less glucose/O2 biofuel cells
biotechnology
-
the enzyme encapsulated in the liposomes composed of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine is a useful biocatalyst for the prolonged glucose oxidation
biotechnology
-
GOX is the most widely used enzyme for the development of electrochemical glucose biosensors and biofuel cell in physiological conditions
biotechnology
-
GOX is the most widely used enzyme for the development of electrochemical glucose biosensors and biofuel cell in physiological conditions
biotechnology
-
transgenic expression of glucose oxidase may be deployed to improve cold tolerance potential of higher plants
biotechnology
bacteriostatic agent. The combination of different concentrations of glucose oxidase and glucose could significantly inhibit the growth of Agrobacterium and Escherichia coli in logarithmic phase during the fermentation process
biotechnology
the enzyme is used for a number of applications in biotechnology and clinical diagnostics
biotechnology
Aspergillus niger ZM-8
-
bacteriostatic agent. The combination of different concentrations of glucose oxidase and glucose could significantly inhibit the growth of Agrobacterium and Escherichia coli in logarithmic phase during the fermentation process
-
diagnostics
-
glucose oxidase can be used in various immunoassays and/or staining procedures as well as removal of excess glucose, in real-time fluorescent microscopy for biological samples, glucose oxidase/catalase is often used for oxygen scavenging to reduce photodamage
diagnostics
-
used in an automatic glucose assay kit in conjunction with catalase and chiefly in biosensors for the detection and estimation of glucose in industrial solutions and in body fluids such as blood and urine
diagnostics
the enzyme is used as a molecular diagnostic and analytical tool in the medical industry for the control of diabetes
diagnostics
the enzyme is used for the manufacture of glucose biosensors and in particular sensor strips used to measure glucose levels in serum
diagnostics
a glassy carbon electrode (GCE) is modified with carbon nanochips (CNCs), and glucose oxidase (GOx) is immobilized on the modified electrode surface. Chitosan (CS) is employed to fix the GOx/CNCs tightly to the surface of the GCE. Characterization of the modified electrode shows that glucose oxidase remains in its native structure when immobilized in CNC film. Application in glucose biosensing and biofuel cells
diagnostics
the enzyme is used for a number of applications in biotechnology and clinical diagnostics
diagnostics
-
the enzyme is used for the manufacture of glucose biosensors and in particular sensor strips used to measure glucose levels in serum
-
energy production
design of a bioanode that directly utilizes starch as a fuel in an enzymatic biofuel cell. The enzymatic fuel cell is based on three enzymes (alpha-amylase, glucoamylase and glucose oxidase). The carbon paste electrode containing these three enzymes and tetrathiafulvalene can both saccharize and oxidize starchy biomass. In cyclic voltammetry, catalytic currents are successfully observed with both glucose and starchy white rice used as a substrate. A membraneless white rice/O2 biofuel cell is assembled and the electrochemical performance is evaluated. The three enzyme based electrode is used as a bioanode and an immobilized bilirubin oxidase (derived from Myrothecium verrucaria) electrode is used as a biocathode. The biofuel cell deliveres an open circuit voltage of 0.522 V and power density of up to 0.099 mW/cm
energy production
enzyme precipitates coatings of glucose oxidase onto carbon paper for biofuel cell applications. The direct immobilization of enzyme precipitation coatings on hierarchical-structured electrodes with a large surface area can further improve the power density of enzymatic biofuel cells and can make their applications more feasible
energy production
glucose oxidase/cellulose-carbon nanotube composite paper as a biocompatible bioelectrode for biofuel cells. Glucose oxidase, which is a redox enzyme capable of oxidizing glucose as a renewable fuel using oxygen, is immobilized on the CL-CNT composite paper. Cyclic voltammograms reveal that the GOx/CL-CNT paper electrode shows a pair of well-defined peaks, which agreed well with that of FAD/FADH2, the redox center of glucose oxidase. These results clearly show that the direct electron transfer between the glucose oxidase and the composite electrode is achieved. It is found that the glucose oxidase immobilized on the composite electrode retains catalytic activity for the oxidation of glucose
energy production
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
energy production
triphenylmethane dyes are an alternative for mediated electronic transfer systems in glucose oxidase biofuel cells
food industry
-
food and beverage additive, used for low alcohol wine production, used for glucose removal from dried egg, improvement of color, flavor, and shelf life of food materials, oxygen removal from fruit juices, canned beverages, and from mayonnaise to prevent rancidity, used as ingredient of toothpaste, for the production of gluconic acid, and as a food preservative
food industry
-
food processing-additive, used for bread making (GOX is an effective oxidant to produce bread with improved texture and increased loaf volume), and in dry egg powder, used as preservative in packaged food and for reduced alcohol wine production
food industry
the enzyme is used as food preservative and color stabilizer
food industry
Horseradish peroxidase, glucose oxidase, and glucose can be applied efficiently to modify several physicochemical properties (especially rheological and emulsifying properties) of soybean protein isolate. Soybean protein products are widely applied in processed foods as important ingredients, due to their higher nutritive values and desirable functional properties. Physical, chemical, and enzymatic modifications can be used to treat food proteins for property improvement
food industry
mutant enzyme Y169C/A211C is a good candidate for the bread baking industry. It has a significant effect on bread volume. Its improved thermostability, pH stability, and catalytic activity, its resistance to SDS, maximal enzymatic activity at low temperatures, and high activity under alkaline conditions are valuable properties that in addition to the bread baking industry
food industry
Penicillium sp. MX3343
potentially useful in food biopreservation, application for the preservation of aquatic products at low-temperatures, good antimicrobial effect against common fish pathogenic bacteria (Listeria monocytogenes and Vibrio parahaemolyticus), excellent freshness preserving agent in the context of the grass carp
food industry
the enzyme is used in clinical, pharmaceutical, food and chemical industries
food industry
Aspergillus niger ATCC 9202
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the enzyme is used in clinical, pharmaceutical, food and chemical industries
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food industry
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mutant enzyme Y169C/A211C is a good candidate for the bread baking industry. It has a significant effect on bread volume. Its improved thermostability, pH stability, and catalytic activity, its resistance to SDS, maximal enzymatic activity at low temperatures, and high activity under alkaline conditions are valuable properties that in addition to the bread baking industry
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industry
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oxygen scavenger, chemical bleaching, used for gluconic acid production and in glucose sensor/assays
industry
in the textile industry, enzyme GOX is used for bio-bleaching and in oral care products as antimicrobial agent
industry
the enzyme is used in clinical, pharmaceutical, food and chemical industries
industry
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in the textile industry, enzyme GOX is used for bio-bleaching and in oral care products as antimicrobial agent
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industry
Aspergillus niger ATCC 9202
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the enzyme is used in clinical, pharmaceutical, food and chemical industries
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synthesis
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preparative production of hydroquinone using a column packed with the enzyme immobilized onto alumina, O2 is replaced with benzoquinone
synthesis
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enzymatic biotransformation of (4R)-limonene to carvone involves addition of glucose oxidase and peroxidase to the biotransformation medium
synthesis
-
AldO is an enantioselective biocatalyst for the kinetic resolution of racemic 1,2-diols
synthesis
-
GOD is used as a commercial source of gluconic acid, which can be produced by the hydrolysis of delta-glucono-1, 5-lactone, the endproduct of GOD catalysis
synthesis
-
utilization of recombinant enzyme expressed in the periplasm or on the cell surface of Escherichia coli as biocatalyst in a non-laborious and non-costly whole-cell application for reacting on towards different polyols such as xylitol and sorbitol
synthesis
recombinant Aga2-GOx fusion proteins in the Saccharomyces cerevisiae cell wall can be used as immobilized catalysts for the production of gluconic acid
synthesis
the addition of ferrous ions (Fe2+) induces the formation of hydroxyl radicals from the hydrogen peroxide, which act as initiating species for the microgel synthesis. Poly(N-vinyl)caprolactam (PVCL) microgels are synthesized by precipitation polymerization initiated by the enzyme and a conventional azo-initiator 2,2'-azobis(N-(2-carboxyethyl)-2-methylpropionamidine) tetrahydrate. The use of enzymes in precipitation polymerization leads to the encapsulation of enzymes in formed microgels. After the GOx-induced polymerization and purification of the microgels, high enzyme activity could be determined in the microgels, enabling facile synthesis of core-shell microgels. The glucose oxidase-based initiator system is a powerful and promising alternative to azo- or peroxide-initiated polymerization, leading to the formation of polymers at low synthesis temperatures
synthesis
-
utilization of recombinant enzyme expressed in the periplasm or on the cell surface of Escherichia coli as biocatalyst in a non-laborious and non-costly whole-cell application for reacting on towards different polyols such as xylitol and sorbitol
-
synthesis
-
AldO is an enantioselective biocatalyst for the kinetic resolution of racemic 1,2-diols
-
additional information
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GOx bioactive paper is fabricated, which can potentially be used as food packaging paper
additional information
despite the broad range of applications for glucose oxidase, the effectiveness of glucose oxidase is restricted by the narrow substrate range of this enzyme and susceptibility to H2O2 inactivation
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Release 2023.1 (January 2023)
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