1.1.3.4: glucose oxidase
This is an abbreviated version!
For detailed information about glucose oxidase, go to the full flat file.
Word Map on EC 1.1.3.4
-
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
- 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
Reaction
Synonyms
AldO, beta-D-glucose oxidase, beta-D-glucose oxygen-1-oxidoreductase, beta-D-glucose/oxygen 1-oxidoreductase, beta-D-glucose: oxygen 1-oxidoreductase, beta-D-glucose:O2 1-oxidoreductase, beta-D-glucose:O2-1-oxidoreductase, beta-D-glucose:oxygen 1-oxido-reductase, beta-D-glucose:oxygen 1-oxidoreductase, beta-D-glucose:oxygen oxidoreductase, beta-D-glucose:oxygen-1-oxidoreductase, beta-D-glucose:quinone oxidoreductase, CngoxA, corylophyline, D-glucose oxidase, D-glucose-1-oxidase, deoxin-1, glucose aerodehydrogenase, glucose oxyhydrase, glucose-1-oxidase, GO-2, GOD, GOX, GOxP5, microcid, More, notatin, oxidase, glucose, pen-GOx, penatin, yGOXpenag
ECTree
1.1.3.4 glucose oxidaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 1.1.3.4 - glucose oxidase
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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
-
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
-
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
-
-
?
