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Information on EC 1.1.3.4 - glucose oxidase
for references in articles please use BRENDA:EC1.1.3.4
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.3 With oxygen as acceptor
1.1.3.4 glucose oxidase
IUBMB Comments
A flavoprotein (FAD).
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 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
showSynonyms
glucose oxidase, d-glucose oxidase, microcid, goxp5, ygoxpenag, cngoxa, beta-d-glucose oxidase, notatin, glucose aerodehydrogenase, beta-d-glucose oxygen 1-oxidoreductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AldO
beta-D-glucose oxidase
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-
-
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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
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-
-
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beta-D-glucose:oxygen 1-oxidoreductase
beta-D-glucose:oxygen-1-oxidoreductase
beta-D-glucose:quinone oxidoreductase
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CngoxA
corylophyline
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-
-
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D-glucose oxidase
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-
-
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D-glucose-1-oxidase
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-
-
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deoxin-1
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-
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glucose aerodehydrogenase
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-
-
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glucose oxyhydrase
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-
-
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GO-2
GOD
GOX
microcid
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-
-
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notatin
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-
-
-
oxidase, glucose
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-
-
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penatin
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additional information
GOD
-
-
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GOX
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GOX
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2
stereochemistry
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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
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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
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
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-
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
MetaCyc
2-deoxy-D-glucose 6-phosphate degradation
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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
LITERATURE
COMMENTARY
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
-
Substrates: -
Products: product identification by NMR
Products: product identification by NMR
?
1,2-pentanediol + O2
2-hydroxypentanoate + H2O2
-
Substrates: -
Products: product identification by NMR
Products: product identification by NMR
?
1,3-butanediol + O2
2-hydroxypropanal + H2O2
-
Substrates: -
Products: product identification by GC-MS
Products: product identification by GC-MS
?
1-phenyl-1,2-ethanediol + O2
hydroxy(phenyl)ethanoic acid + H2O2
-
Substrates: -
Products: -
Products: -
r
2-deoxy-6-fluoro-D-glucose + O2 + H2O
2-deoxy-6-fluoro-D-glucono-1,5-lactone + H2O2
-
Substrates: 1.85% relative activity to beta-D-glucose
Products: -
Products: -
?
2-deoxy-D-glucose + O2
?
Substrates: 19.6% of the activity with D-glucose for the native enzyme, 5.9 for the recombinant enzyme
Products: -
Products: -
?
3,6-methyl-D-glucose + O2 + H2O
3,6-methyl-D-glucono-1,5-lactone + H2O2
-
Substrates: 1.85% relative activity to beta-D-glucose
Products: -
Products: -
?
3-deoxy-D-glucose + O2 + H2O
3-deoxy-D-glucono-1,5-lactone + H2O2
-
Substrates: 1% relative activity to D-glucose
Products: -
Products: -
?
4,6-methyl-D-glucose + O2 + H2O
4,6-methyl-D-glucono-1,5-lactone + H2O2
-
Substrates: 1.22% relative activity to beta-D-glucose
Products: -
Products: -
?
4-deoxy-d-glucose + O2
? + H2O2
-
Substrates: 7% of the activity compared to beta-D-glucose
Products: -
Products: -
?
4-deoxy-D-glucose + O2 + H2O
4-deoxy-D-glucono-1,5-lactone + H2O2
-
Substrates: 2% relative activity to D-glucose
Products: -
Products: -
?
4-O-methy-D-glucose + O2 + H2O
4-O-methyl-D-glucono-1,5-lactone + H2O2
-
Substrates: 15% relative activity to D-glucose
Products: -
Products: -
?
4-O-methyl-D-glucose + O2
4-O-methyl-D-glucono-1,5-lactone + H2O2
-
Substrates: 8% activity compared to beta-D-glucose
Products: -
Products: -
?
4-O-methyl-D-glucose + O2
? + H2O2
-
Substrates: 8% of the activity compared to beta-D-glucose
Products: -
Products: -
?
6-deoxy-6-fluoro-D-glucose + O2 + H2O
6-deoxy-6-fluoro-D-glucono-1,5-lactone + H2O2
-
Substrates: 3% relative activity to beta-D-glucose, when determined with an unspecified enzyme at 0.5 M substrate concentration
Products: -
Products: -
?
6-deoxy-D-glucose + O2
6-deoxy-D-glucono-1,5-lactone + H2O2
-
Substrates: 12% activity compared to beta-D-glucose
Products: -
Products: -
?
6-deoxy-d-glucose + O2
? + H2O2
-
Substrates: 12% of the activity compared to beta-D-glucose
Products: -
Products: -
?
6-deoxy-D-glucose + O2 + H2O
6-deoxy-D-glucono-1,5-lactone + H2O2
-
Substrates: 10% relative activity to D-glucose
Products: -
Products: -
?
6-O-methyl-D-glucose + O2 + H2O
6-O-methyl-D-glucono-1,5-lactone + H2O2
-
Substrates: 1% relative activity to D-glucose
Products: -
Products: -
?
alpha-methyl-D-glucoside + O2 + H2O
? + H2O2
-
Substrates: 13% relative activity to D-glucose
Products: -
Products: -
?
beta-D-glucose + 1,2-naphthoquinone
D-glucono-1,5-lactone + ?
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + 1,2-naphthoquinone-4-sulfonic acid
D-glucono-1,5-lactone + ?
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + 4-benzoquinone
D-glucono-1,5-lactone + 4-benzoquinol
-
Substrates: -
Products: -
Products: -
r
beta-D-glucose + benzoquinone
D-glucono-1,5-lactone + hydroquinone
-
Substrates: enzyme immobilized onto alumina
Products: immobilized enzyme, yield of conversion: 100%
Products: immobilized enzyme, yield of conversion: 100%
?
beta-D-glucose + methyl-1,4-benzoquinone
D-glucono-1,5-lactone + ?
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + N,N,N',N'-tetramethyl-1,4-phenylenediamine
?
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Substrates: -
Products: -
Products: -
r
beta-D-glucose + p-benzoquinone
D-glucono-1,5-lactone + ?
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Substrates: -
Products: -
Products: -
?
beta-D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + ?
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + potassium ferricyanide
D-glucono-1,5-lactone + ?
-
Substrates: -
Products: -
Products: -
?
cellobiose + O2 + H2O
? + H2O2
-
Substrates: 13% relative activity to D-glucose
Products: -
Products: -
?
D-fructose + O2
?
Substrates: 4.9% of the activity with D-glucose for the native enzyme, no activity with the recombinant enzyme
Products: -
Products: -
?
D-fructose + O2 + H2O
? + H2O2
-
Substrates: 4.9% relative activity to D-glucose
Products: -
Products: -
?
D-galactose + O2 + H2O
? + H2O2
-
Substrates: recombinant enzyme
Products: -
Products: -
?
D-glucono-1,5-lactone + O2 + H2O
? + H2O2
-
Substrates: 80% relative activity to D-glucose
Products: -
Products: -
?
D-glucose + di-(2,2'-bipyridinyl)ruthenium(III)dichloride
D-glucono-1,5-lactone + di-(2,2'-bipyridinyl)ruthenium(II)dichloride
-
Substrates: -
Products: -
Products: -
?
D-glucose + [(1,10-phenanthroline)2(Cl)2Ru(III)]
D-glucono-1,5-lactone + [(1,10-phenanthroline)2(Cl)2Ru(II)]
-
Substrates: -
Products: -
Products: -
?
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-
-
Substrates: -
Products: -
Products: -
?
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)]
-
Substrates: -
Products: -
Products: -
?
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-
-
Substrates: -
Products: -
Products: -
?
D-glucose + [(2,2'-bipyridine)2(CO32-)1/2Ru(III)]
D-glucono-1,5-lactone + [(2,2'-bipyridine)2(CO32-)1/2Ru(II)]
-
Substrates: -
Products: -
Products: -
?
D-glucose + [(2,2'-bipyridine)2(H2O)2Ru(III)]PF6-
D-glucono-1,5-lactone + [(2,2'-bipyridine)2(H2O)2Ru(II)]PF6-
-
Substrates: -
Products: -
Products: -
?
D-glucose + [(2,2'-bipyridine)2(SCN-)2Ru(III)]
D-glucono-1,5-lactone + [(2,2'-bipyridine)2(SCN-)2Ru(II)]
-
Substrates: -
Products: -
Products: -
?
D-glucose + [(2,2'-bipyridine)3Ru(II)]PF6-
D-glucono-1,5-lactone + [(2,2'-bipyridine)3Ru(III)]PF6-
-
Substrates: -
Products: -
Products: -
?
D-glucosone + O2 + H2O
? + H2O2
-
Substrates: 30% relative activity to beta-D-glucose
Products: -
Products: -
?
D-maltose + O2 + H2O
?
-
Substrates: 4.5% of D-glucose reactivity
Products: -
Products: -
?
D-mannose + O2
? + H2O2
-
Substrates: 9% activity compared to beta-D-glucose
Products: -
Products: -
?
galactose + O2 + H2O
D-galactono-1,5-lactone + H2O2
-
Substrates: 18% of the activity with beta-D-glucose
Products: -
Products: -
?
L-gulono-gamma-lactone + O2 + H2O
? + H2O2
-
Substrates: 62% relative activity to D-glucose
Products: -
Products: -
?
maltose + O2
?
Substrates: 21.3% of the activity with D-glucose for the native enzyme, 42.2% for the recombinant enzyme
Products: -
Products: -
?
2-deoxy-D-glucose + O2
2-deoxy-D-glucono-1,5-lactone + H2O2
-
Substrates: 10% activity compared to beta-D-glucose
Products: -
Products: -
?
2-deoxy-D-glucose + O2
2-deoxy-D-glucono-1,5-lactone + H2O2
-
Substrates: 10% activity compared to beta-D-glucose
Products: -
Products: -
?
2-deoxy-d-glucose + O2
? + H2O2
-
Substrates: 10% of the activity compared to beta-D-glucose
Products: -
Products: -
?
2-deoxy-d-glucose + O2
? + H2O2
-
Substrates: 10% of the activity compared to beta-D-glucose
Products: -
Products: -
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
Substrates: -
Products: -
Products: -
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
Substrates: 20% relative activity to D-glucose
Products: -
Products: -
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
Substrates: 30% relative activity to beta-D-glucose
Products: -
Products: -
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
Substrates: 25% relative activity to beta-D-glucose
Products: -
Products: -
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
Substrates: low GOD activity
Products: -
Products: -
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
Substrates: recombinant enzyme
Products: -
Products: -
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
Substrates: 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
Products: -
Products: -
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
Substrates: 38% relative activity to D-glucose
Products: -
Products: -
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
Substrates: 36% of the activity with beta-D-glucose
Products: -
Products: -
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
Substrates: 36% of the activity with beta-D-glucose
Products: -
Products: -
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
Substrates: 19.6% relative activity to D-glucose
Products: -
Products: -
?
3,6-methyl-D-glucose + O2
3-O,6-O-dimethyl-D-glucono-1,5-lactone + H2O2
-
Substrates: 10% activity compared to beta-D-glucose
Products: -
Products: -
?
3,6-methyl-D-glucose + O2
3-O,6-O-dimethyl-D-glucono-1,5-lactone + H2O2
-
Substrates: 10% activity compared to beta-D-glucose
Products: -
Products: -
?
3,6-methyl-D-glucose + O2
? + H2O2
-
Substrates: 10% of the activity compared to beta-D-glucose
Products: -
Products: -
?
3,6-methyl-D-glucose + O2
? + H2O2
-
Substrates: 10% of the activity compared to beta-D-glucose
Products: -
Products: -
?
4-deoxy-D-glucose + O2
4-deoxy-D-glucono-1,5-lactone + H2O2
-
Substrates: 7% activity compared to beta-D-glucose
Products: -
Products: -
?
4-deoxy-D-glucose + O2
4-deoxy-D-glucono-1,5-lactone + H2O2
-
Substrates: 7% activity compared to beta-D-glucose
Products: -
Products: -
?
alpha-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
Substrates: 0.64% relative activity to beta-D-glucose
Products: -
Products: -
?
alpha-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
Substrates: very slow reaction
Products: -
Products: -
?
beta-D-glucose + 1,4-benzoquinone
D-glucono-1,5-lactone + hydroquinone
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + 1,4-benzoquinone
D-glucono-1,5-lactone + hydroquinone
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + ?
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + ?
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + ?
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + ferrocinium-methanol
?
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: -
Products: -
Products: -
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: -
Products: -
Products: -
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: -
Products: -
Products: -
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: -
Products: -
Products: -
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: -
Products: -
Products: -
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: -
Products: -
Products: -
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: -
Products: -
Products: -
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: 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
Products: -
Products: -
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: 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
Products: -
Products: -
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: immobilization of biocatalysts in a membranous form, glucose oxidase as a model protein for biosensor analysis
Products: -
Products: -
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: 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
Products: -
Products: -
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
Substrates: 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
Products: -
Products: -
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: 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
Products: -
Products: -
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: cofactor FAD is transiently reduced along the reaction mechanism
Products: -
Products: -
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
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Substrates: enzymatic oxidation by glucose oxidase reduces FAD to FADH2, releasing H2O2 in the presence of O2
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: enzyme assay using the ABTS/horseradish peroxidase system
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: the enzyme is highly specific for D-glucose
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: 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
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: 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
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: -
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: cofactor FAD is transiently reduced along the reaction mechanism
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
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Substrates: -
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
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Substrates: enzymatic oxidation by glucose oxidase reduces FAD to FADH2, releasing H2O2 in the presence of O2
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
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Substrates: -
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
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Substrates: -
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
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Substrates: 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
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Aspergillus tubingensis CTM 507
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Aspergillus tubingensis CTM 507
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Substrates: 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
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: -
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: -
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
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Substrates: -
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
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Substrates: -
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
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Substrates: -
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: -
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
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Substrates: -
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
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Substrates: -
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: -
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: 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
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: 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
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: -
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
Substrates: enzymatic oxidation by glucose oxidase reduces FAD to FADH2, releasing H2O2 in the presence of O2
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
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Substrates: -
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
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Substrates: via cofactor FAD reduction to FADH2, reaction cycles, FADH2 reduces O2, overview
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
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Substrates: -
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
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Substrates: via cofactor FAD reduction to FADH2, reaction cycles, FADH2 reduces O2, overview
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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
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Substrates: -
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