Information on EC 1.1.3.4 - glucose oxidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.1.3.4
-
RECOMMENDED NAME
GeneOntology No.
glucose oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
Pentose phosphate pathway
-
-
SYSTEMATIC NAME
IUBMB Comments
beta-D-glucose:oxygen 1-oxidoreductase
A flavoprotein (FAD).
CAS REGISTRY NUMBER
COMMENTARY hide
9001-37-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain NFCCP
-
-
Manually annotated by BRENDA team
strain NRRL-3
-
-
Manually annotated by BRENDA team
strain Z-25
SwissProt
Manually annotated by BRENDA team
No.319
-
-
Manually annotated by BRENDA team
No.319
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cellular organism
northeastern fall-flower honey
-
-
Manually annotated by BRENDA team
strain ATCC 42132
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Mycoderma aceti
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
strain CBS 120262
-
-
Manually annotated by BRENDA team
strain CBS 120262
-
-
Manually annotated by BRENDA team
apple blue mold, strain O-385-10
-
-
Manually annotated by BRENDA team
Penicillium sp. CBS 120262
strain CBS 120262, two isozymes
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
strain A3(2)
-
-
Manually annotated by BRENDA team
strain 46.1
-
-
Manually annotated by BRENDA team
strain 46.1
-
-
Manually annotated by BRENDA team
strain P16
SwissProt
Manually annotated by BRENDA team
commercial preparation
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-1-phenyl-1,2-ethanediol + O2
(2R)-hydroxy(phenyl)ethanoic acid + H2O2
show the reaction diagram
-
-
product identification by NMR
-
?
(R)-1-phenyl-1,2-ethanediol + O2
?
show the reaction diagram
-
-
-
-
?
(S)-1-phenyl-1,2-ethanediol + O2
?
show the reaction diagram
-
-
-
-
?
1,2,4-butanetriol + O2
?
show the reaction diagram
-
-
-
-
?
1,2-butanediol + O2
?
show the reaction diagram
-
-
-
-
?
1,2-hexanediol + O2
?
show the reaction diagram
-
-
-
-
?
1,2-pentanediol + O2
2-hydroxypentanoate + H2O2
show the reaction diagram
-
-
product identification by NMR
-
?
1,3-butanediol + O2
2-hydroxypropanal + H2O2
show the reaction diagram
-
-
product identification by GC-MS
-
?
2-amino-1-pentanol + O2
?
show the reaction diagram
-
-
-
-
?
2-deoxy-6-fluoro-D-glucose + O2 + H2O
2-deoxy-6-fluoro-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
1.85% relative activity to beta-D-glucose
-
?
2-deoxy-D-glucose + O2
?
show the reaction diagram
19.6% of the activity with D-glucose for the native enzyme, 5.9 for the recombinant enzyme
-
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
show the reaction diagram
3,6-methyl-D-glucose + O2 + H2O
3,6-methyl-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
1.85% relative activity to beta-D-glucose
-
?
3-butene-1,2-diol + O2
?
show the reaction diagram
-
-
-
-
?
3-butenol + O2
?
show the reaction diagram
-
-
-
-
?
3-deoxy-D-glucose + O2 + H2O
3-deoxy-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
1% relative activity to D-glucose
-
?
4,6-methyl-D-glucose + O2 + H2O
4,6-methyl-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
1.22% relative activity to beta-D-glucose
-
?
4-deoxy-D-glucose + O2 + H2O
4-deoxy-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
2% relative activity to D-glucose
-
?
4-O-methy-D-glucose + O2 + H2O
4-O-methyl-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
15% relative activity to D-glucose
-
?
4-pentene-1,2-diol + O2
?
show the reaction diagram
-
-
-
-
?
6-deoxy-6-fluoro-D-glucose + O2 + H2O
6-deoxy-6-fluoro-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
3% relative activity to beta-D-glucose, when determined with an unspecified enzyme at 0.5 M substrate concentration
-
?
6-deoxy-D-glucose + O2 + H2O
6-deoxy-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
10% relative activity to D-glucose
-
?
6-O-methyl-D-glucose + O2 + H2O
6-O-methyl-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
1% relative activity to D-glucose
-
?
alpha-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
alpha-methyl-D-glucoside + O2 + H2O
? + H2O2
show the reaction diagram
-
13% relative activity to D-glucose
-
?
beta-D-glucose
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
-
-
-
?
beta-D-glucose + 1,2-naphthoquinone
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
beta-D-glucose + 1,2-naphthoquinone-4-sulfonic acid
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
beta-D-glucose + 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + ?
show the reaction diagram
beta-D-glucose + benzoquinone
D-glucono-1,5-lactone + hydroquinone
show the reaction diagram
-
enzyme immobilized onto alumina
immobilized enzyme, yield of conversion: 100%
?
beta-D-glucose + ferrocinium-methanol
?
show the reaction diagram
beta-D-glucose + methyl-1,4-benzoquinone
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
beta-D-glucose + p-benzoquinone
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
beta-D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
beta-D-glucose + potassium ferricyanide
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
cellobiose + O2 + H2O
? + H2O2
show the reaction diagram
-
13% relative activity to D-glucose
-
?
D-fructose + O2
?
show the reaction diagram
4.9% of the activity with D-glucose for the native enzyme, no activity with the recombinant enzyme
-
-
?
D-fructose + O2 + H2O
? + H2O2
show the reaction diagram
-
4.9% relative activity to D-glucose
-
?
D-galactose + O2 + H2O
?
show the reaction diagram
-
low GOD activity
-
-
?
D-galactose + O2 + H2O
? + H2O2
show the reaction diagram
-
recombinant enzyme
-
?
D-glucono-1,5-lactone + O2 + H2O
? + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
D-glucose + [(1,10-phenanthroline)2(Cl)2Ru(III)]
D-glucono-1,5-lactone + [(1,10-phenanthroline)2(Cl)2Ru(II)]
show the reaction diagram
-
-
-
-
?
D-glucose + [(1,8-dimethyl-4,5-phenanthroline)3Ru(II)]PF6-
D-glucono-1,5-lactone + [(1,8-dimethyl-4,5-phenanthroline)3Ru(III)]PF6-
show the reaction diagram
-
-
-
-
?
D-glucose + [(2,2'-(4,4'dimethyl)bipyridine)2(Cl)2Ru(III)]
D-glucono-1,5-lactone + [(2,2'-(4,4'dimethyl)bipyridine)2(Cl)2Ru(II)]
show the reaction diagram
-
-
-
-
?
D-glucose + [(2,2'-(4,4'dimethyl)bipyridine)2(Cl)2Ru(III)]PF6-
D-glucono-1,5-lactone + [(2,2'-(4,4'dimethyl)bipyridine)2(Cl)2Ru(II)]PF6-
show the reaction diagram
-
-
-
-
?
D-glucose + [(2,2'-bipyridine)2(CO32-)1/2Ru(III)]
D-glucono-1,5-lactone + [(2,2'-bipyridine)2(CO32-)1/2Ru(II)]
show the reaction diagram
-
-
-
-
?
D-glucose + [(2,2'-bipyridine)2(H2O)2Ru(III)]PF6-
D-glucono-1,5-lactone + [(2,2'-bipyridine)2(H2O)2Ru(II)]PF6-
show the reaction diagram
-
-
-
-
?
D-glucose + [(2,2'-bipyridine)2(SCN-)2Ru(III)]
D-glucono-1,5-lactone + [(2,2'-bipyridine)2(SCN-)2Ru(II)]
show the reaction diagram
-
-
-
-
?
D-glucose + [(2,2'-bipyridine)3Ru(II)]PF6-
D-glucono-1,5-lactone + [(2,2'-bipyridine)3Ru(III)]PF6-
show the reaction diagram
-
-
-
-
?
D-glucosone + O2 + H2O
? + H2O2
show the reaction diagram
-
30% relative activity to beta-D-glucose
-
?
D-maltose + O2 + H2O
?
show the reaction diagram
D-maltose + O2 + H2O
? + H2O2
show the reaction diagram
D-mannitol + O2
?
show the reaction diagram
D-mannose + O2
?
show the reaction diagram
D-mannose + O2 + H2O
?
show the reaction diagram
-
low GOD activity
-
-
?
D-sorbitol + O2
?
show the reaction diagram
D-xylose + O2
?
show the reaction diagram
D-xylose + O2 + H2O
?
show the reaction diagram
D-xylose + O2 + H2O
? + H2O2
show the reaction diagram
galactose + O2 + H2O
D-galactono-1,5-lactone + H2O2
show the reaction diagram
-
18% of the activity with beta-D-glucose
-
-
?
glycerol + O2
?
show the reaction diagram
-
-
-
-
?
L-arabinose + O2
?
show the reaction diagram
L-gulono-gamma-lactone + O2 + H2O
? + H2O2
show the reaction diagram
-
62% relative activity to D-glucose
-
?
L-sorbose + O2 + H2O
?
show the reaction diagram
L-threitol + O2
?
show the reaction diagram
-
-
-
-
?
maltose + O2
?
show the reaction diagram
21.3% of the activity with D-glucose for the native enzyme, 42.2% for the recombinant enzyme
-
-
?
mannose + O2 + H2O
? + H2O2
show the reaction diagram
sorbitol + O2
?
show the reaction diagram
xylitol + O2
?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
D-mannitol + O2
?
show the reaction diagram
D-sorbitol + O2
?
show the reaction diagram
sorbitol + O2
?
show the reaction diagram
xylitol + O2
?
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
-
both the thermal and chemical denaturation of the enzyme cause dissociation of the flavin cofactor
Flavin-hypoxanthine dinucleotide
-
FHD, can substitute FAD
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
active site bound, required
Iron
-
the enzyme contains 2 mol of iron per 160000 Da
Na+
cellular organism
-
required for maximal activity, honey enzyme
additional information
-
no activition by Ca2+ and Ba2+ at 1 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-butyl-1-methylpyrrolidinium tetrafluoroborate
-
the presence of 1-butyl-1-methylpyrrolidinium tetrafluoroborate on the surface of single-walled carbon nanotubes can significantly affect the electrical transfer properties of the nanotube and lead to the decrease of the electrocatalytic activity of the GOx
1-butyl-3-methylimidazolium tetrafluoroborate
-
the presence of 1-butyl-3-methylimidazolium tetrafluoroborate on the surface of single-walled carbon nanotubes can significantly affect the electrical transfer properties of the nanotube and lead to the decrease of the electrocatalytic activity of the GOx
1-butyl-3-methylpyridinium tetrafluoroborate
-
the presence of 1-butyl-3-methylpyridinium tetrafluoroborate on the surface of single-walled carbon nanotubes can significantly affect the electrical transfer properties of the nanotube and lead to the decrease of the electrocatalytic activity of the GOx
2-deoxy-D-glucose
-
-
4-chloromercuribenzoate
-
-
8-hydroxyquinoline
adenine nucleotides
-
inhibition of FAD-binding to apoprotein
AgNO3
-
24% activity remains at 10 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
arsenite
-
-
Ba2+
-
70% residual activity at 1 mM
Cd2+
-
60% residual activity at 1 mM
CuCl2
-
6.5% activity remains at 10 mM
D-arabinose
-
-
D-glucono-delta-lactone
-
weak competitive inhibitor of GOD
dimedone
FeSO4
-
inhibition of enzyme production
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
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 25C because the H2O2 concentration is kept negligible low both outside and inside liposomes throughout the reaction
hydrazine
hydroxylamine
K+
-
97% residual activity at 1 mM
NaCl
-
50% inhibition at a concentration of 4%
NaF
-
72% activity remains at 10 mM
NaHSO4
-
40% inhibition at 1 mM
o-phthalate
oxygen
p-chloromercuribenzoate
-
-
Pb2+
-
45% residual activity at 1 mM
phenylhydrazine
phenylmercuric acetate
putrescine
-
i.e. 1,4-diaminobutane
ribose
-
incubation of Aspergillus niger glucose oxidase with 1 mM ribose for up to 8 days results in 96% loss in activity
Semicarbazide
sodium bisulfate
-
-
Sodium bisulfite
-
partial
Sodium cholate
-
non-competitive inhibition in microemulsion
Sodium nitrate
-
13% inhibition at 10 mM
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
p-chloromercuribenzoate
-
substancial stimulation
Sodium nitrate
-
substancial stimulation
trehalose
-
trehalose does not affect Vmax but instead decreases Km and as a result enzyme efficiency is increased
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.
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10
(R)-1-phenyl-1,2-ethanediol
-
pH 7.5, 30C
86
(S)-1-phenyl-1,2-ethanediol
-
pH 7.5, 30C
170
1,2,4-butanetriol
-
pH 7.5, 30C
150
1,2-Butanediol
-
pH 7.5, 30C
97
1,2-hexanediol
-
pH 7.5, 30C
52
1,2-pentanediol
-
pH 7.5, 30C
3.33
1,4-benzoquinone
-
pH 5.5, 35C
83
1-phenyl-1,2-ethanediol
-
pH 7.5, 30C
0.0368
2,6-dichloroindophenol
-
-
35
2-amino-1-pentanol
-
pH 7.5, 30C
8.3 - 49.8
2-deoxy-D-glucose
250
3-butene-1,2-diol
-
pH 7.5, 30C
480
3-butenol
-
pH 7.5, 30C
42
4-pentene-1,2-diol
-
pH 7.5, 30C
0.019 - 733
beta-D-glucose
162
D-fructose
-
-
76.9 - 952
D-galactose
12.5 - 26
D-glucose
55.5 - 117
D-maltose
36
D-mannitol
-
pH 7.5, 30C
44 - 106
D-mannose
1.4
D-sorbitol
-
pH 7.5, 30C
33 - 384
D-xylose
0.19
di-(2,2'-bipyridinyl)ruthenium(III)dichloride
-
pH 7.3, 30C
0.0638 - 0.1107
ferrocinium-methanol
350
glycerol
-
pH 7.5, 30C
430
L-arabinose
-
pH 7.5, 30C
25
L-Threitol
-
pH 7.5, 30C
2.9 - 7
methyl-1,4-benzoquinone
0.18 - 0.95
O2
2.43
phenazine methosulfate
-
pH 4.7
0.32
xylitol
-
pH 7.5, 30C
0.694
[(1,10-phenanthroline)2(Cl)2Ru(III)]
-
pH 7.3, 30C
0.019
[(1,8-dimethyl-4,5-phenanthroline)3Ru(II)]PF6-
-
pH 7.3, 30C
0.52
[(2,2'-(4,4'dimethyl)bipyridine)2(Cl)2Ru(III)]
-
pH 7.3, 30C
0.0313
[(2,2'-(4,4'dimethyl)bipyridine)2(Cl)2Ru(III)]PF6-
-
pH 7.3, 30C
0.0922
[(2,2'-bipyridine)2(CO32-)1/2Ru(III)]
-
pH 7.3, 30C
0.153
[(2,2'-bipyridine)2(H2O)2Ru(III)]PF6-
-
pH 7.3, 30C
0.0513
[(2,2'-bipyridine)2(SCN-)2Ru(III)]
-
pH 7.3, 30C
0.057
[(2,2'-bipyridine)3Ru(II)]PF6-
-
pH 7.3, 30C
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.74
(R)-1-phenyl-1,2-ethanediol
Streptomyces coelicolor
-
pH 7.5, 30C
0.008
(S)-1-phenyl-1,2-ethanediol
Streptomyces coelicolor
-
pH 7.5, 30C
4.4
1,2,4-butanetriol
Streptomyces coelicolor
-
pH 7.5, 30C
0.29
1,2-Butanediol
Streptomyces coelicolor
-
pH 7.5, 30C
2
1,2-hexanediol
Streptomyces coelicolor
-
pH 7.5, 30C
0.85
1,2-pentanediol
Streptomyces coelicolor
-
pH 7.5, 30C
0.36
1-phenyl-1,2-ethanediol
Streptomyces coelicolor
-
pH 7.5, 30C
1.13
2,6-dichloroindophenol
Pleurotus ostreatus
-
-
0.017
2-amino-1-pentanol
Streptomyces coelicolor
-
pH 7.5, 30C
0.34
3-butene-1,2-diol
Streptomyces coelicolor
-
pH 7.5, 30C
0.1
3-butenol
Streptomyces coelicolor
-
pH 7.5, 30C
15.5
4-benzoquinone
Pleurotus ostreatus
-
-
0.35
4-pentene-1,2-diol
Streptomyces coelicolor
-
pH 7.5, 30C
0.03 - 2003
beta-D-glucose
0.59 - 318.2
D-glucose
9.2
D-mannitol
Streptomyces coelicolor
-
pH 7.5, 30C
17
D-sorbitol
Streptomyces coelicolor
-
pH 7.5, 30C
35.4
di-(2,2'-bipyridinyl)ruthenium(III)dichloride
Aspergillus niger
-
pH 7.3, 30C
1.6
glycerol
Streptomyces coelicolor
-
pH 7.5, 30C
1.7
L-arabinose
Streptomyces coelicolor
-
pH 7.5, 30C
6.3
L-Threitol
Streptomyces coelicolor
-
pH 7.5, 30C
0.33
N,N,N',N'-tetramethyl-1,4-phenylenediamine
Pleurotus ostreatus
-
-
13
xylitol
Streptomyces coelicolor
-
pH 7.5, 30C
10.5
[(1,10-phenanthroline)2(Cl)2Ru(III)]
Aspergillus niger
-
-
50.3
[(1,8-dimethyl-4,5-phenanthroline)3Ru(II)]PF6-
Aspergillus niger
-
pH 7.3, 30C
10.5
[(2,2'-(4,4'dimethyl)bipyridine)2(Cl)2Ru(III)]
Aspergillus niger
-
pH 7.3, 30C
13.8
[(2,2'-(4,4'dimethyl)bipyridine)2(Cl)2Ru(III)]PF6-
Aspergillus niger
-
pH 7.3, 30C
38.6
[(2,2'-bipyridine)2(CO32-)1/2Ru(III)]
Aspergillus niger
-
pH 7.3, 30C
8.3
[(2,2'-bipyridine)2(H2O)2Ru(III)]PF6-
Aspergillus niger
-
pH 7.3, 30C
31.4
[(2,2'-bipyridine)2(SCN-)2Ru(III)]
Aspergillus niger
-
pH 7.3, 30C
158
[(2,2'-bipyridine)3Ru(II)]PF6-
Aspergillus niger
-
pH 7.3, 30C
additional information
additional information
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004 - 323
beta-D-glucose
0.017 - 0.027
ferrocinium-methanol
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
39.8
ammonium chloride
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.33
secreted enzyme in crude cell culture supernatant
3.1
-
in the culture filtrate
6
-
after isolation from the fermenter liquid by gel filtration, lyophilized preparate
15.1
-
oxidation of o-dianisidine at 37C and pH 4.5
17.3
-
substrate xylitol
100
-
immobilized enzyme, pH 5.5, temperature not specified in the publication, high enzyme concentration
135
-
purified enzyme
144
purified recombinant enzyme
153.5
recombinant enzyme after 3.34fold purification, at 35C
172
-
purified enzyme
189
-
GOD-His6 expressed in wild-type cells of Saccharomyces cerevisiae
194
-
GOD-His6 expressed in pmr1DELTA mutant cells of Saccharomyces cerevisiae
216
-
immobilized enzyme, pH 5.5, temperature not specified in the publication, low enzyme concentration
240.5
-
purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 9
-
pH profile of soluble and insoluble enzyme complexes, overview
4 - 4.5
-
initial rate
4.5 - 6.5
-
glycosylated and deglycosylated enzyme
5 - 6
-
10 min oxidation-assay of beta-D-glucose
5.1
-
assay at
5.2 - 7
-
immobilized on silk fibroin
5.2 - 6.2
-
recombinant enzyme
5.6 - 5.8
-
crystalline enzyme
5.7
-
soluble enzyme
5.8
-
immobilized and free form of the enzyme
5.9
-
soluble enzyme and immobilized enzyme in collagen
6.1
cellular organism
-
-
6.3
-
immobilized on activated carbon
6.5
-
native enzyme
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
additional information
-
80% activity at pH 3.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1 - 7.5
-
trend of the dependence of pH on peak current investigated in 0.1 M KCl solution, maximum amperometric response of hydrogen peroxide on the microelectrode dependent on pH over a range from 5.0 to 7.0
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 - 9
-
immobilized on activated carbon
3 - 8
-
pH profile, 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 - 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
3.4 - 7.5
-
soluble enzyme
3.5 - 6.5
-
-
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
4.9 - 8.9
-
70% of maximal activity at pH 4.9 and pH 8.9
5 - 7.5
-
under O2 and Ar at 37C, recombinant enzyme yGOXpenag
5.5 - 9
-
80% of the maximal activity is observed in the pH 5.5-9.0 range
6 - 9
-
over 80% of maximal activity within this range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
28 - 40
-
recombinant enzyme
30 - 50
-
in 100 mM potassium phosphate, pH 5.0
40 - 50
-
glycosylated and deglycosylated enzyme
50 - 80
-
temperature profile of soluble and insoluble enzyme complexes, overview
65
-
rate of oxidation of beta-D-glucose increases up to 65C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 45
-
70% of maximal activity at 10C and 45C
16 - 60
-
temperature profile, overview
25 - 50
-
the activity of the glycosylated and deglycosylated enzyme increases 2fold from 25C to 55C
30 - 55
temperature profile of recombinant enzyme, overview
30 - 60
temperature profile of native enzyme, overview
70
-
pH 5.1, 75% loss of of activity of natural GOD and pmr1DELTA-mutant-derived GOD, 65% loss of activity of hyperglycosylated GOD
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.2
-
isoelectric focusing
4.3
-
intracellular isozyme 1
4.7
-
extracellular isozyme 2
additional information
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
cellular organism
-
northeastern fall-flower
Manually annotated by BRENDA team
additional information