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
1.1.3.4
-
RECOMMENDED NAME
GeneOntology No.
glucose oxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2
show the reaction diagram
stereochemistry
-
beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2
show the reaction diagram
mechanism
-
beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
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).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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:O2-1-oxidoreductase
-
-
beta-D-glucose:O2-1-oxidoreductase
Penicillium adametzii LF F-2044.1
-
-
-
beta-D-glucose:oxygen 1-oxido-reductase
-
-
-
-
beta-D-glucose:oxygen 1-oxidoreductase
-
-
beta-D-glucose:oxygen 1-oxidoreductase
-
-
beta-D-glucose:oxygen oxidoreductase
-
-
beta-D-glucose:oxygen-1-oxidoreductase
-
-
beta-D-glucose:oxygen-1-oxidoreductase
-
-
beta-D-glucose:quinone oxidoreductase
-
-
-
-
corylophyline
-
-
-
-
D-glucose oxidase
-
-
-
-
D-glucose-1-oxidase
-
-
-
-
deoxin-1
-
-
-
-
glucose aerodehydrogenase
-
-
-
-
glucose oxyhydrase
-
-
-
-
glucose-1-oxidase
-
-
GO-2
Penicillium funiculosum
-
-
GO-2
Penicillium funiculosum 46.1
-
-
-
GOD
-
-
-
-
GOD
-
type X
GOD
Aspergillus niger NFCCP
-
-
-
GOX
-
type VII-S
GOX
-
type X-S
GOX
P13006
-
GOX
Penicillium sp. CBS 120262
-
-
-
GOX
Penicillium variabile
Q70FC9
-
GOX
Penicillium variabile P16
Q70FC9
-
-
GOX
D9ZFI1
-
microcid
-
-
-
-
notatin
-
-
-
-
oxidase, glucose
-
-
-
-
penatin
-
-
-
-
yGOXpenag
-
recombinant enzyme
CAS REGISTRY NUMBER
COMMENTARY
9001-37-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
ATCC 9029
-
-
Manually annotated by BRENDA team
G-13 mutant, culture conditions
-
-
Manually annotated by BRENDA team
strain NFCCP
-
-
Manually annotated by BRENDA team
strain NRRL-3
-
-
Manually annotated by BRENDA team
strain Z-25
SwissProt
Manually annotated by BRENDA team
type VII enzyme
-
-
Manually annotated by BRENDA team
type VII-S
-
-
Manually annotated by BRENDA team
wild-type strain denoted BTL
-
-
Manually annotated by BRENDA team
Aspergillus niger NFCCP
strain NFCCP
-
-
Manually annotated by BRENDA team
Aspergillus niger NRRL-3
strain NRRL-3
-
-
Manually annotated by BRENDA team
Aspergillus niger Z-25
strain Z-25
SwissProt
Manually annotated by BRENDA team
No.319
-
-
Manually annotated by BRENDA team
Aspergillus sp. No.319
No.319
-
-
Manually annotated by BRENDA team
cellular organism
northeastern fall-flower honey
-
-
Manually annotated by BRENDA team
larvae collected from the cotton fields in Zhengzhou, Henan Province of China, gene HaGox
UniProt
Manually annotated by BRENDA team
strain ATCC 42132
-
-
Manually annotated by BRENDA team
Mycoderma aceti
-
-
-
Manually annotated by BRENDA team
strain LF F-2044.1
-
-
Manually annotated by BRENDA team
Penicillium adametzii LF F-2044.1
-
-
-
Manually annotated by BRENDA team
Penicillium adametzii LF F-2044.1
strain LF F-2044.1
-
-
Manually annotated by BRENDA team
strain CBS 120262
-
-
Manually annotated by BRENDA team
Penicillium canescens CBS 120262
strain CBS 120262
-
-
Manually annotated by BRENDA team
apple blue mold, strain O-385-10
-
-
Manually annotated by BRENDA team
Penicillium funiculosum
strain 46.1
-
-
Manually annotated by BRENDA team
Penicillium funiculosum 46.1
strain 46.1
-
-
Manually annotated by BRENDA team
Penicillium pinophilum
-
-
-
Manually annotated by BRENDA team
8 species
-
-
Manually annotated by BRENDA team
strain CBS 120262, two isozymes
-
-
Manually annotated by BRENDA team
Penicillium sp. CBS 120262
strain CBS 120262, two isozymes
-
-
Manually annotated by BRENDA team
Penicillium variabile
-
-
-
Manually annotated by BRENDA team
Penicillium variabile
strain P16
SwissProt
Manually annotated by BRENDA team
Penicillium variabile P16
strain P16
SwissProt
Manually annotated by BRENDA team
commercial preparation
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
B2MW81, -
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 ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-1-phenyl-1,2-ethanediol + O2
?
show the reaction diagram
-
-
-
-
?
(R)-1-phenyl-1,2-ethanediol + O2
(2R)-hydroxy(phenyl)ethanoic acid + H2O2
show the reaction diagram
-
-
product identification by NMR
-
?
(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
Penicillium variabile
Q70FC9
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
-
-
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
38% relative activity to D-glucose
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
recombinant enzyme
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
20% relative activity to D-glucose
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
30% relative activity to beta-D-glucose
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
show the reaction diagram
Penicillium variabile
-
19.6% relative activity to D-glucose
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
25% relative activity to beta-D-glucose
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
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
show the reaction diagram
Penicillium funiculosum
-
36% of the activity with beta-D-glucose
-
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
low GOD activity
-
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
show the reaction diagram
Penicillium funiculosum 46.1
-
36% of the activity with beta-D-glucose
-
-
?
3,6-methyl-D-glucose + O2 + H2O
3,6-methyl-D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
1.85% relative activity to beta-D-glucose
-
?
3-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
-
0.64% relative activity to beta-D-glucose
-
?
alpha-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
very slow reaction
-
?
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 + 2,6-dichlorophenol indophenol
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
Penicillium pinophilum
-
-
-
-
-
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
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
P13006
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
B2MW81, -
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
via cofactor FAD reduction to FADH2, reaction cycles, FADH2 reduces O2, overview
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
P13006
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Penicillium sp. CBS 120262
-
-, via cofactor FAD reduction to FADH2, reaction cycles, FADH2 reduces O2, overview
-
-
?
beta-D-glucose + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
P13006
-
-
-
?
beta-D-glucose + O2 + H2O
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
-
-
-
-
ir
beta-D-glucose + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
Penicillium funiculosum
-
-
-
-
?
beta-D-glucose + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
cellular organism
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
Mycoderma aceti
-
-
-
?
beta-D-glucose + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
D9ZFI1
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
highly specific
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
highly specific
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
Penicillium variabile
-
highly specific
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
soluble enzyme and immobilized enzyme on collagen
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
kinetic mechanism
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
glucose is the primary substrate, recombinant enzyme
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
Penicillium pinophilum
-
specific for D-glucose, 2,6-dichloroindophenol can act as artificial electron acceptor
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
glucose is the primary substrate for the enzyme
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
glucose is the primary substrate for the enzyme
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
glucose is the primary substrate for the enzyme
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
glucose is the primary substrate for the enzyme
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
glucose is the primary substrate for the enzyme
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
glucose is the primary substrate for the enzyme
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
Penicillium variabile
-
glucose is the primary substrate for the enzyme
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
native enzyme and enzyme immobilized on mycelium pellets
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
native enzyme and enzyme immobilized on activated carbon
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
GOD is highly specific for the beta-anomer of D-glucose
-
-
ir
beta-D-glucose + O2 + H2O
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
Penicillium adametzii LF F-2044.1
-
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
Penicillium canescens CBS 120262
-
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
Aspergillus sp. No.319
-
-, native enzyme and enzyme immobilized on mycelium pellets
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
Aspergillus niger NRRL-3
-
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
Penicillium funiculosum 46.1
-
-
-
-
?
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
Penicillium variabile
Q70FC9
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
Penicillium variabile
-
4.9% relative activity to D-glucose
-
?
D-galactose + O2 + H2O
? + H2O2
show the reaction diagram
-
recombinant enzyme
-
?
D-galactose + O2 + H2O
?
show the reaction diagram
-
low GOD activity
-
-
?
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 + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
Penicillium variabile
Q70FC9
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
Penicillium variabile
Q70FC9
best substrate
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
the enzyme is involved in apple fruit tissue browning
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
highly substrate specific enzyme
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
Penicillium adametzii LF F-2044.1
-
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
Penicillium variabile P16
Q70FC9
-, best substrate
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
Aspergillus niger NFCCP
-
-, highly substrate specific enzyme
-
-
?
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
-
4.5% of D-glucose reactivity
-
?
D-maltose + O2 + H2O
?
show the reaction diagram
-
4.5% of D-glucose reactivity
-
?
D-maltose + O2 + H2O
? + H2O2
show the reaction diagram
Penicillium variabile
-
21.3% relative activity to D-glucose
-
?
D-maltose + O2 + H2O
? + H2O2
show the reaction diagram
Penicillium funiculosum, Penicillium funiculosum 46.1
-
22% of the activity with beta-D-glucose
-
-
?
D-mannitol + O2
?
show the reaction diagram
-
-
-
-
?
D-mannose + O2
?
show the reaction diagram
Penicillium variabile, Penicillium variabile P16
Q70FC9
7.2% of the activity with D-glucose for the native enzyme, 13.4 for the recombinant enzyme
-
-
?
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
Penicillium variabile, Penicillium variabile P16
Q70FC9
3.0% of the activity with D-glucose for the native enzyme, 5.8 for the recombinant enzyme
-
-
?
D-xylose + O2 + H2O
?
show the reaction diagram
Penicillium variabile
-
3% relative activity to D-glucose
-
?
D-xylose + O2 + H2O
?
show the reaction diagram
-
recombinant enzyme
-
?
D-xylose + O2 + H2O
?
show the reaction diagram
-
4.8% of D-glucose reactivity
-
?
D-xylose + O2 + H2O
?
show the reaction diagram
-
4.8% of D-glucose reactivity
-
?
D-xylose + O2 + H2O
? + H2O2
show the reaction diagram
Penicillium funiculosum, Penicillium funiculosum 46.1
-
11% of the activity with beta-D-glucose
-
-
?
galactose + O2 + H2O
D-galactono-1,5-lactone + H2O2
show the reaction diagram
Penicillium funiculosum
-
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
-
86% relative activity to D-glucose
-
-
?
L-sorbose + O2 + H2O
?
show the reaction diagram
-
5.8% of D-glucose reactivity
-
?
L-sorbose + O2 + H2O
?
show the reaction diagram
-
5.8% of D-glucose reactivity
-
?
L-threitol + O2
?
show the reaction diagram
-
-
-
-
?
maltose + O2
?
show the reaction diagram
Penicillium variabile
Q70FC9
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
-
1% relative activity to D-glucose
-
?
mannose + O2 + H2O
? + H2O2
show the reaction diagram
-
recombinant enzyme
-
?
mannose + O2 + H2O
? + H2O2
show the reaction diagram
Penicillium variabile
-
7.2% relative activity to D-glucose
-
?
sorbitol + O2
?
show the reaction diagram
-
-
-
-
?
xylitol + O2
?
show the reaction diagram
-
-
-
-
?
xylitol + O2
?
show the reaction diagram
-
best substrate
-
-
?
mannose + O2 + H2O
? + H2O2
show the reaction diagram
-
9% relative activity to D-glucose
-
?
additional information
?
-
-
important role in lignin-degradation
-
-
-
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
?
-
Penicillium funiculosum
-
less than 2.5% of the activity with beta-D-glucose with arabinose, lactose, mannitol, sucrose and fructose
-
-
-
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
?
-
Penicillium variabile
Q70FC9
no activity with L-arabinose and D-galactose with the native and recombinant enzyme
-
-
-
additional information
?
-
-
the enzyme binds to concanavalin A forming insoluble complexes, overview
-
-
-
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
?
-
-
AldO catalyzes the C1 oxidation of several polyols
-
-
-
additional information
?
-
-
alpha-D-glucose is not a suitable substrate
-
-
-
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
?
-
-
Rab8, Cdc42, Rho1, and Rho4 are associated with enriched vesicles carrying GOX activity
-
-
-
additional information
?
-
Penicillium variabile P16
Q70FC9
no activity with L-arabinose and D-galactose with the native and recombinant enzyme
-
-
-
additional information
?
-
Penicillium funiculosum 46.1
-
less than 2.5% of the activity with beta-D-glucose with arabinose, lactose, mannitol, sucrose and fructose
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
P13006
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
B2MW81, -
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
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
show the reaction diagram
Penicillium sp. CBS 120262
-
-
-
-
?
beta-D-glucose + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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 + O2 + H2O
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
cellular organism
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
Mycoderma aceti
-
-
-
?
beta-D-glucose + O2 + H2O
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
D9ZFI1
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
show the reaction diagram
Aspergillus sp. No.319
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
Penicillium variabile
Q70FC9
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
-
the enzyme is involved in apple fruit tissue browning
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
Penicillium adametzii LF F-2044.1
-
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
Penicillium variabile P16
Q70FC9
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
Aspergillus niger NFCCP
-
-
-
-
?
D-mannitol + O2
?
show the reaction diagram
-
-
-
-
?
sorbitol + O2
?
show the reaction diagram
-
-
-
-
?
xylitol + O2
?
show the reaction diagram
-
-
-
-
?
D-sorbitol + O2
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
important role in lignin-degradation
-
-
-
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 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
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
FAD
-
2 mol per mol of enzyme
FAD
-
1.5 mol of flavin per mol of protein
FAD
-
defined as flavoprotein oxidase, two very tightly bound FAD molecules per dimer, kinetic behavior
FAD
-
2 mol per mol of enzyme
FAD
-
2 mol per mol of enzyme
FAD
-
electron transfer between FAD centers and metal electrodes after chemical modification of enzyme
FAD
cellular organism
-
not detectable in honey enzyme
FAD
-
4 mol flavin per mol of enzyme
FAD
Penicillium pinophilum
-
1.76 nmol FAD per nmol enzyme
FAD
-
dissociation of FAD from the holoenzyme is responsible for the thermal inaction of the enzyme
FAD
Penicillium variabile
Q70FC9
bound
FAD
-
flavoenzyme
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
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
-
FAD-binding site studies, active site geometry
-
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
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Cu2+
-
active site bound, required
Na+
cellular organism
-
required for maximal activity, honey enzyme
Iron
-
the enzyme contains 2 mol of iron per 160000 Da
additional information
-
no activition by Ca2+ and Ba2+ at 1 mM
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
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-deoxy-D-glucose
-
-
4-chloromercuribenzoate
-
-
8-hydroxyquinoline
-
11% inhibition at 10 mM
8-hydroxyquinoline
-
-
adenine nucleotides
-
inhibition of FAD-binding to apoprotein
Ag+
-
75% inhibition at 10 mM
Ag+
-
inhibits oxidation of the reduced FAD moiety competing with molecular oxygen as a hydrogen acceptor
Ag+
Penicillium variabile
-
inhibition is explained by the high reactivity of this ion for thiol groups essential for enzymic activity
AgNO3
Penicillium variabile
-
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
Ba2+
-
70% residual activity at 1 mM
Cd2+
-
60% residual activity at 1 mM
CN-
cellular organism
-
honey enzyme only
Cu2+
-
30% residual activity at 1 mM
CuCl2
Penicillium variabile
-
6.5% activity remains at 10 mM
CuSO4
-
66% inhibition at 1 mM
D-glucono-delta-lactone
-
weak competitive inhibitor of GOD
dimedone
-
not inhibitory
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
Hg2+
-
35% residual activity at 1 mM
HgCl2
-
complete inhibition at 1 mM
hydroxylamine
-
partial
hydroxylamine
-
not inhibitory
hydroxylamine
-
-
K+
-
97% residual activity at 1 mM
Mg2+
-
85% residual activity at 1 mM
Na+
-
95% residual activity at 1 mM
Na+
-
the inhibiting effect of Na+ions is reduced at Na+concentrations over 0.5 M
NaCl
-
50% inhibition at a concentration of 4%
NaF
Penicillium variabile
-
72% activity remains at 10 mM
NaHSO4
-
40% inhibition at 1 mM
NaNO3
-
non-competitive inhibition in microemulsion and in aqueous medium
NaNO3
-
a competitive inhibitor of glucose oxidase
o-phthalate
-
88% inhibition at 50 mM
p-chloromercuribenzoate
-
-
Pb2+
-
45% residual activity at 1 mM
phenylhydrazine
-
partial
phenylhydrazine
-
30% inhibition at 1 mM
phenylhydrazine
-
-
phenylmercuric acetate
-
-
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
-
20% inhibition at 10 mM
Semicarbazide
cellular organism
-
-
sodium bisulfate
-
-
Sodium bisulfite
-
partial
Sodium cholate
-
non-competitive inhibition in microemulsion
Sodium nitrate
-
13% inhibition at 10 mM
Mg2+
-
total inhibition of the enzyme at a Mg2+ concentration of 1.9 M
additional information
-
glycoprotein from Dioscorea batatas protects mouse thymocytes from glucose/glucose oxidase-induced cell death
-
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
-
ammonium sulfate does not inhibit glucose oxidase
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
beta-D-glucose
B2MW81, -
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
KCN
-
stimulation of activity, 135% 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
KCN
-
substancial stimulation
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]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
Penicillium pinophilum
-
-
35
-
2-amino-1-pentanol
-
pH 7.5, 30C
8.3
-
2-deoxy-D-glucose
-
recombinant enzyme
20
-
2-deoxy-D-glucose
Penicillium variabile
-
-
28.1
49.8
2-deoxy-D-glucose
Penicillium funiculosum
-
pH 5.0, 25C
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
-
beta-D-glucose
-
native enzyme in solution, pH 5.5, temperature not specified in the publication
1.34
-
beta-D-glucose
-
-
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
-
0.05 M Tris buffer, pH 8
1.9
-
beta-D-glucose
-
purified enzyme under argon, in 20 mM phosphate buffer pH 7.4 at 37C
2
14
beta-D-glucose
-
pH 3.45, 35C
2
-
beta-D-glucose
-
0.1 M Tris buffer, pH 8
2.1
-
beta-D-glucose
-
second polyethyleneimine/GOD bilayer
2.5
-
beta-D-glucose
-
non-purified enzyme under argon, in 20 mM phosphate buffer pH 7.4 at 37C
2.9
-
beta-D-glucose
-
first polyethyleneimine/GOD bilayer
4
5.4
beta-D-glucose
-
immobilized enzyme
4
-
beta-D-glucose
-
immobilized enzyme, immobilized membrane with ratio stretching 1.25
4.4
-
beta-D-glucose
-
0.6 M sodium acetate buffer, pH 6
4.5
-
beta-D-glucose
-
immobilized enzyme, methanol treated
5
-
beta-D-glucose
-
0.1 M sodium acetate buffer, pH 5
5.2
-
beta-D-glucose
-
0.1 M sodium acetate buffer, pH 6
5.4
-
beta-D-glucose
-
immobilized enzyme, immobilized membrane with ratio stretching 3
5.7
-
beta-D-glucose
-
native enzyme
6
-
beta-D-glucose
Penicillium variabile
-
-
6.2
-
beta-D-glucose
Penicillium pinophilum
-
-
6.2
-
beta-D-glucose
-
recombinant enzyme
6.3
-
beta-D-glucose
-
deglycosylated enzyme
6.3
-
beta-D-glucose
-
wild-type enzyme conjugated to gold nanoparticles, pH and temperature not specified in the publication
6.4
-
beta-D-glucose
-
0.1 M sodium phosphate buffer, pH 7
6.7
-
beta-D-glucose
-
0.1 M potassium phosphate buffer, pH 7
7.1
-
beta-D-glucose
-
0.1 M sodium acetate buffer, pH 4.5
7.9
-
beta-D-glucose
-
randomly mixed polyethyleneimine/GOD
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
8.1
-
beta-D-glucose
-
0.1 M potassium phosphate buffer, pH 6
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 45C
11
-
beta-D-glucose
-
-
11
-
beta-D-glucose
-
-
11.7
-
beta-D-glucose
-
recombinant enzyme yGOXpenag, using O2 as cosubstrate, pH 6.0, 50C
11.9
-
beta-D-glucose
-
purified enzyme under O2, in 20 mM phosphate buffer pH 7.4 at 37C
12
-
beta-D-glucose
-
enzyme adsorbed on 11-amino-1-undecanethiol coated matrix, pH 5.5, temperature not specified in the publication
12.42
-
beta-D-glucose
-
in the presence of 0.6 M trehalose, at 25C
14.7
15.3
beta-D-glucose
Penicillium funiculosum
-
pH 5.0, 25C
15
-
beta-D-glucose
-
mutant H447C, pH and temperature not specified in the publication
16.5
-
beta-D-glucose
-
0.1 M sodium acetate buffer, pH 4
16.95
-
beta-D-glucose
P13006
recombinant enzyme, in 0.1 M sodium phosphate buffer, pH 6.0, at 35C
18.2
-
beta-D-glucose
-
recombinant enzyme yGOXpenag, using ferrocinium-methanol as cosubstrate, pH 6.0, 50C
18.4
-
beta-D-glucose
-
pH 7.0, 25C
18.76
-
beta-D-glucose
-
in the absence of trehalose, at 25C
22
-
beta-D-glucose
-
soluble enzyme
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
22.5
-
beta-D-glucose
-
0.6 M sodium acetate buffer, pH 4.5
23.7
-
beta-D-glucose
-
BTL wild-type strain enzyme
25.2
-
beta-D-glucose
-
free enzyme
26
30
beta-D-glucose
-
enzymes obtained from different companies
28
-
beta-D-glucose
-
periodate-oxidized enzyme
30
-
beta-D-glucose
-
native enzyme
31.8
-
beta-D-glucose
-
commercially available enzyme
33
-
beta-D-glucose
-
soluble enzyme
33
-
beta-D-glucose
-
-
34.9
-
beta-D-glucose
-
at pH 8.2, 40C
35
-
beta-D-glucose
-
deglycosylated enzyme
37
38
beta-D-glucose
-
-
37
-
beta-D-glucose
-
native enzyme
38
-
beta-D-glucose
-
carbohydrate-depleted enzyme
38.1
-
beta-D-glucose
-
at pH 8.2, 50C
44
-
beta-D-glucose
-
immobilized enzyme
44.9
-
beta-D-glucose
-
at pH 8.2, 60C
50
-
beta-D-glucose
-
pH 6.01, 35C
50.3
-
beta-D-glucose
-
native enzyme, using O2 as cosubstrate, pH 6.5, 70C
55.2
-
beta-D-glucose
-
at pH 8.2, 70C
67
-
beta-D-glucose
-
pH 4.82, 35C
71.2
-
beta-D-glucose
-
native enzyme, using ferrocinium-methanol as cosubstrate, pH 6.5, 70C
72
-
beta-D-glucose
-
immobilized enzyme
87
-
beta-D-glucose
-
pH 4.52, 35C
96.4
-
beta-D-glucose
-
wild-type enzyme, pH and temperature not specified in the publication
106
-
beta-D-glucose
-
pH 4.27, 35C
130
-
beta-D-glucose
-
pH 3.88, 35C
537
-
beta-D-glucose
-
pH 2.84, 35C
162
-
D-fructose
Penicillium variabile
-
-
76.9
126.3
D-galactose
Penicillium funiculosum
-
pH 5.0, 25C
952
-
D-galactose
-
recombinant enzyme
13.5
-
D-glucose
Penicillium variabile
Q70FC9
pH 5.0, 28C, native enzyme
15.25
-
D-glucose
Penicillium variabile
Q70FC9
pH 5.0, 28C, recombinant enzyme
15.6
-
D-glucose
-
pH 5.0, 25C, enzyme fraction 1
21.9
-
D-glucose
-
pH 5.0, 25C, enzyme fraction 2
25
-
D-glucose
-
pH 5.5, 40C
26
-
D-glucose
-
native enzyme
57.3
-
D-maltose
Penicillium funiculosum
-
pH 5.0, 25C
117
-
D-maltose
Penicillium variabile
-
-
36
-
D-Mannitol
-
pH 7.5, 30C
44
-
D-mannose
Penicillium variabile
-
-
106
-
D-mannose
-
recombinant enzyme
1.4
-
D-Sorbitol
-
pH 7.5, 30C
33
-
D-xylose
Penicillium variabile
-
-
42.9
70.7
D-xylose
Penicillium funiculosum
-
pH 5.0, 25C
384
-
D-xylose
-
recombinant enzyme
0.19
-
di-(2,2'-bipyridinyl)ruthenium(III)dichloride
-
pH 7.3, 30C
0.0638
-
ferrocinium-methanol
-
recombinant enzyme yGOXpenag, pH 6.0, 50C
-
0.1107
-
ferrocinium-methanol
-
native enzyme, pH 6.5, 70C
-
350
-
glycerol
-
pH 7.5, 30C
430
-
L-arabinose
-
pH 7.5, 30C
25
-
L-Threitol
-
pH 7.5, 30C
2.9
-
methyl-1,4-benzoquinone
-
low pH, 35C
3.25
-
methyl-1,4-benzoquinone
-
pH 2.84, 35C
3.97
-
methyl-1,4-benzoquinone
-
pH 3.45, 35C
4.98
-
methyl-1,4-benzoquinone
-
pH 3.88, 35C
5.7
-
methyl-1,4-benzoquinone
-
pH 4.27, 35C
6.22
-
methyl-1,4-benzoquinone
-
pH 4.52, 35C
6.63
-
methyl-1,4-benzoquinone
-
pH 4.82, 35C
6.94
-
methyl-1,4-benzoquinone
-
pH 6.01, 35C
0.18
-
O2
-
periodate-oxidized enzyme
0.2
-
O2
-
native enzyme
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
7
-
methyl-1,4-benzoquinone
-
pH 7, 35C
additional information
-
additional information
-
values for glyco-enzyme and aglyco-enzyme
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
KM-value of immunoaffinity-layered glucose oxidase preparations remains unaltered
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
kinetics of enzyme-pentacyanoferrate(III)-nucleophilic ligands-complex interactions, detailed overview
-
additional information
-
additional information
-
thermodynamics
-
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
-
Michaelis-Menten kinetics, overview
-
additional information
-
additional information
-
steady-state kinetics, overview
-
additional information
-
additional information
-
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.74
-
(R)-1-phenyl-1,2-ethanediol
-
pH 7.5, 30C
0.008
-
(S)-1-phenyl-1,2-ethanediol
-
pH 7.5, 30C
4.4
-
1,2,4-butanetriol
-
pH 7.5, 30C
0.29
-
1,2-Butanediol
-
pH 7.5, 30C
2
-
1,2-hexanediol
-
pH 7.5, 30C
0.85
-
1,2-pentanediol
-
pH 7.5, 30C
0.36
-
1-phenyl-1,2-ethanediol
-
pH 7.5, 30C
1.13
-
2,6-dichloroindophenol
-
-
0.017
-
2-amino-1-pentanol
-
pH 7.5, 30C
0.34
-
3-butene-1,2-diol
-
pH 7.5, 30C
0.1
-
3-butenol
-
pH 7.5, 30C
15.5
-
4-benzoquinone
-
-
0.35
-
4-pentene-1,2-diol
-
pH 7.5, 30C
0.168
-
beta-D-glucose
-
pH 7, 30C, 2-ethylhexylsulfosuccinate medium or polyethylene glycol p-tert octyl phenyl ether medium
0.3
-
beta-D-glucose
-
pH 7, 30C, aqeous medium
5.2
-
beta-D-glucose
-
pH 9.0, 33C, deglycosylated recombinant enzyme with PEG-5000 reagent
5.5
-
beta-D-glucose
-
pH 9.0, 33C, deglycosylated recombinant enzyme with PEG-350 reagent
5.9
-
beta-D-glucose
-
pH 9.0, 33C, recombinant enzyme expressed in yeast
6.1
-
beta-D-glucose
-
pH 9.0, 33C, wild-type enzyme
6.3
-
beta-D-glucose
-
pH 9.0, 33C, deglycosylated recombinant enzyme
22.8
-
beta-D-glucose
-
wild-type enzyme conjugated to gold nanoparticles, pH and temperature not specified in the publication
55.3
-
beta-D-glucose
-
mutant H447C conjugated to gold nanoparticles, pH and temperature not specified in the publication
152
-
beta-D-glucose
-
wild-type enzyme, pH and temperature not specified in the publication
323
-
beta-D-glucose
-
periodate-oxidized enzyme
337
-
beta-D-glucose
-
native enzyme
425
-
beta-D-glucose
-
mutant H447C, pH and temperature not specified in the publication
484.3
-
beta-D-glucose
P13006
recombinant enzyme, in 0.1 M sodium phosphate buffer, pH 6.0, at 35C
741
-
beta-D-glucose
-
pH 7.0, 25C
1695
-
beta-D-glucose
-
recombinant enzyme yGOXpenag, using ferrocinium-methanol as cosubstrate, pH 6.0, 50C
1808
-
beta-D-glucose
-
recombinant enzyme yGOXpenag, using O2 as cosubstrate, pH 6.0, 50C
1890
-
beta-D-glucose
-
native enzyme, using O2 as cosubstrate, pH 6.5, 70C
1938
-
beta-D-glucose
-
native enzyme, using ferrocinium-methanol as cosubstrate, pH 6.5, 70C
1950
-
beta-D-glucose
-
deglycosylated enzyme
2000
-
beta-D-glucose
-
native enzyme; recombinant enzyme
0.59
-
D-glucose
-
pH 5.0, 25C, enzyme fraction 1
235.1
-
D-glucose
-
pH 5.0, 25C, enzyme fraction 1
318.2
-
D-glucose
-
pH 5.0, 25C, enzyme fraction 2
9.2
-
D-Mannitol
-
pH 7.5, 30C
17
-
D-Sorbitol
-
pH 7.5, 30C
35.4
-
di-(2,2'-bipyridinyl)ruthenium(III)dichloride
-
pH 7.3, 30C
1.6
-
glycerol
-
pH 7.5, 30C
1.7
-
L-arabinose
-
pH 7.5, 30C
0.33
-
N,N,N',N'-tetramethyl-1,4-phenylenediamine
-
-
13
-
xylitol
-
pH 7.5, 30C
10.5
-
[(1,10-phenanthroline)2(Cl)2Ru(III)]
-
-
50.3
-
[(1,8-dimethyl-4,5-phenanthroline)3Ru(II)]PF6-
-
pH 7.3, 30C
10.5
-
[(2,2'-(4,4'dimethyl)bipyridine)2(Cl)2Ru(III)]
-
pH 7.3, 30C
13.8
-
[(2,2'-(4,4'dimethyl)bipyridine)2(Cl)2Ru(III)]PF6-
-
pH 7.3, 30C
38.6
-
[(2,2'-bipyridine)2(CO32-)1/2Ru(III)]
-
pH 7.3, 30C
8.3
-
[(2,2'-bipyridine)2(H2O)2Ru(III)]PF6-
-
pH 7.3, 30C
31.4
-
[(2,2'-bipyridine)2(SCN-)2Ru(III)]
-
pH 7.3, 30C
158
-
[(2,2'-bipyridine)3Ru(II)]PF6-
-
pH 7.3, 30C
6.3
-
L-Threitol
-
pH 7.5, 30C
additional information
-
additional information
-
pH-dependence
-
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
Penicillium variabile
Q70FC9
native enzyme and recombinant enzyme at pH 5.0, 28C
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
27
-
beta-D-glucose
-
native enzyme, using ferrocinium-methanol as cosubstrate, pH 6.5, 70C
7894
38
-
beta-D-glucose
-
native enzyme, using O2 as cosubstrate, pH 6.5, 70C
7894
93
-
beta-D-glucose
-
recombinant enzyme yGOXpenag, using ferrocinium-methanol as cosubstrate, pH 6.0, 50C
7894
155
-
beta-D-glucose
-
recombinant enzyme yGOXpenag, using O2 as cosubstrate, pH 6.0, 50C
7894
0.017
-
ferrocinium-methanol
-
native enzyme, pH 6.5, 70C
0
0.027
-
ferrocinium-methanol
-
recombinant enzyme yGOXpenag, pH 6.0, 50C
0
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
39.8
-
ammonium chloride
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.33
-
Penicillium variabile
Q70FC9
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
-
Penicillium variabile
Q70FC9
purified recombinant enzyme
153.5
-
P13006
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
914
956
Penicillium funiculosum
-
-
additional information
-
-
continous flow determination
additional information
-
-
-
additional information
-
-
activity of different mutants
additional information
-
-
-
additional information
-
-
assay method
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
effect of culture conditions on enzyme activity
additional information
-
cellular organism
-
-
additional information
-
Penicillium variabile
-
-
additional information
-
-
-
additional information
-
Penicillium pinophilum
-
-
additional information
-
-
-
additional information
-
-
1.08 U/mg dry weight for the intracellular enzyme, and 6.9U/ml for the extracellular enzyme
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
-
-
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
-
-
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
-
-
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
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
9
-
pH profile of soluble and insoluble enzyme complexes, overview
4
4.5
Penicillium funiculosum
-
initial rate
4
6
Penicillium pinophilum
-
-
4.5
6.5
-
glycosylated and deglycosylated enzyme
5
6
-
native and deglycosylated enzyme
5
6
Penicillium funiculosum
-
10 min oxidation-assay of beta-D-glucose
5
-
-
enzyme immobilized onto alumina
5
-
-
enzyme immobilized on mycelium pellets
5
-
-
assay at
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
5
-
-
assay at
5.1
-
-
assay at
5.2
6.2
-
recombinant enzyme
5.2
7
-
immobilized on silk fibroin
5.5
-
-
immobilized on polyacrylamide
5.5
-
-
-
5.5
-
-
free enzyme
5.5
-
-
glyco-GOD
5.5
-
-
assay at
5.6
5.8
-
crystalline enzyme
5.6
-
-
pH-dependence of individual reaction steps
5.6
-
-
assay at
5.7
-
-
soluble enzyme
5.8
-
-
immobilized and free form of the enzyme
5.9
-
-
soluble enzyme and immobilized enzyme in collagen
6
-
-
native enzyme
6
-
Penicillium variabile
-
-
6
-
-
natural GOD, pmr1DELTA-mutant-derived GOD,hyperglycosylated GOD expressed in wild-type cells of Saccharomyces cerevisiae
6
-
-
assay at
6
-
Penicillium variabile
Q70FC9
native and recombinant enzyme
6
-
P13006
-
6
-
-
under O2 and Ar at 37C, recombinant enzyme yGOXpenag
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
-
-
optimum of limonene transformation
7.2
-
-
enzyme-pentacyanoferrate(III)-nucleophilic ligands-complex interaction assay
7.5
-
-
assay at
additional information
-
-
80% activity at pH 3.0
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
9
-
immobilized on activated carbon
3
8
-
pH profile, overview
3
8
Penicillium variabile
Q70FC9
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
Penicillium funiculosum
-
pH 3.0: about 45% of maximal activity, pH 9.0: about 40% of maximal activity, 10 min oxidation-assay of beta-D-glucose
3.4
7.5
-
soluble enzyme
4
7
-
more than 90% of activity maximum at pH 4.0 and 7.0
4
8
P13006
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
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
assay at room temperature
25
-
-
assay at
25
-
-
enzyme-pentacyanoferrate(III)-nucleophilic ligands-complex interaction assay
25
-
-
assay at
25
-
-
measurements at
25
-
-
assay at
28
40
-
recombinant enzyme
30
50
Penicillium pinophilum
-
in 100 mM potassium phosphate, pH 5.0
30
-
-
immobilized and free form of the enzyme
35
-
-
assay at
40
50
-
glycosylated and deglycosylated enzyme
40
-
-
immobilized on polyacrylamide
40
-
-
soluble enzyme and immobilized enzyme in collagen
40
-
cellular organism
-
-
40
-
P13006
-
45
-
Penicillium variabile
Q70FC9
recombinant enzyme
50
80
-
temperature profile of soluble and insoluble enzyme complexes, overview
50
-
-
recombinant enzyme
55
-
Penicillium variabile
-
-
55
-
Penicillium variabile
Q70FC9
native enzyme
65
-
Penicillium funiculosum
-
rate of oxidation of beta-D-glucose increases up to 65C
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10
45
-
70% of maximal activity at 10C and 45C
16
60
-
temperature profile, overview
30
55
Penicillium variabile
Q70FC9
temperature profile of recombinant enzyme, overview
30
60
Penicillium variabile
Q70FC9
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
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.2
-
-
isoelectric focusing
4.3
-
-
intracellular isozyme 1
4.7
-
-
extracellular isozyme 2
additional information
-
-
-
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Aspergillus niger NRRL-3, Penicillium canescens CBS 120262
-
-
-
Manually annotated by BRENDA team
cellular organism
-
northeastern fall-flower
Manually annotated by BRENDA team
Aspergillus niger NFCCP
-
-
-
Manually annotated by BRENDA team
additional information
-
poor growth of the organism in medium containing glucose as sole carbon source, in this culture gluconate accumulates
Manually annotated by BRENDA team
additional information
B2MW81, -
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
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Aspergillus niger NRRL-3
-
12% of glucose oxidase activity in the stationary phase and 16% of glucose oxidase activity in the mid-exponential phase is localised in the cytoplasm
-
Manually annotated by BRENDA team
Penicillium canescens CBS 120262
-
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
-
Manually annotated by BRENDA team
Penicillium funiculosum
-
-
-
Manually annotated by BRENDA team
-
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
-
Manually annotated by BRENDA team
-
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
-
Manually annotated by BRENDA team
Aspergillus niger NRRL-3
-
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
-
-
Manually annotated by BRENDA team
Penicillium adametzii LF F-2044.1
-
-
-
-
Manually annotated by BRENDA team
Penicillium canescens CBS 120262
-
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
-
-
Manually annotated by BRENDA team
Penicillium funiculosum 46.1
-
-
-
-
Manually annotated by BRENDA team
Penicillium sp. CBS 120262
-
isozyme 2
-
-
Manually annotated by BRENDA team
Penicillium sp. CBS 120262
-
isozyme 1
-
Manually annotated by BRENDA team
-
34% of glucose oxidase activity in the stationary phase and 26% of glucose oxidase activity in the mid-exponential phase is localised in the membrane
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Aspergillus niger NRRL-3
-
34% of glucose oxidase activity in the stationary phase and 26% of glucose oxidase activity in the mid-exponential phase is localised in the membrane
-
Manually annotated by BRENDA team
Penicillium canescens CBS 120262
-
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
-
Manually annotated by BRENDA team
additional information
-
peroxisome-like structure
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
70000
-
D9ZFI1
SDS-PAGE
94000
-
P13006
SDS-PAGE
120000
-
-
recombinant enzyme, native PAGE
126000
-
Penicillium variabile
-
gel filtration
130000
150000
-
aglyco-GOD, gel filtration, native PAGE
140000
-
-
native enzyme, gel filtration
148000
-
Penicillium pinophilum
-
gel filtration on Superdex 200
148000
-
-
gel filtration
150000
153000
-
periodate-oxidized enzyme; sedimentation and diffusion data
150000
153000
-
sedimentation and diffusion data
152000
-
-
SDS-PAGE
152800
-
Penicillium pinophilum
-
electron microscopy
154000
-
-
crystalline enzyme
158000
160000
-
gel filtration
158000
160000
-
sedimentation equilibrium centrifugation
159000
-
Penicillium pinophilum
-
calculated value based on Stokes' radius and sedimentation coefficient
160000
-
-
gel filtration
160000
-
-
sedimentation equilibrium studies
160000
-
Penicillium pinophilum
-
gel filtration on Sephacryl S-300
160000
-
-
gel filtration
160000
-
-
-
167000
-
-
glycosylated enzyme, PAGE under non-dissociating conditions
175000
180000
-
gel filtration
175000
180000
-
gel filtration
175000
-
Penicillium variabile
Q70FC9
gel filtration
176000
-
-
glycosylated enzyme, gel filtration
180000
-
-
gel filtration, overestimation may be due to hydrodynamic properties of the enzyme
186000
-
-
-
290000
-
-
gel filtration
669000
-
-
PEGylated enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 87100, SDS-PAGE
?
-
x * 75000, SDS-PAGE
?
-
x * 136000 deglycosylated recombinant enzyme, SDS-PAGE; x * 146000, deglycosylated recombinant enzyme with PEG-350 reagent, SDS-PAGE; x * 155000, wild-type enzyme, SDS-PAGE; x * 211000, deglycosylated recombinant enzyme with PEG-5000 reagent, SDS-PAGE; x * 320000, recombinant enzyme expressed in yeast, SDS-PAGE
?
B2MW81, -
x * 67000, SDS-PAGE
?
-
x * 182200, PEGylated enzyme, SDS-PAGE
dimer
-
2 * 80000, identical, SDS-PAGE
dimer
-
2 * 72000, SDS-PAGE
dimer
-
2 * 79000, SDS-PAGE
dimer
-
each unit in the dimer is composed of two polypeptide chains connected by a disulfide bond
dimer
-
2 * 60000, aglyco-GOD, SDS-PAGE; 2 * 70000, glyco-GOD, SDS-PAGE
dimer
Penicillium variabile
-
2 * 62000, SDS-PAGE
dimer
Penicillium pinophilum
-
2 * 77700, SDS-PAGE, confirmed by electron-microscopic examinations
dimer
-
2 * 60000, SDS-PAGE, recombinant enzyme
dimer
-
for both native and deglycosylated GOD at pH 6 and 10 only the dimeric configuration is observed
dimer
Penicillium variabile
Q70FC9
2 * 82000, recombinant enzyme, SDS-PAGE
dimer
-
homodimer
dimer
-
2 * 70000, SDS-PAGE
dimer
-
2 * 86400, native enzyme, SDS-PAGE
dimer
Penicillium sp. CBS 120262
-
2 * 70000, SDS-PAGE
-
dimer
Penicillium variabile P16
-
2 * 82000, recombinant enzyme, SDS-PAGE
-
homodimer
-
2 * 80000
homodimer
-
2 * 77000, native enzyme, SDS-PAGE
homodimer
-
2 * 72000, recombinant enzyme, SDS-PAGE
oligomer
-
dimer or trimer, secondary structure
oligomer
Penicillium adametzii LF F-2044.1
-
dimer or trimer, secondary structure
-
tetramer
-
4 * 45000, 2 polypeptide chains linked by disulfide bond, sedimentation equilibrium centrifugation, treatment with guanidine-HCl and 2-mercaptoethanol
tetramer
-
4 * 70000, SDS-PAGE
monomer
-
1 * 45100
additional information
-
AldO shares the same folding topology of the members of the vanillyl-alcohol oxidase family of flavoenzymes, three-dimensional structure analysis, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
N- and O-linked sugar chains, the enzyme contains 15.2% carbohydrates
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
-
the enzyme contains 74% protein, 16.4% neutral sugar and 2.4% amino sugar, major component: mannose
glycoprotein
-
carbohydrate content between 10.7 and 16.5%, major component: mannose
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
-
carbohydrate content between 10.7 and 16.5%, major component: mannose
glycoprotein
-
no significant differences in catalytic properties of glyco- and aglyco-GOD
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
no glycoprotein
-
recombinant enzyme is nonglycosylated
glycoprotein
-
-
glycoprotein
Penicillium variabile
Q70FC9
the recombinant enzyme from Pichia pastoris is higher glycosylated, 17%, compared to the native enzyme, 14%
glycoprotein
Penicillium variabile P16
-
the recombinant enzyme from Pichia pastoris is higher glycosylated, 17%, compared to the native enzyme, 14%
-
additional information
-
endo-beta-N-acetylglucosaminidase from Flavobacterium sp. releases about 30% of the N-linked sugar chains from the enzyme
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
of the partially deglycosylated enzyme, crystal structure determined by isomorphous replacement and refined to 2.3 A resolution
-
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
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1.9
-
-
stable for 1 h, when FAD is added, bound to Blue Dextran
2
-
-
acid-induced unfolding of both forms of enzyme, significant loss of FAD cofactor and secondary structure
2.5
-
-
the BTL wild-type strain enzyme is slightly more stable than the commercially available enzyme
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
3
5
-
deglycosylated enzyme, 4C, 4 months, 65-75% activity retained
3
9
-
2 h, 25C, 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
3
-
-
the BTL wild-type strain enzyme is slightly more stable than the commercially available enzyme
3
-
-
at 4C, 7 months, glycine/HCl buffer, residual activity of the glycosylated enzyme: 34%, residual activity of the deglycosylated enzyme: 10%
3
-
Penicillium pinophilum
-
50% activity
3
-
Penicillium variabile
Q70FC9
half-life native enzyme: 166.3 min
4
5.5
-
-
4
-
-
rapid inactivation below
4
-
-
both the BTL wild-type strain enzyme and the commercially available enzyme are stable for at least 48 h
4
-
-
at 4C, 7 months, acetate buffer, residual activity of the glycosylated enzyme: 65%, residual activity of the deglycosylated enzyme: 59%; at 4C, 7 months, glycine/HCl buffer, residual activity of the glycosylated enzyme: 58%, residual activity of the deglycosylated enzyme: 30%
4.5
5.2
-
recombinant enzyme, exhibits more than 80% of the maximum activity
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
4.5
9
-
stable
5
7
-
native and immobilized enzyme
5
7
-
at 40C, 2 h
5
7
-
recombinant enzyme, more than 90% of the residual activity retained after 72 h incubation at room temperature
5
8
-
native and deglycosylated form
5
-
-
both the BTL wild-type strain enzyme and the commercially available enzyme are stable for at least 48 h
5
-
-
at 4C, 7 months, acetate buffer, residual activity of the glycosylated enzyme: 81%, residual activity of the deglycosylated enzyme: 60%
5
-
Penicillium pinophilum
-
extremely stable, no loss of activity detected after 300 days at 4C and 30C
5.5
-
-
50C, most stable, immobilized enzyme
6
-
-
50C, most stable at, soluble enzyme
6
-
-
both the BTL wild-type strain enzyme and the commercially available enzyme are stable for at least 48 h
6
-
-
at 4C, 7 months, acetate buffer, residual activity of the glycosylated enzyme: 76%, residual activity of the deglycosylated enzyme: 70%; at 4C, 7 months, phosphate buffer, residual activity of the glycosylated enzyme: 80%, residual activity of the deglycosylated enzyme: 75%
6
-
Penicillium pinophilum
-
extremely stable
6
-
-
at pH 6.0 and at 50C, the half life of the enzyme is about 20 h
6.2
6.5
-
recombinant enzyme, exhibits more than 80% of the maximum activity
7
-
-
at 4C, 7 months, phosphate buffer, residual activity of the glycosylated enzyme: 88%, residual activity of the deglycosylated enzyme: 87%; at 4C, 7 months, Tris/HCl buffer, residual activity of the glycosylated enzyme: 71%, residual activity of the deglycosylated enzyme: 70%
7
-
-
above, the recombinant enzyme is slightly less stable than native and deglycosylated enzyme
7
-
Penicillium variabile
Q70FC9
half-life native enzyme: 76.3 min
7.5
-
Penicillium pinophilum
-
50% activity
8
-
-
unstable above
8
-
-
at 4C, 7 months, phosphate buffer, residual activity of the glycosylated enzyme: 7%, residual activity of the deglycosylated enzyme: 5%; at 4C, 7 months, TRIS/HCl buffer, residual activity of the glycosylated enzyme: 20%, residual activity of the deglycosylated enzyme: 16%
9
-
-
at 4C, 7 months, glycine/NaOH buffer, residual activity of the glycosylated enzyme: less than 5%, residual activity of the deglycosylated enzyme: less than 5%; at 4C, 7 months, Tris/HCl buffer, residual activity of the glycosylated enzyme: less than 2%, residual activity of the deglycosylated enzyme: less than 2%
10
-
-
at 4C, 7 months, glycine/NaOH buffer, residual activity of the glycosylated enzyme: less than 1%, residual activity of the deglycosylated enzyme: less than 1%
10
-
-
the native enzyme shows partial unfolding but the deglycosylated form shows a compaction of conformation
11
-
-
at 4C, 7 months, glycine/NaOH buffer, residual activity of the glycosylated enzyme: less than 1%, residual activity of the deglycosylated enzyme: less than 1%
12
-
-
at 4C, 7 months, glycine/NaOH buffer, residual activity of the glycosylated enzyme: less than 1%, residual activity of the deglycosylated enzyme: less than 1%
additional information
-
-
comparison of soluble and immobilized enzyme
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
60
P13006
the activity of recombinant GOD increases slightly at the reaction temperature ranging from 20-40C, and then falls moderately till 60C. The recombinant enzyme retains more than 90% of activity within 40C. Over 30% of activity is lost at 50C, whereas almost no activity is detected above 60C
25
70
-
70% relative activity after 30 min at 25C, 100% activity after 30 min at 30C, 90% relative activity after 30 min at 37C, 75% relative activity after 30 min at 50C, 30% relative activity after 30 min at 70C
25
-
-
10 h, purified enzyme, stable
35
-
-
stable up to
37
-
-
half-life: 30 min, purified enzyme
37
-
-
half-life of 40 h
37
-
-
GOD has half-life of approximately 30 min at 37C, immobilized GOD is more effective for applications at 37C
37
-
-
at 37C and in pH 7.5 buffer, the half life of the native enzyme is 48 h
37
-
-
at 37C and in pH 7.5 buffer, the half life of the recombinant enzyme yGOXpenag is 6 h
37
-
-
loss in specific activity of PEGylated GOx and native GOx in the absence of glucose and at 37C, 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
40
-
-
60 min
40
-
-
up to, soluble enzyme
40
-
-
up to, soluble enzyme
40
-
-
at or below both the BTL wild-type strain enzyme and the commercially available enzyme are stable for at least 48 h
40
-
Penicillium pinophilum
-
at pH 2-4 and pH 7-8, half life: less than 1 day
40
-
-
purified enzyme, half-life: 30 min
40
-
Penicillium variabile
Q70FC9
half-life native enzyme: 103 min, half-life recombinant enzyme: 26 min
45
65
-
at 45C the enzyme half-life is 99 min and at 65C it is 20.38 min under similar conditions
45
-
-
bound to Blue Dextran, in the absence of added FAD, 60% activity retained after 3 h
45
-
-
30 min, considerable inactivation
45
-
Penicillium variabile
Q70FC9
half-life native enzyme: 23 min, half-life recombinant enzyme: 3 min
50
60
-
at pH 6.0 and at 50C, the half life of the enzyme is about 20 h, thermal denaturation is observed above 60C
50
70
-
the half-life is diminished from 210 min at 50C to 0.61 min at 70C, the inactivation rate constant decreases by up to 50% at temperatures between 50 and 70C in the presence of 0.6 M trehalose
50
-
-
the activity of the free enzyme decreases to 30% of the original value, the activity of the immobilized enzyme scarcely decreases
50
-
-
both native and carbonhydrate-depleted enzyme retain full activity below
50
-
-
up to, immobilized enzyme
50
-
-
stable below, pH 5.6 for 15 min
50
-
-
up to, native and deglycosylated enzyme
50
-
-
half-life of 4 h
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 50C for 35 h
50
-
-
at pH 6.0 and at 50C, the half life of the enzyme is about 20 h, thermal denaturation is observed above 50C
55
-
-
native and carbohydrate-depleted enzyme, inactivation above
55
-
-
inactivation above
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
55.8
-
-
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
-
cellular organism
-
complete inactivation
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
-
-
2 h, stable, insoluble enzyme complex
62
-
-
midpoint for loss of secondary and tertiary structure
63
-
-
half-life of native enzyme without additive: 7.5 min, half-life of enzyme in presence of lysozyme: 24 min, half-life of enzyme in presence of 1 M NaCl: 146 min, half-life of enzyme in presence of 0.2 M K2SO4: 62 min
65
-
-
soluble enzyme: inactivation, mycelia-bound: 85% activity retained
65
-
Penicillium variabile
-
completely inactive
65
-
-
the commercially available enzyme is more stable than the BTL wild-type strain enzyme
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
-
-
inmobilized enzyme, more than 60% of the activity remains
70
-
-
completely inactivated after 15 min in the absence of glucose and 50% inactivated in the presence of glucose
70
-
-
stable for 120 min
72.4
-
-
denaturation point of native enzyme
72.8
-
-
denaturation point of periodate-oxidized enzyme
73
-
-
70% loss of activity after 60 min
80
-
-
the pure enzyme is inactive at 80C, thermal resistance is high only at pH 7.0
additional information
-
-
native and carbohydrate-depleted enzyme, no decrease of activity after 100 freeze-thaw cycles
additional information
-
-
the enzyme is very stable at cold temperatures
additional information
-
-
glucose stabilizes against heat inactivation
additional information
-
-
comparison of stability of enzyme from different sources
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 60C 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
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
3C, little loss of activity, 3 years
-
4.0 M urea, immunoaffinity-layered preparation retains 87% of original activity after 2 h and 40% of activity after 24 h of incubation, whereas the soluble enzyme loses all of its activity within 1 h of preincubation
-
after immobilization of the oxidized GOX with silver nanoparticles, the Km and Vmax of the immobilization enzyme remarkably reduce and increase, respectively. While the bioconjugate is stable in lower temperatures and also in neutral to basic pH, the enzymatic activity of the bioconjugate slightly decreases in higher temperature
-
Ca2+ and Mg2+ at 1 M induce compaction of the native conformation of the enzyme, and the enzyme shows a higher stability as compared to the native enzyme against urea denaturation, Ca2+ and Mg2+ at concentrations above 2 M induce dissociation of the native dimeric enzyme, resulting in stabilization of the enzyme monomer, 3 M Ca2+-stabilized monomer retains about 70% secondary structure present in the native enzyme dimer, however there is a complete loss of cooperative interactions between these secondary structural elements present in the enzyme
-
chemical denaturation by 6.67 M guanidine HCl is accompanied by dissociation of the homodimeric enzyme into monomers
-
comparative stability of insoluble complexes of enzyme obtained with concanavalin A and glycosyl-specific polyclonal antibodies, overview
-
comparison of stability immobilized on various materials
-
D2O stabilizes
-
divalent cations such as Ba2+, Ca2+ and Mg2+ have a slightly negative effect on stability
-
encapsulation of the enzyme in the liposomes composed of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine increases the enzyme stability through its decreased inhibition because of H2O2 produced in glucose oxidation
-
freezing/thawing, stable
-
K2SO4 enhances the thermal stability by primarily strengthening the hydrophobic interactions and makes the holoenzyme a more compact dimeric structure
-
KCl stabilizes
-
low temperature ultrasonic processing of GOx (23 kHz at 4C) does not appreciably compromise bioactivity
-
most stable, highly active and high-yield glucose oxidase preparations are optained by assembling the enzyme on small amounts of immunoaffinity support using glycosyl-specific polyclonal antibodies
-
NaCl stabilizes
-
SDS, 1%, 30C, pH 5.5, stable 30 h incubation
-
SDS, 1.5%, 2-mercaptoethanol, 55C, residual activity: 24%
-
SDS, 5%, stable to
-
stabilita to 4 M urea of soluble and insoluble enzyme complexes, overview
-
the activity of glucose oxidase is retained for more than three days in the water pool of the microemulsion, while a 30% loss in activity of the enzyme occurs in aqueous medium during that period
-
the complexation between GOX, chitosan, and calcium alginate stabilizes the enzyme, GOX retains its integrity upon adsorption to calcium alginate gel beads during the coating and after release from alginate/chitosan microsphere
-
the enzyme stability is not influenced by physiological concentration of sodium chloride (140 mM)
-
the maximum enzymatic activity of copolymer-conjugated GOD (poly(N-isopropylacrylamide-co-methacrylic acid-co-octadecylacrylate)-conjugated GOD) is about 40-55% of that of native GOD
-
the poly(methyl methacrylate)-bovine serum albumin particle-adsorbed GOx can retain at least 80% of the free enzyme activity
-
the stabilization of the enzyme by NaCl and lysozyme is primarily the result of charge neutralization
-
urea: 7 M, 5 min, activity fully restored
-
the enzyme stability is not influenced by physiological concentration of sodium chloride (140 mM)
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Acetone
-
50%, 37C, 6 h, immunoeffinity immobilized enzyme preparation retains 72% of the original activity, soluble enzyme retains 18% of the initial activity
Acetone
-
2h, 37C, 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
dimethylformamide
-
50%, 37C, 6 h, immunoeffinity immobilized enzyme preparation retains 99% of the original activity, soluble enzyme retains 63% of the initial activity
dioxane
-
50%, 37C, 6 h, immunoeffinity immobilized enzyme preparation retains 99% of the original activity, soluble enzyme retains 63% of the initial activity
dioxane
-
2h, 37C, 10-50%, effects on soluble and insoluble enzyme complexes, overview
tetrahydrofuran
-
50%, 37C, 6 h, immunoeffinity immobilized enzyme preparation retains 87% of the original activity, soluble enzyme retains 1% of the initial activity
tetrahydrofuran
-
2h, 37C, 10-50%, effects on soluble and insoluble enzyme complexes, overview
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, lyophilised enzyme, minimum of 6 months, remains stable
-
-20C, purified thioaniline-functionalized enzyme, at least three months, no noticeable degradation in its activity
-
0C, as a solid, stable for at least 2 years
-
3C, purified enzyme, several years
-
4C, immobilized, 11% loss of activity, 1 year
-
4C, lyophilized enzyme, no loss of activity after 1 year, 10% loss of activity after 2 years
-
4C, purified recombinant enzyme in 100 mM sodium phosphate, pH 5.1, several months, no loss of activity
-
4C, storage for 30 days with a retainment of 90% activity
-
lyophilized, over P2O5
-
4C, immobilized, 3 months
-
4C, immobilized, membrane in dried state, more than 12 months
-
4C, more than 90% activity retained, 100 mM phosphate buffer, pH 7, immobilized, 4 months
-
-15C crystalline suspension, stable for at least 8 years
-
0C, as a solid, stable for at least 2 years
-
4C, purified recombinant enzyme in 100 mM sodium phosphate, pH 5.1, several months, no loss of activity
-
4-5C, immobilized, 90% activity retained, 8 months
-
the lyophilized purified enzyme is stable at -20 C for a minimum of 6 months.
-
frozen, at least 1 week
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonium sulfate precipitation
P13006
ammonium sulfate precipitation and anion exchange column chromatography
-
ammonium sulfate precipitation, ion exchange chromatography, and gel filtration
-
from BTL wild-type strain using ammonium sulfate precipitation, column chromatography on Q-Sepharose at pH 6 and pH 4.5 and gel filtration on SW-300
-
from commercial preparation
-
from commercial preparation using DEAE-cellulose chromatography and Sephadex G-200 gel filtration
-
G-25 column chromatography
-
HiTrap phenyl HP column chromatography and HiTrap Q FF column chromatography
-
native enzyme by ammonium sulfate fractionation, ion exchange chromatography, and gel filtration
-
native enzyme by liquid-liquid cationic reversed micelles extraction, CTAB micelles, method evaluation, overview
-
phenyl Sepharose column chromatography, Q Sepharose column chromatography, gel filtration
-
purchased and further purified by DEAE-Toyopearl 650M column chromatography
-
Sephacryl 200 gel filtration
-
Sephadex G-50 gel filtration
-
using dialysis, ammonium sulfate fractionation and column chromatography on DEAE-cellulose
-
recombinant protein, gel filtration
-
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
-
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
-
from a partially purified sample, using column chromatography on DEAE-cellulose; from commercial preparation
-
isolation of glyco-GOD and aglyco-GOD from tunicamycin containing growth medium
-
of the reactivated recombinant enzyme, using mild acidification and anion-exchange chromatography on Q-Sepharose
-
phenyl Sepharose column chromatography and Q Sepharose column chromatography
-
using ion-exchange chromatography on a Mono Q HR 5/5 column
-
ammonium sulfate precipitation, DEAE cellulose column chromatography, and Sephadex G-100 gel filtration
-
using high performance hydrophobic-interaction chromatography on a pentylagarose column
-
native enzyme to homogeneity
-
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
Penicillium pinophilum
-
native enzyme 63fold by ammonium sulfate fractionation, ultrafiltration, anion exchange chromatography, and gel filtration, to 93% purity
-
recombinant enzyme 2.4fold from Pichia pastoris culture supernatant by ultrafiltration, anion exchange chromatography, and gel filtration
Penicillium variabile
Q70FC9
using ion-exchange chromatography on DEAE-Sepharose and gel filtration chromatography on Sephacryl S-300
Penicillium variabile
-
using column chromatography on DEAE-Sephadex, Sephacryl S-300 and DEAE-Sepharose
-
using ammonium sulfate precipitation, gel filtration, anion-exchange and hydrophobic-interaction chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
construction of a recombinant strain, the recombinant strain produces up to four times more extracellular enzyme than wild type under identical conditions
-
expressed in Nicotiana tabaccum cultivar SR1
-
expressed in Pichia pastoris strain GS115
-
expressed in Pichia pastoris strain SMD1168
P13006
expressed in Saccharomyces cerevisiae
-
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
-
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
-
gene HaGox, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real time-PCR expression analysis
B2MW81, -
recombinant protein, expressed in Escherichia coli strain BL21, pET17b expression vector
-
cloning of the gene encoding the enzyme and expression in Escherichia coli
-
expressed in Pichia pastoris strain GS115
-
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
Penicillium variabile
Q70FC9
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
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
GOX protein expression levels and GOX enzymatic activities increase with dietary glucose
B2MW81, -
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
D9ZFI1
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
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
T56V/T132S
-
site-directed mutagenesis, the mutant shows improved catalytic efficiency. The protein has three native cysteines, of which two are involved in a disulfide bond and the third is a free cysteine, Cys 521
T56V/T132S/C521S
-
site-directed mutagenesis, the mutant shows improved catalytic efficiency, mutation C521S does not alter enzyme activity, but the attachment of AuNPs to the native free thiol is prevented
Y435C
-
site-directed mutagenesis, the mutation does not affect enzyme activity. Attachment of gold nanoparticles to the purified proteins leads to an immediate and dramatic decrease in activity
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
additional information
-
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
-
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
-
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
-
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
-
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 60C 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
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
thermal denaturation of glucose oxidase is an irreversible transition to the compact denatured form with a defined oligomeric structure that is significantly different from the chemically denatured state of the enzyme, unfolded monomer
-
refolding after treatment with 8 M urea and 30 mM dithiothreitol and subsequent dilution in a buffer containing reduced glutathione, FAD and glycerol
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
biosensor system prepared for continuous flow analysis of enzyme activity
analysis
-
immobilized enzyme on polyacrylamide employed for the determination of glucose concentration in blood sera
analysis
-
phosphate sensor consisting of glucose oxidase coimmobilized with glutaraldehyde with maltose phosphorylase and bovine serum albumin
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 enzyme is useful in designing of biosensors for use in clinical, biochemical, and diagnostic assays
analysis
-
the enzym eis used in a model system to study physiological effects of hepatic H2O2 release on rat liver
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
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
-
transgenic expression of glucose oxidase may be deployed to improve cold tolerance potential of higher plants
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
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
-
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
synthesis
-
preparative production of hydroquinone using a column packed with the enzyme immobilized onto alumina, O2 is replaced with benzoquinone
synthesis
-
enzymatic biotransformation of (4R)-limonene to carvone involves addition of glucose oxidase and peroxidase to the biotransformation medium
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
analysis
Aspergillus niger NFCCP
-
the enzyme is useful in designing of biosensors for use in clinical, biochemical, and diagnostic assays
-
analysis
-
enzyme immobilized in Bombyx mori silk fibroin membrane applied to glucose sensor
medicine
-
analysis of the chronic inflammatory skin disorder Atopic eczema (AE)
biotechnology
-
GOX is the most widely used enzyme for the development of electrochemical glucose biosensors and biofuel cell in physiological conditions
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
analysis
-
the enzyme might by useful in designing of biosensors for use in clinical, biochemical, and diagnostic assays
analysis
Penicillium sp. CBS 120262
-
the enzyme might by useful in designing of biosensors for use in clinical, biochemical, and diagnostic assays
-
analysis
Penicillium variabile
Q70FC9
the enzyme finds wide application in food industry and clinical analysis
analysis
Penicillium variabile P16
-
the enzyme finds wide application in food industry and clinical analysis
-
synthesis
-
AldO is an enantioselective biocatalyst for the kinetic resolution of racemic 1,2-diols
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
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
industry
-
oxygen scavenger, chemical bleaching, used for gluconic acid production and in glucose sensor/assays
additional information
-
GOx bioactive paper is fabricated, which can potentially be used as food packaging paper