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Information on EC 1.1.3.4 - glucose oxidase and Organism(s) Penicillium amagasakiense and UniProt Accession P81156
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1.1.3.4 glucose oxidaseIUBMB Comments
A flavoprotein (FAD).
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The taxonomic range for the selected organisms is: Penicillium amagasakiense
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
glucose oxidase, d-glucose oxidase, microcid, goxp5, ygoxpenag, cngoxa, beta-d-glucose oxidase, notatin, glucose aerodehydrogenase, beta-d-glucose oxygen 1-oxidoreductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
beta-D-glucose oxidase
-
-
-
-
beta-D-glucose:oxygen 1-oxido-reductase
-
-
-
-
beta-D-glucose:quinone oxidoreductase
-
-
-
-
corylophyline
-
-
-
-
D-glucose oxidase
-
-
-
-
D-glucose-1-oxidase
-
-
-
-
deoxin-1
-
-
-
-
glucose aerodehydrogenase
-
-
-
-
glucose oxyhydrase
-
-
-
-
GOD
-
-
-
-
microcid
-
-
-
-
notatin
-
-
-
-
oxidase, glucose
-
-
-
-
penatin
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2
stereochemistry
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
beta-D-glucose:oxygen 1-oxidoreductase
A flavoprotein (FAD).
CAS REGISTRY NUMBER
COMMENTARY
9001-37-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
6-deoxy-6-fluoro-D-glucose + O2 + H2O
6-deoxy-6-fluoro-D-glucono-1,5-lactone + H2O2
-
3% relative activity to beta-D-glucose, when determined with an unspecified enzyme at 0.5 M substrate concentration
-
?
D-glucosone + O2 + H2O
? + H2O2
-
30% relative activity to beta-D-glucose
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
kinetic studies on the oxidation of beta-D-glucose combined with molecular modelling show the side chain of Arg516, which forms two hydrogen bonds with the 3-OH group of beta-D-glucose, to be absolutely essential for the efficient binding of beta-D-glucose. Of the residues forming the active site of glucose oxidase, Arg516 is the most critical amino acid for the efficient binding of beta-D-glucose by the enzyme, whereas aromatic residues at positions 73, 418 and 430 are important for the correct orientation and maximal velocity of glucose oxidation
-
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
recombinant enzyme
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
25% relative activity to beta-D-glucose, when determined with a commercial preparation of the enzyme at 0.1 M substrate concentration, 12% relative activity to beta-D-glucose, when determined with a commercial preparation of glucose oxidase, containing catalase, at 0.05 M substrate concentration
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
kinetic mechanism
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
glucose is the primary substrate, recombinant enzyme
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
the enzyme can use 2,6-dichlorophenolindophenol as hydrogen acceptor in addition to oxygen, the rate of glucose oxidation in the presence of 2,6-dichlorophenolindophenol is only 3.3% of that in the presence of oxygen
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
dimerization is only possible with the proper incorporation of the cofactor in the FAD-binding pocket
FAD
enzyme pen-GOx contains one mol of tightly but not covalently bound FAD cofactor at the active site of each subunit. The FAD-binding domain of GOx is formed by a beta-sheet lid. The lid prevents the release of FAD from the dimer. Loosening of tertiary structure leads to opening of this lid, causing FAD loss anddissociation of the dimer. Loss of FAD from GOx is concurrent with tertiary structure loss. FAD, especially isoalloxazine, is important for the catalytic activity for beta-D-glucose. The binding of FAD cofactor also plays a key role on the catalytic activity of flavoproteins for the correct folding, assembly and protein stability. The three-dimensional structure of the glucose oxidase is stabilized by FAD, which can act as a redox carrier in catalysis
FAD
-
defined as flavoprotein oxidase, two very tightly bound FAD molecules per dimer, kinetic behavior
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0638
ferrocinium-methanol
-
recombinant enzyme yGOXpenag, pH 6.0, 50°C
additional information
additional information
-
values for glyco-enzyme and aglyco-enzyme
-
2.5
beta-D-glucose
-
recombinant wild-type enzyme, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme
2.6
beta-D-glucose
-
recombinant mutant K424E, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme
3.2
beta-D-glucose
-
recombinant mutant K424E, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme
3.4
beta-D-glucose
-
recombinant mutant K424I, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme
3.8
beta-D-glucose
-
recombinant wild-type enzyme, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme
11.7
beta-D-glucose
-
recombinant enzyme yGOXpenag, using O2 as cosubstrate, pH 6.0, 50°C
18.2
beta-D-glucose
-
recombinant enzyme yGOXpenag, using ferrocinium-methanol as cosubstrate, pH 6.0, 50°C
22
beta-D-glucose
-
recombinant mutant K424I, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
238
beta-D-glucose
-
recombinant wild-type enzyme, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme
245
beta-D-glucose
-
recombinant mutant K424I, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme
250
beta-D-glucose
-
recombinant mutant K424E, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme
433
beta-D-glucose
-
recombinant mutant K424I, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme
458
beta-D-glucose
-
recombinant wild-type enzyme, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme
464
beta-D-glucose
-
recombinant mutant K424E, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme
1695
beta-D-glucose
-
recombinant enzyme yGOXpenag, using ferrocinium-methanol as cosubstrate, pH 6.0, 50°C
1808
beta-D-glucose
-
recombinant enzyme yGOXpenag, using O2 as cosubstrate, pH 6.0, 50°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.027
ferrocinium-methanol
-
recombinant enzyme yGOXpenag, pH 6.0, 50°C
93
beta-D-glucose
-
recombinant enzyme yGOXpenag, using ferrocinium-methanol as cosubstrate, pH 6.0, 50°C
95.2
beta-D-glucose
-
recombinant wild-type enzyme, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme
96
beta-D-glucose
-
recombinant mutant K424E, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme
120
beta-D-glucose
-
recombinant wild-type enzyme, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme
122
beta-D-glucose
-
recombinant mutant K424I, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme
127
beta-D-glucose
-
recombinant mutant K424I, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme
145
beta-D-glucose
-
recombinant mutant K424E, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme
155
beta-D-glucose
-
recombinant enzyme yGOXpenag, using O2 as cosubstrate, pH 6.0, 50°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
enzyme structure and structure-activity relationship analysis and molecular dynamic simulations, detailed overview. Active-site residues of pen-GOx are two histidines, His520 and His563, which act as general base and general acid in the reductive half-reaction and the oxidative half-reaction, respectively
additional information
-
424 is a key position for enzyme activity of the immobilized enzyme on electrode surfaces, overview
additional information
-
enzyme denaturing process analysis by molecular dynamics simulations, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GOX_PENAG
587
0
63965
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
160000
167000
-
glycosylated enzyme, PAGE under non-dissociating conditions
45000
-
4 * 45000, 2 polypeptide chains linked by disulfide bond, sedimentation equilibrium centrifugation, treatment with guanidine-HCl and 2-mercaptoethanol
60000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
2 * 66700, SDS-PAGE and crystal structure analysis
dimer
homodimer
tetramer
-
4 * 45000, 2 polypeptide chains linked by disulfide bond, sedimentation equilibrium centrifugation, treatment with guanidine-HCl and 2-mercaptoethanol
additional information
dimer
-
each unit in the dimer is composed of two polypeptide chains connected by a disulfide bond
additional information
enzyme structure and structure-activity relationship analysis and molecular dynamic simulations, detailed overview. The three-dimensional structure of the glucose oxidase is stabilized by FAD, which can act as a redox carrier in catalysis
additional information
-
the monomers of GOx-pa contain 587 amino acids each, and one prosthetic group, flavin adenine dinucleotide (FAD). Dimer interface analysis
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
the enzyme consists of 13% carbohydrate comprising 95 residues of mannose, 12 residues of glucosamine and 5 residues of galactose per molecule of enzyme, six N-glycosylation sites estimated for the dimer
glycoprotein
-
no significant differences in catalytic properties of glyco- and aglyco-GOD
glycoprotein
-
carbohydrate content between 10.7 and 16.5%, major component: mannose
glycoprotein
-
the enzyme has four N-glycosylation sites at positions ASN93, ASN165, ASN357, and ASN392, respectively. Three different sugars are bound at these positions: N-acetyl-D-glucosamine, beta-D-mannose, and alpha-D-mannose
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
deglycosylation and purification to isoelectric homogeneity are important prerequisite steps to obtain crystals suitable for X-ray investigations. Crystals of the deglycosylated enzyme are reproducibly grown using ammonium sulfate as precipitant at pH 7.4 to 7.5. Crystals diffract to at least 2.0 A resolution and belong to the orthorhombic space group P2(1)2(1)2(1), with refined lattice constants of a = 59.3 A, b = 136.3 A and c = 156.7 A. Crystallized as a complex with the coenzyme FAD
the enzyme crystallizes from 1.3 M ammonium sulfate, 100 mM citrate/phosphate buffer pH 7.4 in the orthorhombic space group P212121, with unit-cell dimensions a = 57.6, b = 132.1, c = 151.3 A and one dimeric molecule per asymmetric unit. The structure is determined by molecular replacement and refined at 1.8 A resolution to an R value of 16.4%
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K424E
increased electron transfer (2.4fold), 20% decrease in O2 sensitivity
R516K
the mutant enzyme whose side chain forms only one hydrogen bond with the 3-OH group of beta-D-glucose, exhibits an 80fold higher apparent Km (513 mM) but a Vmax only 70% lower than the wild type
R516Q
the complete elimination of a hydrogen-bond interaction between residue 516 and the 3-OH group of beta-D-glucose through the substitution R516Q effects a 120fold increase in the apparent Km for glucose (to 733 mM) and a decrease in the Vmax to 1/30
S114A/F355L
increased electron transfer, 88% decrease in O2 sensitivity
V464A/K424E
2.4fold increase in electron transfer, 95% decrease in O2 sensitivity
V564S
1.1fold increase in electron transfer, 88% decrease in O2 sensitivity
G423D
K424E
-
site-directed mutagenesis, the single mutation results in a significant increase in the current density which becomes 2.4 fold higher than the current obtained for the wild-type
K424I
-
site-directed mutagenesis, the mutation does not significantly affect the enzyme activity
additional information
G423D
-
site-directed mutagenesis, the mutant shows no activity compared to the wild-type enzyme
G423D
-
site-directed mutagenesis, the mutants containing the mutation G423D leads to quadruple mutants that are not able to reconstitute. The mutant enzymes displays a dramatic decrease in activity compared to thré wild-type enzyme
additional information
the removal of aromatic or bulky residues at positions 73, 418 or 430 result in decreases in the maximum rates of glucose oxidation to less than 1/90
additional information
-
the removal of aromatic or bulky residues at positions 73, 418 or 430 result in decreases in the maximum rates of glucose oxidation to less than 1/90
additional information
-
for use on electrode surfaces, the key amino acid at the entrance of the active site of glucose oxidase from Penicilium amagasakiense, Lys424, Gln75, Gln184, and Gly423, are redesign by nonactive site mutations, leading to enzymatic anodes with 2.4fold higher current densities, making the biosensor more effective. 424 is the key position
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
-
at 4°C, 7 months, glycine/NaOH buffer, residual activity of the glycosylated enzyme: less than 1%, residual activity of the deglycosylated enzyme: less than 1%
389832
11
-
at 4°C, 7 months, glycine/NaOH buffer, residual activity of the glycosylated enzyme: less than 1%, residual activity of the deglycosylated enzyme: less than 1%
389832
12
-
at 4°C, 7 months, glycine/NaOH buffer, residual activity of the glycosylated enzyme: less than 1%, residual activity of the deglycosylated enzyme: less than 1%
389832
3
-
at 4°C, 7 months, glycine/HCl buffer, residual activity of the glycosylated enzyme: 34%, residual activity of the deglycosylated enzyme: 10%
389832
4.5 - 5.2
-
recombinant enzyme, exhibits more than 80% of the maximum activity
389835
5
-
at 4°C, 7 months, acetate buffer, residual activity of the glycosylated enzyme: 81%, residual activity of the deglycosylated enzyme: 60%
389832
5 - 7
-
recombinant enzyme, more than 90% of the residual activity retained after 72 h incubation at room temperature
389835
6.2 - 6.5
-
recombinant enzyme, exhibits more than 80% of the maximum activity
389835
4
-
at 4°C, 7 months, glycine/HCl buffer, residual activity of the glycosylated enzyme: 58%, residual activity of the deglycosylated enzyme: 30%
389832
4
-
at 4°C, 7 months, acetate buffer, residual activity of the glycosylated enzyme: 65%, residual activity of the deglycosylated enzyme: 59%
389832
6
-
at 4°C, 7 months, acetate buffer, residual activity of the glycosylated enzyme: 76%, residual activity of the deglycosylated enzyme: 70%
389832
6
-
at 4°C, 7 months, phosphate buffer, residual activity of the glycosylated enzyme: 80%, residual activity of the deglycosylated enzyme: 75%
389832
6
-
at pH 6.0 and at 50°C, the half life of the enzyme is about 20 h
712533
7
-
above, the recombinant enzyme is slightly less stable than native and deglycosylated enzyme
389835
7
-
at 4°C, 7 months, Tris/HCl buffer, residual activity of the glycosylated enzyme: 71%, residual activity of the deglycosylated enzyme: 70%
389832
7
-
at 4°C, 7 months, phosphate buffer, residual activity of the glycosylated enzyme: 88%, residual activity of the deglycosylated enzyme: 87%
389832
8
-
at 4°C, 7 months, phosphate buffer, residual activity of the glycosylated enzyme: 7%, residual activity of the deglycosylated enzyme: 5%
389832
8
-
at 4°C, 7 months, TRIS/HCl buffer, residual activity of the glycosylated enzyme: 20%, residual activity of the deglycosylated enzyme: 16%
389832
9
-
at 4°C, 7 months, glycine/NaOH buffer, residual activity of the glycosylated enzyme: less than 5%, residual activity of the deglycosylated enzyme: less than 5%
389832
9
-
at 4°C, 7 months, Tris/HCl buffer, residual activity of the glycosylated enzyme: less than 2%, residual activity of the deglycosylated enzyme: less than 2%
389832
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
at 37°C and in pH 7.5 buffer, the half life of the recombinant enzyme yGOXpenag is 6 h
50
-
at pH 6.0 and at 50°C, the half life of the enzyme is about 20 h, thermal denaturation is observed above 50°C
additional information
additional information
-
comparison of stability of enzyme from different sources
additional information
-
enzyme denaturing process at different temperatures, localization of breaking points, analysis by molecular dynamics simulations, overview. Identification of the transition state of protein folding/unfolding, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme stability is not influenced by physiological concentration of sodium chloride (140 mM)
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified recombinant enzyme in 100 mM sodium phosphate, pH 5.1, several months, no loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
all reconstituted variants are purified to homogeneity by mild acidification and ion-exchange chromatography
from a partially purified sample, using column chromatography on DEAE-cellulose
-
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli, expression of all enzyme variants leads to the formation of insoluble inclusion bodies. Refolding of most variants can be followed by measuring increases in enzyme activity
overexpressed either in Escherichia coli or in Pichia pastoris
cloning of the gene encoding the enzyme and expression in Escherichia coli
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
refolding after treatment with 8 M urea and 30 mM dithiothreitol and subsequent dilution in a buffer containing reduced glutathione, FAD and glycerol
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
GOX is the most widely used enzyme for the development of electrochemical glucose biosensors and biofuel cell in physiological conditions
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Eriksson, K.O.; Kourteva, I.; Yao, K.; Liao, J.L.; Kilar, F.; Hjerten, S.
Application of high-performance chromatographic and electrophoretic methods to the purification and characterization of glucose oxidase and catalase from Penicillium chrysogenum
J. Chromatogr.
397
239-249
1987
Aspergillus niger, Penicillium amagasakiense, Penicillium chrysogenum, Penicillium janthinellum, Talaromyces purpureogenus
Bright, H.J.; Porter, D.J.T.
Flavoprotein oxidases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
12
421-505
1975
Aspergillus niger, Penicillium amagasakiense
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Bentley, R.
Glucose oxidase
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1963
Aspergillus niger, Mycoderma aceti, Penicillium amagasakiense
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Kusai, K.; Sekuzu, I.; Hagihara, B.; Okumuki, K.; Yamaguchi, S.; Nakai, M.
Crystallization of glucose oxidase from Penicillium amagasakiense
Biochim. Biophys. Acta
40
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1960
Penicillium amagasakiense
Yoshimura, T.; Isemura, T.
Subunit structure of glucose oxidase from Penicillium amagasakiense
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1971
Penicillium amagasakiense
Hayashi, S.; Nakamura, S.
Comparison of fungal glucose oxidases. Chemical, physicochemical and immunological studies
Biochim. Biophys. Acta
438
37-48
1976
Aspergillus niger, Penicillium amagasakiense
Kim, J.M.; Schmid, R.D.
Comparison of Penicillium amagasakiense glucose oxidase purified as glyco- and aglyco-proteins
FEMS Microbiol. Lett.
78
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1991
Penicillium amagasakiense
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Kalisz, H.M.; Hendle, J.; Schmid, R.D.
Structural and biochemical properties of glycosylated and deglycosylated glucose oxidase from Penicillium amagasakiense
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47
502-507
1997
Penicillium amagasakiense
Witt, S.; Singh, M.; Kalisz, H.M.
Structural and kinetic properties of nonglycosylated recombinant Penicillium amagasakiense glucose oxidase expressed in Escherichia coli
Appl. Environ. Microbiol.
64
1405-1411
1998
Penicillium amagasakiense
Courjean, O.; Mano, N.
Recombinant glucose oxidase from Penicillium amagasakiense for efficient bioelectrochemical applications in physiological conditions
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151
122-129
2011
Aspergillus niger, Penicillium amagasakiense
Wohlfahrt, G.; Witt, S.; Hendle, J.; Schomburg, D.; Kalisz, H.M.; Hecht, H.J.
1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes
Acta Crystallogr. Sect. D
55
969-977
1999
Aspergillus niger (P13006), Aspergillus niger, Penicillium amagasakiense (P81156), Penicillium amagasakiense
Witt, S.; Wohlfahrt, G.; Schomburg, D.; Hecht, H.-J.; Kalisz, H.M.
Conserved arginine-516 of Penicillium amagasakiense glucose oxidase is essential for the efficient binding of beta-D-glucose
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347
553-559
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Penicillium amagasakiense (P81156), Penicillium amagasakiense, Penicillium amagasakiense ATCC 28686 (P81156)
Hendle, J.; Hecht, H.J.; Kalisz, H.M.; Schmid, R.D.; Schomburg, D.
Crystallization and preliminary X-ray diffraction studies of a deglycosylated glucose oxidase from Penicillium amagasakiense
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1992
Penicillium amagasakiense (P81156), Penicillium amagasakiense
Suraniti, E.; Courjean, O.; Gounel, S.; Tremey, E.; Mano, N.
Uncovering and redesigning a key amino acid of glucose oxidase for improved biotechnological applications
Electroanalysis
25
606-611
2013
Penicillium amagasakiense
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Janati-Fard, F.; Housaindokht, M.; Monhemi, H.
Investigation of structural stability and enzymatic activity of glucose oxidase and its subunits
J. Mol. Catal. B
134
16-24
2016
Penicillium amagasakiense (P81156)
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Todde, G.; Hovmoeller, S.; Laaksonen, A.; Mocci, F.
Glucose oxidase from Penicillium amagasakiense characterization of the transition state of its denaturation from molecular dynamics simulations
Proteins
82
2353-2363
2014
Penicillium amagasakiense
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