Information on EC 1.1.5.9 - glucose 1-dehydrogenase (FAD, quinone)

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

EC NUMBER
COMMENTARY hide
1.1.5.9
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RECOMMENDED NAME
GeneOntology No.
glucose 1-dehydrogenase (FAD, quinone)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-glucose + a quinone = D-glucono-1,5-lactone + a quinol
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Pentose phosphate pathway
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
D-glucose:quinone 1-oxidoreductase
A glycoprotein containing one mole of FAD per mole of enzyme. 2,6-Dichloroindophenol can act as acceptor. cf. EC 1.1.5.2, quinoprotein glucose dehydrogenase.
CAS REGISTRY NUMBER
COMMENTARY hide
37250-84-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
SM4, moderate thermophilic
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Manually annotated by BRENDA team
strain SM4
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Manually annotated by BRENDA team
anamorph Colletotrichum gloeosporoides
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Manually annotated by BRENDA team
Mucor prainii
-
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Manually annotated by BRENDA team
Mucor prainii NISL0103
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
additional information
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amperometric glucose biosensor utilizing FAD-dependent glucose dehydrogenase immobilized on nanocomposite electrode. Unlike the common glucose oxidase based biosensor, the presented biosensors is O2-independent, method and biosensorevlauation, overview. Polyphenols also do not interfere at used measuring conditions. Determination of D-glucose in beverages and wines using biosensors, HPLC and enzymatic-spectrophotometric assay, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
2-deoxy-D-glucose + a quinone
2-deoxy-D-glucono-1,5-lactone + a quinol
show the reaction diagram
-
-
-
-
?
alpha-trehalose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
0.5% activity compared to D-glucose
-
-
?
beta-D-glucose + Fe(CN)63-
D-glucono-1,5-lactone + Fe(CN)64-
show the reaction diagram
-
-
-
-
?
cellobiose + a quinone
? + a quinol
show the reaction diagram
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low activity
-
-
?
D-galactose + 2,6-dichlorophenolindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
D-galactose + acceptor
D-galactono-1,5-lactone + reduced acceptor
show the reaction diagram
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6.5% of the activity with D-glucose
-
-
?
D-glucose + 1,4-benzoquinone
D-glucono-1,5-lactone + 1,4-benzoquinol
show the reaction diagram
D-glucose + 2,6-dichlorophenolindophenol
D-gluconic acid + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + 2,6-dichlorophenolindophenol
show the reaction diagram
100% activity
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
D-glucose + a quinone
D-glucono-1,5-lactone + a quinol
show the reaction diagram
D-glucose + a quinone
D-glucono-1,5-lactone + a reduced quinol
show the reaction diagram
D-glucose + acceptor
D-glucono-1,5-lactone + reduced acceptor
show the reaction diagram
-
-
-
-
?
D-glucose + coenzyme Q1
D-glucono-1,5-lactone + reduced coenzyme Q1
show the reaction diagram
-
-
-
-
?
D-glucose + ferricenium hexafluorophosphate
D-glucono-1,5-lactone + ferrocenium hexafluorophosphate
show the reaction diagram
D-glucose + ferricenium ion
D-glucono-1,5-lactone + ferrocenium ion
show the reaction diagram
-
-
-
-
?
D-glucose + ferricyanide
D-glucono-1,5-lactone + ferrocyanide
show the reaction diagram
D-glucose + menadione
D-glucono-1,5-lactone + menadiol
show the reaction diagram
-
-
-
-
?
D-glucose + oxidized 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenol indophenol
show the reaction diagram
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + reduced phenazine methosulfate
show the reaction diagram
D-glucose + tetramethyl-p-phenylenediamine
D-glucono-1,5-lactone + reduced tetramethyl-p-phenylenediamine
show the reaction diagram
-
-
-
-
?
D-lactose + 2,6-dichlorophenolindophenol
D-lactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
D-maltose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
D-maltose + acceptor
?
show the reaction diagram
-
-
-
-
?
D-mannose + acceptor
D-manno-1,5-lactone + reduced acceptor
show the reaction diagram
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8.6% of the activity with D-glucose
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?
D-raffinose + 2,6-dichlorophenolindophenol
D-raffinono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
D-xylose + 2,6-dichloroindophenol
D-xylono-1,5-lactone + 2,6-dichlorophenolindophenol
show the reaction diagram
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
D-xylose + acceptor
D-xylono-1,5-lactone + reduced acceptor
show the reaction diagram
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13% of the activity with D-glucose
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?
D-xylose + ferricenium ion
D-xylono-1,5-lactone + ferrocenium ion
show the reaction diagram
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?
D-xylose + oxidized 2,6-dichlorophenol indophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenol indophenol
show the reaction diagram
fructose + 2,6-dichlorophenolindophenol
?
show the reaction diagram
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8% of the activity with D-glucose
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?
glutamine + a quinone
? + a quinol
show the reaction diagram
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low activity
-
-
?
L-arabinose + 2,6-dichlorophenolindophenol
L-arabinono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
1.5% activity compared to D-glucose
-
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?
L-arabinose + acceptor
L-arabinono-1,5-lactone + reduced acceptor
show the reaction diagram
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2.8% of the activity with D-glucose
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?
L-rhamnose + acceptor
L-rhamnone-1,5-lactone + reduced acceptor
show the reaction diagram
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7.5% of the activity with D-glucose
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?
maltose + 2,6-dichlorophenol indophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
maltose + 2,6-dichlorophenolindophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
maltose + acceptor
?
show the reaction diagram
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3.2% of the activity with D-glucose
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?
maltotetraose + 2,6-dichlorophenolindophenol
maltotetraono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
Mucor prainii
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0.66% activity compared to D-glucose
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?
maltotriose + 2,6-dichlorophenolindophenol
maltotriono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
mannose + 2,6-dichlorophenolindophenol
mannono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
Mucor prainii
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0.66% activity compared to D-glucose
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?
trehalose + 2,6-dichlorophenolindophenol
trehalono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
Mucor prainii
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0.22% activity compared to D-glucose
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-glucose + a quinone
D-glucono-1,5-lactone + a quinol
show the reaction diagram
D-glucose + a quinone
D-glucono-1,5-lactone + a reduced quinol
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
[3Fe-4S]-center
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additional information
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properties of the prosthetic group
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe(CN)63-
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additional information
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no activation by Ca2+ or Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
p-benzoquinone
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competitive inhibition of the activity with 2,6-dichlorophenolindophenol or coenzyme Q1, non-competitive inhibition of reaction with phenazine methosulfate
Urea
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urea causes a dose-dependent but reversible inhibition by dissoziation of the hetero-oligomeric enzyme comparable with the effect of heat-treatment, 3.5 M urea reduces GDH activity by 20%, 5 M urea by 80% and 8 M urea by ca. 90%
additional information
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not inhibited by EDTA (1-10 mM)
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04 - 1.6
2,6-dichlorophenolindophenol
0.06
coenzyme Q1
-
-
0.4638 - 89.7
D-glucose
2 - 26
D-xylose
65
Fe(CN)63-
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apparent KM-value
0.69
ferricyanide
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17 - 28
glucose
0.13 - 2.7
phenazine methosulfate
0.56
tetramethyl-p-phenylenediamine
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
69.54 - 5330
D-glucose
40 - 61
D-xylose
230
Fe(CN)63-
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apparent turnover number
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
17.6 - 24.5
D-glucose
1.9 - 2.7
D-xylose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
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A472F mutant towards maltose
6
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at 75°C after preincubation of the enzyme at 70°C for 30 min
21
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N475D mutant towards maltose
118
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N475D mutant towards glucose
120
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A472F mutant towards glucose
139
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wild type towards maltose
430
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enzymatic activity of wild-type FADGDH in an assay with 40 mM maltose
543
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wild type towards glucose
565
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purified enzyme with ferrocenium hexafluorophosphate, pH 5.5, 30°C
795
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pH and temperature not specified in the publication
840
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purified enzyme with 2,6-dichlorophenol indophenol , pH 5.5, 30°C
878
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pH and temperature not specified in the publication
950
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enzymatic activity of wild-type FADGDH in an assay with 40 mM glucose
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
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reaction with ferricyanide
5.5
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assay at with 2,6-dichlorophenol indophenol or ferrocenium hexafluorophosphate
6 - 7.5
Mucor prainii
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6
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reaction with 2,6-dichlorophenolindophenol
8.8
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reaction with phenazine methosulfate or tetramethyl-p-phenylenediamine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.5
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6.5 - 8.5
more than 70% activity between pH 6.0 and 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
40
Mucor prainii
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46
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recombinant enzyme expressed from Pichia pastoris
65
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glucose dehydrogenase cross-linked with glutaraldehyde
75
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after preincubating the enzyme at 70°C for 30 min
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 85
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20% of maximal activity at 20°C and 10% of maximal activity at 85°C, maximal activity is at 45°C with a second activity peak at 70°C (30% of maximal activity)
25 - 50
Mucor prainii
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about 70% activity at 25°C, about 90% activity at 30°C, about 95% activity at 35°C, 100% activity at 40°C, about 65% activity at 45°C, less than 20% activity at 50°C
30 - 65
about 70% activity at 30°C, about 80% activity at 35°C, about 90% activity at 45°C, about 95% activity at 50°C, 100% activity at 55°C, about 98% activity at 60°C, about 85% activity at 65°C
30 - 60
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30°C: about 45% of maximal activity, 60°C: about 25% of maximal activity, native enzyme
40 - 80
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40°C: about 45% of maximal activity, 80°C: about 45% of maximal activity, glucose dehydrogenase cross-linked with glutaraldehyde
40 - 85
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after preincubation of the enzyme at 70°C for 30 min: 15% of maximal activity at 40°C and 50% of maximal activity at 85°C, maximal activity at 75°C
50 - 80
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after preincubation with 5.8 M urea for 30 min at 25°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6
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isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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encapsulation tissue
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13000
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SDS-PAGE, X * 60000 (alpha-subunit), x * 40000 (beta-subunit), x * 18000 (gamma-subunit), x * 13000 (gamma-subunit)
40000
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SDS-PAGE, X * 60000 (alpha-subunit), x * 40000 (beta-subunit), x * 18000 (gamma-subunit), x * 13000 (gamma-subunit)
59800
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1 * 59800 + 1 * 18000, SDS-PAGE
60000
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SDS-PAGE, X * 60000 (alpha-subunit), x * 40000 (beta-subunit), x * 18000 (gamma-subunit), x * 13000 (gamma-subunit)
68000
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1 * 68000, deglycosylated enzyme, SDS-PAGE
85000
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after preincubation at 70°C for 30 min, native PAGE
86000
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calculation from titration of the prosthetic group with glucose
87000
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1 * 87000, monomeric in presence of 1% Triton X-100, aggregation after removing the detergent, urea-SDS-PAGE
88000 - 131000
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93000
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sucrose density gradient centrifugation, in presence of Triton X-100
95000 - 135000
97000
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deglycosylated enzyme, gel filtration
118000
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low speed sedimentation without reaching equilibrium
120000
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gel filtration
350000
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native PAGE
380000
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gel filtration chromatography
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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1 * 59800 + 1 * 18000, SDS-PAGE
heteromer
homooligomer
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after preincubation at 70°C for 30 min: x * 67000 (alpha-subunit), SDS-PAGE
monomer
additional information
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aggregation in medium containing no Triton X-100 to dimers, trimers and tetramers
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with FAD and/or D-glucono-1,5-lactone, sitting-drop vapor diffusion method, using 0.1 M of BisTris, pH 6.5, and 22–25% (w/v) PEG3350
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sitting drop vapor diffusion method, using 30% (w/v) PEG 8000, 0.2 M ammonium sulfate, 0.1 M sodium acetate pH 4.5
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 9
the enzyme remains stable after 20 min at pH 3.0-9.0
740853
3 - 11
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the enzyme is stable for 20 h between pH 3.0 and 11.0
740363
4
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30°C, 2 h, about 40% loss of activity
348274
5 - 5.8
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pH-dependent thermal stability with the highest Tm values in the acidic range of pH 4.5 to pH 6.4. The maximum Tm value of 56°C is measured in 50 mM sodium acetate buffer pH 5.0 and in 50 mM MES buffer pH 5.8
725879
5
Mucor prainii
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approximately 80% of the enzymatic activity is retained after incubation at 40°C for 15 min at pH 5.0. Treatment at 25°C for 16 h shows that the enzyme is stable from pH 3.5 to 7.0
740778
6 - 8
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30°C, 2 h, stable, rapid inactivation outside this range
348274
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 70
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enzyme is stable at temperatures between 5-37°C for 30 min, after incubating enzyme at 45°C for 30 min 40% of enzyme activity remains, at 70°C for 30 min 10% of enzyme activity remains
5 - 75
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after preincubation at 70°C for 30 min the enzyme is stable at temperatures between 5-50°C for 30 min, after incubating enzyme at 70°C for 30 min 70% of activity remains
25 - 40
Mucor prainii
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the enzyme remains stable after 15 min at 25-40°C, then activity drops to about 70% at 50°C and is completely lost at 55°C
30
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15 min, stable
40 - 70
after heat treatment at 40-70°C for 15 min, unglycosylated enzyme maintains nearly 100% activity at temperatures up to 45°C, but completely loses activity at 60°C, while glycosylated enzyme displays high thermostability, maintaining 89% activity at 60°C. The melting temperature of the glycosylated enzyme is 66.4°C
40 - 60
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after heat treatment at 40-60°C for 15 min, the enzyme maintains its activity close to 100%
40 - 62
unglycosylated enzym e is stable at temperatures up to 45°C , while glycosylatedenzyme maintains 75% activity at 60°C. The melting temperature of the glycosylated enzyme is 62.5°C
45
-
the wild type enzyme is inactivated rapidly at 45°C, with less than 20% of the initial activity remaining after 25 min and a half-life of inactivation of less than 10 min
50
-
15 min, about 40% loss of activity
56
-
pH-dependent thermal stability with the highest Tm values in the acidic range of pH 4.5 to pH 6.4. The maximum Tm value of 56°C is measured in 50 mM sodium acetate buffer pH 5.0 and in 50 mM MES buffer pH 5.8
65
-
half-life of native enzyme: 2.5 min, half life of enzyme cross-linked to glutaraldehyde: 72 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glucose, 0.2 M, protects during heat treatment
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, 0.05 M potassium phosphate buffer, pH 6.5, 10% loss of activity after 3 months, 50% loss of activity after 6 months
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GcGDH/Os-polymer modified electrode under storage conditions of 50 mM phosphate buffer, pH 7.4, 4 °C, injection of 0.05 ml of a 5 mM glucose solution into the electrochemical cell for 6 days, the biosensor keeps more than 90% of its initial activity after the first day
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; by DEAE-5PW and Superdex-200 10/300GL column chromatography
-
DEAE-5PW column chromatography and Superdex-200 gel filtration
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HisTrap nickel affinity chromatography
-
isopropanol precipitation and nickel affinity column chromatography
native extracellular enzyme 23.7fold from culture supernatant by anion exchange and hydrophobic interaction chromatography, ammonium sulfate fractionation, and ultrafiltration
-
Ni-NTA agarose column chromatography
recombinant enzyme from Escherichia coli strain BL21RIL
-
recombinant enzyme from Pichia pastoris strain X-33 5.1fold by hydrophobic interaction and anion exchange chromatography
-
recombinant enzyme from Pichia pastoris to homogeneity
-
resource Q column chromatography
Toyopearl Butyl-650C column chromatography, DEAE Cellufine A-500m column chromatography, and Q-Sepharose column chromatography
-
Toyopearl-butyl 650C column chromatography and SP-Sepharose column chromatography
Mucor prainii
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic analysis
-
DNA and amino acid sequence determination and analysis, phylogenetic tree, recombinant expression in Escherichia coli strain BL21 (DE3)
expressed as recombinant protein in Escherichia coli strain DH5alpha
-
expressed as recombinant protein in Escherichia coli strain DH5alpha; expression in Escherichia coli
-
expressed in Aspergillus oryzae strain NS4
-
expressed in Aspergillus sojae
Mucor prainii
-
expressed in Escherichia coli and Pichia pastoris
expressed in Escherichia coli BL21 (DE3) cells
-
expressed in Escherichia coli BL21 cells
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expressed in Escherichia coli strain BLR(DE3) and Pichia pastoris strain GS115
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expressed in Escherichia coli strain Origami2 (DE3)
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expressed in Escherichia coli strain Origami2(DE3)
-
expressed in Pichia pastoris strain GS115
expression in Escherichia coli strain BL21RIL, no GDH activity when cells expressing the alpha-subunit alone
-
recombinant expression in Pichia pastoris
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recombinant overexpression in Escherichia coli strains Rosetta 2, T7 Express and T7 Express (pGro7) and Pichia pastoris strain X-33, with a much higher expression level and 4800fold higher enzyme activity in Pichia pastoris, fed-batch cultivation of a Pichia pastoris transformant, method evaluation, overview
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H505A
-
the mutant enzyme shows drastic decrease in the enzymatic activity
H548A
-
the mutant enzyme shows drastic decrease in the enzymatic activity
V149C/G190C
-
the mutant shows a 110 min half-life of thermal inactivation at 45°C, which is 13fold greater than that of the wild type enzyme
H505A
-
the mutant enzyme shows drastic decrease in the enzymatic activity
-
H548A
-
the mutant enzyme shows drastic decrease in the enzymatic activity
-
A472C
-
site directed mutagenesis
A472D
-
site directed mutagenesis
A472E
-
site directed mutagenesis
A472F
-
mutant with higher substrate specificity for glucose in relation to maltose, constructed by site-directed mutagenesis; site directed mutagenesis
A472G
-
site directed mutagenesis
A472H
-
site directed mutagenesis
A472I
-
site directed mutagenesis
A472K
-
site directed mutagenesis
A472L
-
site directed mutagenesis
A472M
-
site directed mutagenesis
A472N
-
site directed mutagenesis
A472P
-
site directed mutagenesis
A472Q
-
site directed mutagenesis
A472R
-
site directed mutagenesis
A472S
-
site directed mutagenesis
A472T
-
site directed mutagenesis
A472V
-
site directed mutagenesis
A472W
-
site directed mutagenesis
A472Y
-
site directed mutagenesis
C212S
-
inactive
C213S
-
the mutant shows 68% of wild type activity
C218S
-
inactive
C222S
-
inactive
N475A
-
site directed mutagenesis
N475C
-
site directed mutagenesis
N475D
-
mutant with higher substrate specificity for glucose in relation to maltose, constructed by site-directed mutagenesis; site directed mutagenesis
N475E
-
site directed mutagenesis
N475F
-
site directed mutagenesis
N475G
-
site directed mutagenesis
N475H
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site directed mutagenesis
N475I
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site directed mutagenesis
N475K
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site directed mutagenesis
N475L
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site directed mutagenesis
N475M
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site directed mutagenesis
N475P
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site directed mutagenesis
N475Q
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site directed mutagenesis
N475R
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site directed mutagenesis
N475S
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site directed mutagenesis
N475T
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site directed mutagenesis
N475V
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site directed mutagenesis
N475W
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site directed mutagenesis
N475Y
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site directed mutagenesis
S326C
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S326E
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S326G
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S326H
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the mutant shows reduced activity toward D-glucose and increased activity with maltose compared to the wild type enzyme
S326K
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the mutant shows increased activity toward D-glucose compared to the wild type enzyme
S326Q
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the mutant shows reduced activity toward D-glucose and increased activity with maltose compared to the wild type enzyme
S326Q/S365Y
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the mutant is virtually non-reactive to maltose while retaining high D-glucose dehydrogenase activity
S326R
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S326T
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S326V
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S326Y
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the mutant shows reduced activity toward D-glucose and increased activity with maltose compared to the wild type enzyme
S365A
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the mutant shows reduced activity toward D-glucose and increased activity with maltose compared to the wild type enzyme
S365C
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365D
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365E
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365F
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the mutant shows reduced activity toward D-glucose and increased activity with maltose compared to the wild type enzyme
S365G
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365H
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365I
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365K
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365L
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365M
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365N
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365P
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365Q
-
the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365R
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365T
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365V
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365W
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365Y
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the mutant shows reduced activity compared to the wild type enzyme; the mutant shows strongly reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365Y/S326E
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the mutant shows reduced activity compared to the wild type enzyme
S365Y/S326G
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the mutant shows reduced activity compared to the wild type enzyme
S365Y/S326H
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the mutant shows reduced activity compared to the wild type enzyme
S365Y/S326K
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the mutant shows reduced activity compared to the wild type enzyme
S365Y/S326Q
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the mutant shows reduced activity compared to the wild type enzyme
S365Y/S326R
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the mutant shows reduced activity compared to the wild type enzyme
S365Y/S326T
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the mutant shows reduced activity compared to the wild type enzyme
S365Y/S326V
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the mutant shows reduced activity compared to the wild type enzyme
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using 0.05 mM FAD,10% (v/v) glycerol,and 20 mM potassium phosphate buffer, pH 6.5
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
biofuel production
diagnostics
medicine
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use of the enzyme as an indicator of cellular immune response activation