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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-
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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
-
-
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
-
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
-
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
-
-
?
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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-
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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 75C after preincubation of the enzyme at 70C 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, 30C
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, 30C
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 70C for 30 min
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 85
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20% of maximal activity at 20C and 10% of maximal activity at 85C, maximal activity is at 45C with a second activity peak at 70C (30% of maximal activity)
25 - 50
Mucor prainii
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about 70% activity at 25C, about 90% activity at 30C, about 95% activity at 35C, 100% activity at 40C, about 65% activity at 45C, less than 20% activity at 50C
30 - 65
about 70% activity at 30C, about 80% activity at 35C, about 90% activity at 45C, about 95% activity at 50C, 100% activity at 55C, about 98% activity at 60C, about 85% activity at 65C
30 - 60
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30C: about 45% of maximal activity, 60C: about 25% of maximal activity, native enzyme
40 - 80
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40C: about 45% of maximal activity, 80C: about 45% of maximal activity, glucose dehydrogenase cross-linked with glutaraldehyde
40 - 85
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after preincubation of the enzyme at 70C for 30 min: 15% of maximal activity at 40C and 50% of maximal activity at 85C, maximal activity at 75C
50 - 80
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after preincubation with 5.8 M urea for 30 min at 25C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6
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isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
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 70C 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 70C 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 2225% (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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30C, 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 56C 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 40C for 15 min at pH 5.0. Treatment at 25C for 16 h shows that the enzyme is stable from pH 3.5 to 7.0
740778
6 - 8
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30C, 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 5-37C for 30 min, after incubating enzyme at 45C for 30 min 40% of enzyme activity remains, at 70C for 30 min 10% of enzyme activity remains
5 - 75
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after preincubation at 70C for 30 min the enzyme is stable at temperatures between 5-50C for 30 min, after incubating enzyme at 70C for 30 min 70% of activity remains
25 - 40
Mucor prainii
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the enzyme remains stable after 15 min at 25-40C, then activity drops to about 70% at 50C and is completely lost at 55C
30
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15 min, stable
40 - 70
after heat treatment at 40-70C for 15 min, unglycosylated enzyme maintains nearly 100% activity at temperatures up to 45C, but completely loses activity at 60C, while glycosylated enzyme displays high thermostability, maintaining 89% activity at 60C. The melting temperature of the glycosylated enzyme is 66.4C
40 - 60
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after heat treatment at 40-60C for 15 min, the enzyme maintains its activity close to 100%
40 - 62
unglycosylated enzym e is stable at temperatures up to 45C , while glycosylatedenzyme maintains 75% activity at 60C. The melting temperature of the glycosylated enzyme is 62.5C
45
-
the wild type enzyme is inactivated rapidly at 45C, 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 56C 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
-18C, 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
-
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
-
expressed in Escherichia coli strain BLR(DE3) and Pichia pastoris strain GS115
-
expressed in Escherichia coli strain Origami2 (DE3)
-
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 45C, 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
-
site directed mutagenesis
N475I
-
site directed mutagenesis
N475K
-
site directed mutagenesis
N475L
-
site directed mutagenesis
N475M
-
site directed mutagenesis
N475P
-
site directed mutagenesis
N475Q
-
site directed mutagenesis
N475R
-
site directed mutagenesis
N475S
-
site directed mutagenesis
N475T
-
site directed mutagenesis
N475V
-
site directed mutagenesis
N475W
-
site directed mutagenesis
N475Y
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site directed mutagenesis
S326C
-
the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S326E
-
the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S326G
-
the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S326H
-
the mutant shows reduced activity toward D-glucose and increased activity with maltose compared to the wild type enzyme
S326K
-
the mutant shows increased activity toward D-glucose compared to the wild type enzyme
S326Q
-
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
-
the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S326T
-
the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S326V
-
the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S326Y
-
the mutant shows reduced activity toward D-glucose and increased activity with maltose compared to the wild type enzyme
S365A
-
the mutant shows reduced activity toward D-glucose and increased activity with maltose compared to the wild type enzyme
S365C
-
the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365D
-
the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365E
-
the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365F
-
the mutant shows reduced activity toward D-glucose and increased activity with maltose compared to the wild type enzyme
S365G
-
the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365H
-
the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365I
-
the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365K
-
the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365L
-
the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365M
-
the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365N
-
the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365P
-
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
-
the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365T
-
the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365V
-
the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365W
-
the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365Y
-
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
-
the mutant shows reduced activity compared to the wild type enzyme
S365Y/S326G
-
the mutant shows reduced activity compared to the wild type enzyme
S365Y/S326H
-
the mutant shows reduced activity compared to the wild type enzyme
S365Y/S326K
-
the mutant shows reduced activity compared to the wild type enzyme
S365Y/S326Q
-
the mutant shows reduced activity compared to the wild type enzyme
S365Y/S326R
-
the mutant shows reduced activity compared to the wild type enzyme
S365Y/S326T
-
the mutant shows reduced activity compared to the wild type enzyme
S365Y/S326V
-
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
-
use of the enzyme as an indicator of cellular immune response activation