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Information on EC 1.1.5.9 - glucose 1-dehydrogenase (FAD, quinone)
for references in articles please use BRENDA:EC1.1.5.9
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.5 With a quinone or similar compound as acceptor
1.1.5.9 glucose 1-dehydrogenase (FAD, quinone)
IUBMB Comments
A glycoprotein containing one mole of FAD per mole of enzyme. 2,6-Dichloroindophenol can act as acceptor. cf. EC 1.1.5.2, glucose 1-dehydrogenase (PQQ, quinone).
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 1.1.5.9
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electrode
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bioanode
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transfer-type
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bioelectrocatalytic
- glomerella
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fungi-derived
- analysis
- cingulata
- biofuel production
- diagnostics
- medicine
- biotechnology
showSynonyms
fad-gdh, fadgdh, fad-dependent glucose dehydrogenase, flavin adenine dinucleotide-dependent glucose dehydrogenase, thermostable glucose dehydrogenase, fad-glucose dehydrogenase, fad dependent glucose dehydrogenase, gdh-fad, flavin adenine dinucleotide dependent glucose dehydrogenase, fad-dependent gdh, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, glucose (acceptor)
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dehydrogenase, glucose (Aspergillus)
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EC 1.1.99.10
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formerly
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FAD glucose dehydrogenase
FAD-dependent GDH
FAD-dependent glucose dehydrogenase
FAD-GDH
FAD-glucose dehydrogenase
FAD-glucose dehydrogenases
FADGDH
flavin adenine dinucleotide dependent glucose dehydrogenase
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flavin adenine dinucleotide-dependent glucose dehydrogenase
GDH
GLD
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glucose dehydrogenase
glucose dehydrogenase (Aspergillus)
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glucose dehydrogenase (decarboxylating)
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thermostable glucose dehydrogenase
FAD-glucose dehydrogenase
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flavin adenine dinucleotide-dependent glucose dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glucose + a quinone = D-glucono-1,5-lactone + a quinol
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
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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, glucose 1-dehydrogenase (PQQ, quinone).
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CAS REGISTRY NUMBER
COMMENTARY
37250-84-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
2-deoxy-D-glucose + a quinone
2-deoxy-D-glucono-1,5-lactone + a quinol
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Substrates: -
Products: -
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?
alpha,alpha-trehalose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
Substrates: 0.5% activity compared to D-glucose
Products: -
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?
beta-D-glucose + Fe(CN)63-
D-glucono-1,5-lactone + Fe(CN)64-
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Substrates: -
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?
cellobiose + a quinone
? + a quinol
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Substrates: low activity
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?
D-galactose + 2,6-dichlorophenolindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
D-galactose + acceptor
D-galactono-1,5-lactone + reduced acceptor
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Substrates: 6.5% of the activity with D-glucose
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?
D-glucose + 1,2-naphthoquinone
D-glucono-1,5-lactone + 1,2-naphthoquinol
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Substrates: an electrochemical method is applied to evaluate the bimolecular rate constants of selected electron acceptors. With regard to the formal potential, higher kcat/Km values are found for ortho-quinones (including 9,10-phenanthrenequinone and 1,2-naphthoquinone) than for para-quinones in the reaction with FAD-GDH. Thus, the mechanism for effective electron transfer can be explained by steric hindrance (the electron transfer distance between the FAD site and the redox site of the quinone molecules)
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D-glucose + 1,4-naphthoquinone
D-glucono-1,5-lactone + 1,4-naphthoquinol
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Substrates: -
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D-glucose + 1,6-pyrenedione
D-glucono-1,5-lactone + 1,6-pyrenediol
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Substrates: the electro-oxidation of pyrene forms an efficient mediator for the enzyme (FAD-GDH) which surpasses currently used mediators like naphthoquinone in terms of electrocatalytic current densities and stability
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D-glucose + 1,8-pyrenedione
D-glucono-1,5-lactone + 1,8-pyrenediol
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Substrates: the electro-oxidation of pyrene forms an efficient mediator for the enzyme (FAD-GDH) which surpasses currently used mediators like naphthoquinone in terms of electrocatalytic current densities and stability
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D-glucose + 2,6-dichlorophenolindophenol
D-gluconic acid + reduced 2,6-dichlorophenolindophenol
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
D-glucose + 9,10-phenanthrenequinone
D-glucono-1,5-lactone + 9,10-phenanthrenequinol
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Substrates: an electrochemical method is applied to evaluate the bimolecular rate constants of selected electron acceptors. With regard to the formal potential, higher kcat/Km values are found for ortho-quinones (including 9,10-phenanthrenequinone and 1,2-naphthoquinone) than for para-quinones in the reaction with FAD-GDH. Thus, the mechanism for effective electron transfer can be explained by steric hindrance (the electron transfer distance between the FAD site and the redox site of the quinone molecules)
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D-glucose + acceptor
D-glucono-1,5-lactone + reduced acceptor
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Substrates: -
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D-glucose + coenzyme Q1
D-glucono-1,5-lactone + reduced coenzyme Q1
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Substrates: -
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D-glucose + ferricenium hexafluorophosphate
D-glucono-1,5-lactone + ferrocenium hexafluorophosphate
D-glucose + ferricenium ion
D-glucono-1,5-lactone + ferrocenium ion
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Substrates: -
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D-glucose + menadione
D-glucono-1,5-lactone + menadiol
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Substrates: -
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D-glucose + oxidized 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenol indophenol
D-glucose + tetramethyl-p-phenylenediamine
D-glucono-1,5-lactone + reduced tetramethyl-p-phenylenediamine
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Substrates: -
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D-lactose + 2,6-dichlorophenolindophenol
D-lactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: 0.6% activity compared to D-glucose
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?
D-maltose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
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Substrates: -
Products: -
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?
D-mannose + acceptor
D-manno-1,5-lactone + reduced acceptor
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Substrates: 8.6% of the activity with D-glucose
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?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
D-xylose + acceptor
D-xylono-1,5-lactone + reduced acceptor
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Substrates: 13% of the activity with D-glucose
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?
D-xylose + ferricenium ion
D-xylono-1,5-lactone + ferrocenium ion
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Substrates: -
Products: -
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?
D-xylose + oxidized 2,6-dichlorophenol indophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenol indophenol
fructose + 2,6-dichlorophenolindophenol
?
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Substrates: 8% of the activity with D-glucose
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glutamine + a quinone
? + a quinol
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Substrates: low activity
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L-arabinose + 2,6-dichlorophenolindophenol
L-arabinono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
L-arabinose + acceptor
L-arabinono-1,5-lactone + reduced acceptor
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Substrates: 2.8% of the activity with D-glucose
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?
L-rhamnose + acceptor
L-rhamnone-1,5-lactone + reduced acceptor
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Substrates: 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
maltose + 2,6-dichlorophenolindophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
maltose + acceptor
?
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Substrates: 3.2% of the activity with D-glucose
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maltotetraose + 2,6-dichlorophenolindophenol
maltotetraono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
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Substrates: 0.66% activity compared to D-glucose
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maltotriose + 2,6-dichlorophenolindophenol
maltotriono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
mannose + 2,6-dichlorophenolindophenol
mannono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
trehalose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
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Substrates: 0.22% activity compared to D-glucose
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?
2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: 11.5% activity compared to D-glucose
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?
2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: 11.5% activity compared to D-glucose
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?
2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
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Substrates: about 11% activity compared to D-glucose
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?
2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
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Substrates: about 8.4% activity compared to D-glucose
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2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
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Substrates: about 11% activity compared to D-glucose
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?
2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
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Substrates: about 11% activity compared to D-glucose
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2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: 60.1% activity compared to D-glucose
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2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: 60.1% activity compared to D-glucose
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D-galactose + 2,6-dichlorophenolindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: 2.2% activity compared to D-glucose
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?
D-galactose + 2,6-dichlorophenolindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: 2.2% activity compared to D-glucose
Products: -
Products: -
?
D-galactose + 2,6-dichlorophenolindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
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Substrates: 0.44% activity compared to D-glucose
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Products: -
?
D-galactose + 2,6-dichlorophenolindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Mucor circinelloides NISL0103
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Substrates: 0.44% activity compared to D-glucose
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Products: -
?
D-glucose + 1,4-benzoquinone
D-glucono-1,5-lactone + 1,4-benzoquinol
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Substrates: -
Products: -
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?
D-glucose + 1,4-benzoquinone
D-glucono-1,5-lactone + 1,4-benzoquinol
-
Substrates: -
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?
D-glucose + 2,6-dichlorophenolindophenol
D-gluconic acid + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
D-glucose + 2,6-dichlorophenolindophenol
D-gluconic acid + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
D-glucose + 2,6-dichlorophenolindophenol
D-gluconic acid + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
D-glucose + 2,6-dichlorophenolindophenol
D-gluconic acid + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
D-glucose + 2,6-dichlorophenolindophenol
D-gluconic acid + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
r
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: 100% activity
Products: -
Products: -
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
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?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
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?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
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Substrates: the enzyme has high specificity toward D-glucose
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D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Mucor circinelloides NISL0103
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Substrates: the enzyme has high specificity toward D-glucose
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D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: high substrate specificity for D-glucose
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D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: high substrate specificity for D-glucose
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D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
Substrates: 100% activity
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D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
Substrates: 100% activity
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D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
Substrates: 100% activity
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D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: high substrate specificity for D-glucose
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D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: high substrate specificity for D-glucose
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D-glucose + a quinone
D-glucono-1,5-lactone + a quinol
-
Substrates: -
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D-glucose + a quinone
D-glucono-1,5-lactone + a quinol
-
Substrates: -
Products: -
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D-glucose + a quinone
D-glucono-1,5-lactone + a quinol
-
Substrates: -
Products: -
Products: -
?
D-glucose + a quinone
D-glucono-1,5-lactone + a quinol
-
Substrates: -
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Products: -
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D-glucose + a quinone
D-glucono-1,5-lactone + a quinol
-
Substrates: -
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D-glucose + a quinone
D-glucono-1,5-lactone + a quinol
-
Substrates: -
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D-glucose + a quinone
D-glucono-1,5-lactone + a reduced quinol
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Substrates: -
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D-glucose + a quinone
D-glucono-1,5-lactone + a reduced quinol
-
Substrates: -
Products: -
Products: -
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D-glucose + ferricenium hexafluorophosphate
D-glucono-1,5-lactone + ferrocenium hexafluorophosphate
-
Substrates: -
Products: -
Products: -
?
D-glucose + ferricenium hexafluorophosphate
D-glucono-1,5-lactone + ferrocenium hexafluorophosphate
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Substrates: -
Products: -
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D-glucose + ferricyanide
D-glucono-1,5-lactone + ferrocyanide
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Substrates: -
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D-glucose + ferricyanide
D-glucono-1,5-lactone + ferrocyanide
-
Substrates: -
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D-glucose + ferricyanide
D-glucono-1,5-lactone + ferrocyanide
-
Substrates: -
Products: -
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D-glucose + oxidized 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenol indophenol
-
Substrates: with phenazine methosulfate
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D-glucose + oxidized 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenol indophenol
-
Substrates: with phenazine methosulfate
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D-glucose + oxidized 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenol indophenol
-
Substrates: -
Products: -
Products: -
?
D-glucose + oxidized 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenol indophenol
-
Substrates: -
Products: -
Products: -
?
D-glucose + oxidized 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenol indophenol
-
Substrates: -
Products: -
Products: -
?
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + reduced phenazine methosulfate
-
Substrates: -
Products: -
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D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + reduced phenazine methosulfate
-
Substrates: -
Products: -
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D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + reduced phenazine methosulfate
-
Substrates: -
Products: -
Products: -
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D-raffinose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
Substrates: about 3.2% activity compared to D-glucose
Products: -
Products: -
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D-raffinose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
Substrates: about 4.5% activity compared to D-glucose
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D-raffinose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
Substrates: about 3.2% activity compared to D-glucose
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Products: -
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D-raffinose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
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Substrates: about 3.2% activity compared to D-glucose
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Products: -
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D-xylose + 2,6-dichloroindophenol
D-xylono-1,5-lactone + 2,6-dichlorophenolindophenol
Substrates: 24.8% activity compared to D-glucose
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D-xylose + 2,6-dichloroindophenol
D-xylono-1,5-lactone + 2,6-dichlorophenolindophenol
Substrates: 24.8% activity compared to D-glucose
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D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: 17% activity compared to D-glucose
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D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
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Substrates: 1.8% activity compared to D-glucose
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D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: 7.4% activity compared to D-glucose
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Products: -
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: 7.4% activity compared to D-glucose
Products: -
Products: -
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
Substrates: 1.53% activity compared to D-glucose
Products: -
Products: -
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Mucor circinelloides NISL0103
-
Substrates: 1.53% activity compared to D-glucose
Products: -
Products: -
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
Substrates: about 50% activity compared to D-glucose
Products: -
Products: -
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
Substrates: about 40% activity compared to D-glucose
Products: -
Products: -
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
Substrates: about 50% activity compared to D-glucose
Products: -
Products: -
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
Substrates: about 50% activity compared to D-glucose
Products: -
Products: -
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: 27.6% activity compared to D-glucose
Products: -
Products: -
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: 27.6% activity compared to D-glucose
Products: -
Products: -
?
D-xylose + oxidized 2,6-dichlorophenol indophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenol indophenol
-
Substrates: with phenazine methosulfate
Products: -
Products: -
?
D-xylose + oxidized 2,6-dichlorophenol indophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenol indophenol
-
Substrates: with phenazine methosulfate
Products: -
Products: -
?
L-arabinose + 2,6-dichlorophenolindophenol
L-arabinono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: 1.5% activity compared to D-glucose
Products: -
Products: -
?
L-arabinose + 2,6-dichlorophenolindophenol
L-arabinono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: 1.5% activity compared to D-glucose
Products: -
Products: -
?
maltose + 2,6-dichlorophenol indophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
Substrates: 1.09% activity compared to D-glucose
Products: -
Products: -
?
maltose + 2,6-dichlorophenol indophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Mucor circinelloides NISL0103
-
Substrates: 1.09% activity compared to D-glucose
Products: -
Products: -
?
maltose + 2,6-dichlorophenolindophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: 17.7% activity compared to D-glucose
Products: -
Products: -
?
maltose + 2,6-dichlorophenolindophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: 17.7% activity compared to D-glucose
Products: -
Products: -
?
maltose + 2,6-dichlorophenolindophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
maltose + 2,6-dichlorophenolindophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
Substrates: about 11% activity compared to D-glucose
Products: -
Products: -
?
maltose + 2,6-dichlorophenolindophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
Substrates: about 21% activity compared to D-glucose
Products: -
Products: -
?
maltose + 2,6-dichlorophenolindophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
Substrates: about 11% activity compared to D-glucose
Products: -
Products: -
?
maltose + 2,6-dichlorophenolindophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
Substrates: about 11% activity compared to D-glucose
Products: -
Products: -
?
maltotriose + 2,6-dichlorophenolindophenol
maltotriono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
Substrates: 0.88% activity compared to D-glucose
Products: -
Products: -
?
maltotriose + 2,6-dichlorophenolindophenol
maltotriono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: 3.4% activity compared to D-glucose
Products: -
Products: -
?
maltotriose + 2,6-dichlorophenolindophenol
maltotriono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: 3.4% activity compared to D-glucose
Products: -
Products: -
?
maltotriose + 2,6-dichlorophenolindophenol
maltotriono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: 6.8% activity compared to D-glucose
Products: -
Products: -
?
maltotriose + 2,6-dichlorophenolindophenol
maltotriono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Substrates: 6.8% activity compared to D-glucose
Products: -
Products: -
?
mannose + 2,6-dichlorophenolindophenol
mannono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
Substrates: 0.66% activity compared to D-glucose
Products: -
Products: -
?
mannose + 2,6-dichlorophenolindophenol
mannono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
Mucor circinelloides NISL0103
-
Substrates: 0.66% activity compared to D-glucose
Products: -
Products: -
?
additional information
?
-
Substrates: less than 1% activity with D-mannose, D-maltose, D-galactose, D-allose, D-lactose, D-fructose, sucrose, and cellobiose
Products: -
Products: -
?
additional information
?
-
-
Substrates: less than 1% activity with maltose, cellobiose, lactose, mannose, fructose, allose, galactose, and sucrose
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate sppecificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate sppecificity, overview
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with D-fructose, S-sorbitol, and D-sucrose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with D-fructose, S-sorbitol, and D-sucrose
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, overview. Lactose, gluconic acid, mannose, mannitol, sorbitol, galactose, sucrose, maltose, arabinose, xylitol, rhamnose, fucose, trehalose, and fructose are poor or no substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: suitable electron acceptors are quinones, phenoxy radicals, 2,6-dichloroindophenol, ferricyanide and ferrocenium hexafluorophosphate. Reduction of quinones and phenoxy radicals by extracellular enzyme, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme participates in strengthening the encapsulation and in killing reaction, via reaction with quinones generated by phenolidase and subsequent production of free radicals
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme participates in the immune reaction by donating electrons during regeneration of its cofactor FAD. The enzyme is required for the generation of reactive oxygen species by hemocytes at the encapsulation site. The enzyme activity increases immediately at post-oviposition and post-injection of purified polyDNA viruses
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with sucrose
Products: -
Products: -
?
additional information
?
-
Substrates: no activity in the presence of maltose, D-arabinose, D-fructose, D-galactose, maltotetraose, D-mannitol, D-mannose, D-raffinose, D-sorbitol, sucrose, and D-trehalose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity in the presence of maltose, D-arabinose, D-fructose, D-galactose, maltotetraose, D-mannitol, D-mannose, D-raffinose, D-sorbitol, sucrose, and D-trehalose
Products: -
Products: -
?
additional information
?
-
Substrates: no activity in the presence of maltose, D-arabinose, D-fructose, D-galactose, maltotetraose, D-mannitol, D-mannose, D-raffinose, D-sorbitol, sucrose, and D-trehalose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with D-arabinose, D-cellobiose, D-fructose, D-galactose, lactitol, maltitol, D-mannitol, D-mannose, D-sorbitol, sucrose, and D-trehalose
Products: -
Products: -
?
additional information
?
-
Substrates: no activity in the presence of maltose, D-arabinose, D-fructose, D-galactose, maltotetraose, D-mannitol, D-mannose, D-raffinose, D-sorbitol, sucrose, and D-trehalose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity in the presence of maltose, D-arabinose, D-fructose, D-galactose, maltotetraose, D-mannitol, D-mannose, D-raffinose, D-sorbitol, sucrose, and D-trehalose
Products: -
Products: -
?
additional information
?
-
Substrates: no activity in the presence of maltose, D-arabinose, D-fructose, D-galactose, maltotetraose, D-mannitol, D-mannose, D-raffinose, D-sorbitol, sucrose, and D-trehalose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity in the presence of maltose, D-arabinose, D-fructose, D-galactose, maltotetraose, D-mannitol, D-mannose, D-raffinose, D-sorbitol, sucrose, and D-trehalose
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-glucose + a quinone
D-glucono-1,5-lactone + a quinol
-
Substrates: -
Products: -
Products: -
?
D-glucose + a quinone
D-glucono-1,5-lactone + a quinol
-
Substrates: -
Products: -
Products: -
?
D-glucose + a quinone
D-glucono-1,5-lactone + a quinol
-
Substrates: -
Products: -
Products: -
?
D-glucose + a quinone
D-glucono-1,5-lactone + a quinol
-
Substrates: -
Products: -
Products: -
?
D-glucose + a quinone
D-glucono-1,5-lactone + a quinol
-
Substrates: -
Products: -
Products: -
?
D-glucose + a quinone
D-glucono-1,5-lactone + a quinol
-
Substrates: -
Products: -
Products: -
?
D-glucose + a quinone
D-glucono-1,5-lactone + a reduced quinol
-
Substrates: -
Products: -
Products: -
?
D-glucose + a quinone
D-glucono-1,5-lactone + a reduced quinol
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme participates in strengthening the encapsulation and in killing reaction, via reaction with quinones generated by phenolidase and subsequent production of free radicals
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme participates in the immune reaction by donating electrons during regeneration of its cofactor FAD. The enzyme is required for the generation of reactive oxygen species by hemocytes at the encapsulation site. The enzyme activity increases immediately at post-oviposition and post-injection of purified polyDNA viruses
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-benzoquinone
-
competitive inhibition of the activity with 2,6-dichlorophenolindophenol or coenzyme Q1, non-competitive inhibition of reaction with phenazine methosulfate
Urea
-
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%
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.97
D-glucose
-
wild type enzyme, at pH 7.0, temperature not specified in the publication
0.99
D-glucose
-
mutant enzyme C213S, at pH 7.0, temperature not specified in the publication
1.3
D-glucose
-
at 40°C after preincubation of the enzyme at 70°C for 30 min
2.8
D-glucose
pH 7.0, 37°C, glycosylated recombinant protein
3.09
D-glucose
-
pH 7.4, 37°C, enzyme immobilized on amperometric electrode
4.6
D-glucose
pH 7.0, 37°C, unglycosylated recombinant protein
6.3
D-glucose
-
reaction with phenazine methosulfate/2,6-dichlorophenolindophenol at pH 8.75
17
D-glucose
-
A472F mutant, higher specificity toward glucose compared to the wild type enzyme, no activity towards maltose
28
D-glucose
-
N475D mutant, higher specificity toward glucose compared to the wild type enzyme, no activity towards maltose
406
D-glucose
pH 7.0, 37°C, unglycosylated recombinant protein
2.7
phenazine methosulfate
-
at 40°C after preincubation of the enzyme at 70°C for 30 min
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
749.7
D-glucose
-
recombinant enzyme, apparent value, at pH 7.0 and 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
430
-
enzymatic activity of wild-type FADGDH in an assay with 40 mM maltose
565
-
purified enzyme with ferrocenium hexafluorophosphate, pH 5.5, 30°C
836
840
-
purified enzyme with 2,6-dichlorophenol indophenol , pH 5.5, 30°C
950
-
enzymatic activity of wild-type FADGDH in an assay with 40 mM glucose
additional information
836
-
purified recombinant enzyme expressed from Pichia pastoris, pH 7.5, 30°C
additional information
-
590 micromol/min/mg Vmax for the FADGDH mutant A472F
additional information
-
770 micromol/min/mg Vmax for the FADGDH mutant N475D
additional information
-
290 micromol/min/mg Vmax of oxidation of glucose at 40°C
additional information
-
470 micromol/min/mg Vmax of oxidation of phenazine methosulfate at 40°C
additional information
-
66 micromol/min/mg Vmax of oxidation of glucose at 40°C after preincubation of the enzyme at 70°C for 30 min
additional information
-
4.3 micromol/min/mg Vmax of oxidation of phenazine methosulfate at 40°C after preincubation of the enzyme at 70°C for 30 min
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
-
assay at with 2,6-dichlorophenol indophenol or ferrocenium hexafluorophosphate
6.5
7.4
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
70
45
-
enzyme activity shows a second peak at 70°C with 30% of maximal activity
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 85
-
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
-
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 - 60
-
30°C: about 45% of maximal activity, 60°C: about 25% of maximal activity, native enzyme
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
40 - 80
-
40°C: about 45% of maximal activity, 80°C: about 45% of maximal activity, glucose dehydrogenase cross-linked with glutaraldehyde
40 - 85
-
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
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bacterial strain SM4 is used, isolated from a soil sample near a Japanese hot spring
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
signal peptide consists of residues Met1 to Ala17
-
brenda
-
signal peptide consists of residues Met1 to Ala17
-
-
brenda
signal peptide consists of residues Met1 to Ala16
-
brenda
-
signal peptide consists of residues Met1 to Ala16
-
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
-
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
evolution
-
the enzyme belongs to the to the GMC family of oxidoreductases, phylogenetic analysis
evolution
-
the enzyme belongs to the to the GMC family of oxidoreductases, phylogenetic analysis
-
physiological function
-
the enzyme from Glomerella cingulata might play a role in plant pathogenicity. The quinone and phenoxy radical reducing enzyme light act to neutralize the action of plant laccase, phenoloxidase or peroxidase activities, which are increased in infected plants to evade fungal attack
physiological function
-
the enzyme from Glomerella cingulata might play a role in plant pathogenicity. The quinone and phenoxy radical reducing enzyme light act to neutralize the action of plant laccase, phenoloxidase or peroxidase activities, which are increased in infected plants to evade fungal attack
-
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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). DHGL_DROPS
625
0
68599
Swiss-Prot
-
B8MX95_ASPFN
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167)
593
0
63665
TrEMBL
-
Q0CDD9_ASPTN
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
591
0
64446
TrEMBL
-
Q8GQE7_BURCE
539
0
59832
TrEMBL
Chloroplast (Reliability: 5)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
13000
-
SDS-PAGE, X * 60000 (alpha-subunit), x * 40000 (beta-subunit), x * 18000 (gamma-subunit), x * 13000 (gamma-subunit)
18000
40000
-
SDS-PAGE, X * 60000 (alpha-subunit), x * 40000 (beta-subunit), x * 18000 (gamma-subunit), x * 13000 (gamma-subunit)
43000
60000
67000
86000
-
calculation from titration of the prosthetic group with glucose
87000
-
1 * 87000, monomeric in presence of 1% Triton X-100, aggregation after removing the detergent, urea-SDS-PAGE
95000 - 135000
18000
-
SDS-PAGE, X * 60000 (alpha-subunit), x * 40000 (beta-subunit), x * 18000 (gamma-subunit), x * 13000 (gamma-subunit)
43000
-
after preincubation at temperatures below 45°C: x * 67000 (alpha-subunit) x * 43000 (beta subunit), SDS-PAGE
43000
-
SDS-PAGE, x * 67000, alpha-subunit, x * 43000, beta subunit, determined as cytochrome c via spectroscopic analyses
60000
-
SDS-PAGE, X * 60000 (alpha-subunit), x * 40000 (beta-subunit), x * 18000 (gamma-subunit), x * 13000 (gamma-subunit)
67000
-
after preincubation at 70°C for 30 min: x * 67000 (alpha-subunit), SDS-PAGE
67000
-
after preincubation at temperatures below 45°C: x * 67000 (alpha-subunit) x * 43000 (beta subunit), SDS-PAGE
67000
-
SDS-PAGE, x * 67000, alpha-subunit, x * 43000, beta subunit, determined as cytochrome c via spectroscopic analyses
67000
-
x * 67000, deglycosylated recombinant enzyme expressed from Pichia pastoris, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heteromer
homooligomer
-
after preincubation at 70°C for 30 min: x * 67000 (alpha-subunit), SDS-PAGE
monomer
additional information
-
aggregation in medium containing no Triton X-100 to dimers, trimers and tetramers
?
-
x * 67000, deglycosylated recombinant enzyme expressed from Pichia pastoris, SDS-PAGE
?
60000, recombinant protein expressed in Escherichia coli, 90000-150000, expressed in Pichia pastoris, 110000-250000, expressed in Saccharomyces cerevisiae, respectively, SDS-PAGE. Recombinant proteins have different glycoforms
heteromer
-
after preincubation at temperatures below 45°C: x * 67000 (alpha-subunit) x * 43000 (beta subunit), SDS-PAGE
heteromer
-
SDS-PAGE, x * 67000, alpha-subunit, x * 43000, beta subunit, determined as cytochrome c via spectroscopic analyses
heteromer
-
SDS-PAGE, X * 60000 (alpha-subunit), x * 40000 (beta-subunit), x * 18000 (gamma-subunit), x * 13000 (gamma-subunit)
heteromer
-
SDS-PAGE, X * 60000 (alpha-subunit), x * 40000 (beta-subunit), x * 18000 (gamma-subunit), x * 13000 (gamma-subunit)
-
monomer
-
1 * 87000, monomeric in presence of 1% Triton X-100, aggregation after removing the detergent, urea-SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
contains 24% carbohydrate consisting of glucose, mannose and hexosamines
glycoprotein
-
four potential N-glycosylation sites at N55, N233, N255 and N339
glycoprotein
-
four potential N-glycosylation sites at N55, N233, N255 and N339
-
glycoprotein
recombinant proteins have different glycoforms. Molecluar mass is 60000, recombinant protein expressed in Escherichia coli, i.e. unglycosylated, 90000-150000, expressed in Pichia pastoris, 110000-250000, expressed in Saccharomyces cerevisiae, respectively
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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
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
-
A472F
N475D
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
-
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
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
A472F
-
mutant with higher substrate specificity for glucose in relation to maltose, constructed by site-directed mutagenesis
N475D
-
mutant with higher substrate specificity for glucose in relation to maltose, constructed by site-directed mutagenesis
S365Y
-
the mutant shows reduced activity compared to the wild type enzyme
S365Y
-
the mutant shows strongly reduced activity toward D-glucose and maltose compared to the wild type enzyme
additional information
-
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
additional information
-
the FAD-dependent glucose dehydrogenase is evaluated electrochemically connected to an osmium redox polymer [Os(4,4'-dimethyl-2,2'-bipyridine)2 (PVI)10Cl]+ on graphite electrode for possible use in glucose-based biosensors and biofuel cells, method and sensitivity, overview
additional information
-
the purified recombinnat enzyme is used as an anode catalyst for enzyme fuel cells, method, overview. The recombinant FAD-GDH is able to maintain its native glucose affinity during immobilization in the carbon nanotube and operation of enzyme fuel cells. Heterogeneous electron transfer coefficient of FAD-GDHmenadione on a glassy carbon electrode was 10.73/s
additional information
-
the FAD-dependent glucose dehydrogenase is evaluated electrochemically connected to an osmium redox polymer [Os(4,4'-dimethyl-2,2'-bipyridine)2 (PVI)10Cl]+ on graphite electrode for possible use in glucose-based biosensors and biofuel cells, method and sensitivity, overview
additional information
-
glucose-oxidizing properties of the enzyme on spectrographic graphite electrodes and as a recognition element in glucose biosensors, immobilization on spectrographic graphite electrode's surface, method, overiew. The ratio of GcGDH/Os polymer and the overall loading of the enzyme electrode significantly affect the performance of the enzyme electrode for glucose oxidation. Best suited matiral is osmium redox polymer [Os(4,4'-dimethyl-2,2'-bipyridine)2 (PVI)10Cl]+, evaluation of different Os polymers, coupled assay method with glucose oxidase, EC 1.1.3.4,overview
additional information
-
the FAD-dependent glucose dehydrogenase is evaluated electrochemically connected to an osmium redox polymer [Os(4,4'-dimethyl-2,2'-bipyridine)2 (PVI)10Cl]+ on graphite electrode for possible use in glucose-based biosensors and biofuel cells, method and sensitivity, overview
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 9
5
-
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
5 - 5.8
-
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 40
-
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
40 - 60
-
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
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
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
5 - 70
-
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
-
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
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
60
65
-
half-life of native enzyme: 2.5 min, half life of enzyme cross-linked to glutaraldehyde: 72 min
60
the enzyme displays very high thermal stability with a half-life of 82 min at 60°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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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
-
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
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 Pichia pastoris strain X-33 5.1fold by hydrophobic interaction and anion exchange chromatography
-
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
-
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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 in Escherichia coli and Pichia pastoris
expressed in Escherichia coli strain BLR(DE3) and Pichia pastoris strain GS115
-
expression in Escherichia coli strain BL21RIL, no GDH activity when cells expressing the alpha-subunit alone
-
expression in Escherichia coli, Pichia pastoris and Saccharomyces cerevisiae
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
-
DNA and amino acid sequence determination and analysis, phylogenetic tree, recombinant expression in Escherichia coli strain BL21 (DE3)
-
DNA and amino acid sequence determination and analysis, phylogenetic tree, recombinant expression in Escherichia coli strain BL21 (DE3)
-
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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
LITERATURE
analysis
biofuel production
biotechnology
construction of a direct electron transfer bioanode composed of FADGDH and a single-walled carbon nanotube. The bioanode exhibits a large anodic current due to the enzymatic reaction (1 mA/cm) at ambient temperature and works at 70°C for 12 h
diagnostics
medicine
-
use of the enzyme as an indicator of cellular immune response activation
analysis
-
possible use of the enzyme as amperometric glucose biosensor
analysis
-
possible use of the enzyme as amperometric glucose biosensor
analysis
-
the enzyme can be used as O2-independent biosensor for glucoe detection
biofuel production
-
a glucose biofuel cell anode, in which the aminoferrocene and FAD-GDH-immobilized MgO-templated porous carbon is coated on a carbon cloth, is constructed. The anode is combined with bilirubin oxidase and a 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)-immobilized biocathode
biofuel production
-
synthesis of a naphthoquinone-functionalized redox polymer that is used to immobilize and electronically communicate with flavin adenine dinucleotide-dependent glucose dehydrogenase, yielding an enzymatic bioanode that is able to deliver large catalytic current densities for glucose oxidation at a relatively low associated potential
diagnostics
-
the enzyme can be used as O2-independent biosensor for glucoe detection
diagnostics
-
an oxygen insensitive glucose biosensor is developed which comprises FAD-dependent glucose dehydrogenase, dichlorophenol indophenol or 2,3-dichloro-naphthoquinone as redox mediators and polydopamine as a constraining layer. It shows long term bioelectrocatalytic activity for at least 3 days without any additional coating or treatment. The system shows great reproducibility, as well as an easy fabrication methodology that should allow low-cost manufacturing
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bak, T.G.
Studies on glucose dehydrogenase of Aspergillus oryzae. II. Purification and physical and chemical properties
Biochim. Biophys. Acta
139
277-293
1967
Aspergillus oryzae
brenda
Mller, H.M.
Gluconic acid forming enzymes in Aspergillus niger
Zentralbl. Bakteriol. Parasitenkd. Infektionskr. Hyg.
132
14-24
1977
Aspergillus niger
brenda
Matsushita, K.; Ohno, Y.; Shinagawa, E.; Adachi, O.; Ameyama, M.
Gluconsure bildende Enzyme bei Aspergillus niger
Agric. Biol. Chem.
44
1505-1512
1980
Pseudomonas sp.
-
brenda
Hauge, J.G.
Glucose dehydrogenase of Bacterium anitratum: an enzyme with a novel prosthetic group
J. Biol. Chem.
239
3630-3639
1964
Acinetobacter baumannii
brenda
Cox-Foster, D.L.; Stehr, J.E.
Induction of localization of FAD-glucose dehydrogenase (GLD) during encapsulation of abiotic implants in Manduca sexta larvae
J. Insect Physiol.
40
235-249
1994
Manduca sexta
-
brenda
Lovallo, N.; Cox-Foster, D.L.
Alteration in FAD-glucose dehydrogenase activity and hemocyte behavior contribute to initial disruption of Manduca sexta immune response to Cotesia congregata parasitoids
J. Insect Physiol.
45
1037-1048
1999
Manduca sexta
brenda
Yamazaki, T.; Tsugawa, W.; Sode, K.
Increased thermal stability of glucose dehydrogenase by cross-linking chemical modification
Biotechnol. Lett.
21
199-202
1999
Bacteria
-
brenda
Tsujimura, S.; Kojima, S.; Kano, K.; Ikeda, T.; Sato, M.; Sanada, H.; Omura, H.
Novel FAD-dependent glucose dehydrogenase for a dioxygen-insensitive glucose biosensor
Biosci. Biotechnol. Biochem.
70
654-659
2006
Aspergillus terreus
brenda
Yamaoka, H.; Yamashita, Y.; Ferri, S.; Sode, K.
Site directed mutagenesis studies of FAD-dependent glucose dehydrogenase catalytic subunit of Burkholderia cepacia
Biotechnol. Lett.
30
1967-1972
2008
Burkholderia cepacia
brenda
Yamazaki, T.; Tsugawa, W.; Sode, K.
Subunit Analyses of a Novel Thermostable Glucose Dehydrogenase Showing Different Temperature Properties According to Its Quaternary Structure
Appl. Biochem. Biotechnol.
77-79
325-335
1999
Burkholderia cepacia
-
brenda
Yamaoka, H.; Ferri, S.; Fujikawa, M.; Sode, K.
Essential role of the small subunit of thermostable glucose dehydrogenase from Burkholderia cepacia
Biotechnol. Lett.
26
1757-1761
2004
Burkholderia cepacia, Burkholderia cepacia SM4
brenda
Okuda-Shimazaki, J.; Kakehi, N.; Yamazaki, T.; Tomiyama, M.; Sode, K.
Biofuel cell system employing thermostable glucose dehydrogenase
Biotechnol. Lett.
30
1753-1758
2008
Burkholderia cepacia, Burkholderia cepacia SM4
brenda
Sode, K.; Tsugawa, W.; Yamazaki, T.; Watanabe, M.; Ogasawara, N.; Tanaka, M.
A novel thermostable glucose dehydrogenase varying temperature properties by altering its quaternary structures
Enzyme Microb. Technol.
19
82-85
1996
Burkholderia cepacia
-
brenda
Zafar, M.N.; Beden, N.; Leech, D.; Sygmund, C.; Ludwig, R.; Gorton, L.
Characterization of different FAD-dependent glucose dehydrogenases for possible use in glucose-based biosensors and biofuel cells
Anal. Bioanal. Chem.
402
2069-2077
2012
Colletotrichum gloeosporioides, Komagataella pastoris, Aspergillus sp.
brenda
Zafar, M.N.; Wang, X.; Sygmund, C.; Ludwig, R.; Leech, D.; Gorton, L.
Electron-transfer studies with a new flavin adenine dinucleotide dependent glucose dehydrogenase and osmium polymers of different redox potentials
Anal. Chem.
84
334-341
2012
Colletotrichum gloeosporioides
brenda
Mori, K.; Nakajima, M.; Kojima, K.; Murakami, K.; Ferri, S.; Sode, K.
Screening of Aspergillus-derived FAD-glucose dehydrogenases from fungal genome database
Biotechnol. Lett.
33
2255-2263
2011
Aspergillus oryzae, Aspergillus terreus
brenda
Monosik, R.; Stredansky, M.; Luspai, K.; Magdolen, P.; Sturdik, E.
Amperometric glucose biosensor utilizing FAD-dependent glucose dehydrogenase immobilized on nanocomposite electrode
Enzyme Microb. Technol.
50
227-232
2012
Aspergillus oryzae
brenda
Sygmund, C.; Staudigl, P.; Klausberger, M.; Pinotsis, N.; Djinovic-Carugo, K.; Gorton, L.; Haltrich, D.; Ludwig, R.
Heterologous overexpression of Glomerella cingulata FAD-dependent glucose dehydrogenase in Escherichia coli and Pichia pastoris
Microb. Cell Fact.
10
106
2011
Colletotrichum gloeosporioides
brenda
Sygmund, C.; Klausberger, M.; Felice, A.K.; Ludwig, R.
Reduction of quinones and phenoxy radicals by extracellular glucose dehydrogenase from Glomerella cingulata suggests a role in plant pathogenicity
Microbiology
157
3203-3212
2011
Colletotrichum gloeosporioides, Colletotrichum gloeosporioides DSM 62728
brenda
Fapyane, D.; Lee, S.J.; Kang, S.H.; Lim, D.H.; Cho, K.K.; Nam, T.H.; Ahn, J.P.; Ahn, J.H.; Kim, S.W.; Chang, I.S.
High performance enzyme fuel cells using a genetically expressed FAD-dependent glucose dehydrogenase alpha-subunit of Burkholderia cepacia immobilized in a carbon nanotube electrode for low glucose conditions
Phys. Chem. Chem. Phys.
15
9508-9512
2013
Burkholderia cepacia
brenda
Komori, H.; Inaka, K.; Furubayashi, N.; Honda, M.; Higuchi, Y.
Crystallographic analysis of FAD-dependent glucose dehydrogenase
Acta Crystallogr. Sect. F
71
1017-1019
2015
Aspergillus terreus
brenda
Ozawa, K.; Iwasa, H.; Sasaki, N.; Kinoshita, N.; Hiratsuka, A.; Yokoyama, K.
Identification and characterization of thermostable glucose dehydrogenases from thermophilic filamentous fungi
Appl. Microbiol. Biotechnol.
101
173-183
2017
Rasamsonia emersonii (A0A1E1GL61), Rasamsonia emersonii, Thermoascus crustaceus (A0A1E1GL87), Thermoascus crustaceus, Rasamsonia emersonii NBRC 31232 (A0A1E1GL61), Thermoascus crustaceus NBRC 9129 (A0A1E1GL87), Thermoascus crustaceus NBRC 9129
brenda
Shiota, M.; Yamazaki, T.; Yoshimatsu, K.; Kojima, K.; Tsugawa, W.; Ferri, S.; Sode, K.
An Fe-S cluster in the conserved Cys-rich region in the catalytic subunit of FAD-dependent dehydrogenase complexes
Bioelectrochemistry
112
178-183
2016
Burkholderia cepacia
brenda
Sode, K.; Loew, N.; Ohnishi, Y.; Tsuruta, H.; Mori, K.; Kojima, K.; Tsugawa, W.; LaBelle, J.T.; Klonoff, D.C.
Novel fungal FAD glucose dehydrogenase derived from Aspergillus niger for glucose enzyme sensor strips
Biosens. Bioelectron.
87
305-311
2017
Aspergillus niger
brenda
Sakai, G.; Kojima, K.; Mori, K.; Oonishi, Y.; Sode, K.
Stabilization of fungi-derived recombinant FAD-dependent glucose dehydrogenase by introducing a disulfide bond
Biotechnol. Lett.
37
1091-1099
2015
Aspergillus flavus (B8MX95)
brenda
Iwasa, H.; Ozawa, K.; Sasaki, N.; Kinoshita, N.; Hiratsuka, A.; Yokoyama, K.
Thermostable FAD-dependent glucose dehydrogenases from thermophilic filamentous fungus Thermoascus aurantiacus
Electrochemistry
84
342-348
2016
Thermoascus aurantiacus, Thermoascus aurantiacus NBRC 6766, Thermoascus aurantiacus NBRC 9748
-
brenda
Yamashita, Y.; Ferri, S.; Huynh, M.L.; Shimizu, H.; Yamaoka, H.; Sode, K.
Direct electron transfer type disposable sensor strip for glucose sensing employing an engineered FAD glucose dehydrogenase
Enzyme Microb. Technol.
52
123-128
2013
Burkholderia cepacia
brenda
Satake, R.; Ichiyanagi, A.; Ichikawa, K.; Hirokawa, K.; Araki, Y.; Yoshimura, T.; Gomi, K.
Novel glucose dehydrogenase from Mucor prainii: Purification, characterization, molecular cloning and gene expression in Aspergillus sojae
J. Biosci. Bioeng.
120
498-503
2015
Mucor circinelloides, Mucor circinelloides NISL0103
brenda
Yang, Y.; Huang, L.; Wang, J.; Wang, X.; Xu, Z.
Efficient expression, purification, and characterization of a novel FAD-dependent glucose dehydrogenase from Aspergillus terreus in Pichia pastoris
J. Microbiol. Biotechnol.
24
1516-1524
2014
Aspergillus terreus (Q0CDD9), Aspergillus terreus, Aspergillus terreus NIH2624 (Q0CDD9), Aspergillus terreus NIH2624
brenda
Yoshida, H.; Sakai, G.; Mori, K.; Kojima, K.; Kamitori, S.; Sode, K.
Structural analysis of fungus-derived FAD glucose dehydrogenase
Sci. Rep.
5
13498
2015
Aspergillus flavus (B8MX95), Aspergillus flavus, Aspergillus flavus ATCC 200026 (B8MX95)
brenda
Iwasa, H.; Hiratsuka, A.; Yokoyama, K.; Uzawa, H.; Orihara, K.; Muguruma, H.
Thermophilic Talaromyces emersonii flavin adenine dinucleotide-dependent glucose dehydrogenase bioanode for biosensor and biofuel cell applications
ACS Omega
2
1660-1665
2017
Rasamsonia emersonii (A0A1E1GL61)
-
brenda
Blanchard, P.; Buzzetti, P.; Davies, B.; Nedellec, Y.; Girotto, E.; Gross, A.; Le Goff, A.; Nishina, Y.; Cosnier, S.; Holzinger, M.
Electrosynthesis of pyrenediones on carbon nanotube electrodes for efficient electron transfer with FAD-dependent glucose dehydrogenase in biofuel cell anodes
ChemElectroChem
6
5242-5247
2019
Aspergillus sp.
-
brenda
Cohen, R.; Cohen, Y.; Mukha, D.; Yehezkeli, O.
Oxygen insensitive amperometric glucose biosensor based on FAD dependent glucose dehydrogenase co-entrapped with DCPIP or DCNQ in a polydopamine layer
Electrochim. Acta
367
137477
2021
Aspergillus sp.
-
brenda
Tsuruoka, N.; Sadakane, T.; Hayashi, R.; Tsujimura, S.
Bimolecular rate constants for FAD-dependent glucose dehydrogenase from Aspergillus terreus and organic electron Acceptors
Int. J. Mol. Sci.
18
604
2017
Aspergillus terreus
brenda
Suzuki, R.; Shitanda, I.; Aikawa, T.; Tojo, T.; Kondo, T.; Tsujimura, S.; Itagaki, M.; Yuasa, M.
Wearable glucose/oxygen biofuel cell fabricated using modified aminoferrocene and flavin adenine dinucleotide-dependent glucose dehydrogenase on poly(glycidyl methacrylate)-grafted MgO-templated carbon
J. Power Sources
479
228807
2020
Aspergillus oryzae
-
brenda
Milton, R.
FAD-dependent glucose dehydrogenase immobilization and mediation within a Naphthoquinone redox polymer
Methods Mol. Biol.
1504
193-202
2017
Aspergillus sp.
brenda
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