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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
-
-
-
-
?
alpha,alpha-trehalose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
0.5% activity compared to D-glucose
-
-
?
beta-D-glucose + Fe(CN)63-
D-glucono-1,5-lactone + Fe(CN)64-
-
-
-
-
?
cellobiose + a quinone
? + a quinol
-
low activity
-
-
?
D-galactose + 2,6-dichlorophenolindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
D-galactose + acceptor
D-galactono-1,5-lactone + reduced acceptor
-
6.5% of the activity with D-glucose
-
-
?
D-glucose + 1,2-naphthoquinone
D-glucono-1,5-lactone + 1,2-naphthoquinol
-
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)
-
-
?
D-glucose + 1,4-benzoquinone
D-glucono-1,5-lactone + 1,4-benzoquinol
D-glucose + 1,4-naphthoquinone
D-glucono-1,5-lactone + 1,4-naphthoquinol
-
-
-
-
?
D-glucose + 1,6-pyrenedione
D-glucono-1,5-lactone + 1,6-pyrenediol
-
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
-
-
?
D-glucose + 1,8-pyrenedione
D-glucono-1,5-lactone + 1,8-pyrenediol
-
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
-
-
?
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
-
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)
-
-
?
D-glucose + a quinone
D-glucono-1,5-lactone + a quinol
D-glucose + a quinone
D-glucono-1,5-lactone + a reduced quinol
D-glucose + acceptor
D-glucono-1,5-lactone + reduced acceptor
-
-
-
-
?
D-glucose + coenzyme Q1
D-glucono-1,5-lactone + reduced coenzyme Q1
-
-
-
-
?
D-glucose + ferricenium hexafluorophosphate
D-glucono-1,5-lactone + ferrocenium hexafluorophosphate
D-glucose + ferricenium ion
D-glucono-1,5-lactone + ferrocenium ion
-
-
-
-
?
D-glucose + ferricyanide
D-glucono-1,5-lactone + ferrocyanide
D-glucose + menadione
D-glucono-1,5-lactone + menadiol
-
-
-
-
?
D-glucose + oxidized 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenol indophenol
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + reduced phenazine methosulfate
D-glucose + tetramethyl-p-phenylenediamine
D-glucono-1,5-lactone + reduced tetramethyl-p-phenylenediamine
-
-
-
-
?
D-lactose + 2,6-dichlorophenolindophenol
D-lactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
D-maltose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-maltose + acceptor
?
-
-
-
-
?
D-mannose + acceptor
D-manno-1,5-lactone + reduced acceptor
-
8.6% of the activity with D-glucose
-
-
?
D-raffinose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
D-xylose + 2,6-dichloroindophenol
D-xylono-1,5-lactone + 2,6-dichlorophenolindophenol
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
D-xylose + acceptor
D-xylono-1,5-lactone + reduced acceptor
-
13% of the activity with D-glucose
-
-
?
D-xylose + ferricenium ion
D-xylono-1,5-lactone + ferrocenium ion
-
-
-
-
?
D-xylose + oxidized 2,6-dichlorophenol indophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenol indophenol
fructose + 2,6-dichlorophenolindophenol
?
-
8% of the activity with D-glucose
-
-
?
glutamine + a quinone
? + a quinol
-
low activity
-
-
?
L-arabinose + 2,6-dichlorophenolindophenol
L-arabinono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
1.5% activity compared to D-glucose
-
-
?
L-arabinose + acceptor
L-arabinono-1,5-lactone + reduced acceptor
-
2.8% of the activity with D-glucose
-
-
?
L-rhamnose + acceptor
L-rhamnone-1,5-lactone + reduced acceptor
-
7.5% of the activity with D-glucose
-
-
?
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
?
-
3.2% of the activity with D-glucose
-
-
?
maltotetraose + 2,6-dichlorophenolindophenol
maltotetraono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
0.66% activity compared to D-glucose
-
-
?
maltotriose + 2,6-dichlorophenolindophenol
maltotriono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
mannose + 2,6-dichlorophenolindophenol
mannono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
0.66% activity compared to D-glucose
-
-
?
trehalose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
0.22% activity compared to D-glucose
-
-
?
additional information
?
-
2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
11.5% activity compared to D-glucose
-
-
?
2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
11.5% activity compared to D-glucose
-
-
?
2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
about 11% activity compared to D-glucose
-
-
?
2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
about 8.4% activity compared to D-glucose
-
-
?
2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
about 11% activity compared to D-glucose
-
-
?
2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
about 8.4% activity compared to D-glucose
-
-
?
2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
about 11% activity compared to D-glucose
-
-
?
2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
about 8.4% activity compared to D-glucose
-
-
?
2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
60.1% activity compared to D-glucose
-
-
?
2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
60.1% activity compared to D-glucose
-
-
?
D-galactose + 2,6-dichlorophenolindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
2.2% activity compared to D-glucose
-
-
?
D-galactose + 2,6-dichlorophenolindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
2.2% activity compared to D-glucose
-
-
?
D-galactose + 2,6-dichlorophenolindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
0.44% activity compared to D-glucose
-
-
?
D-galactose + 2,6-dichlorophenolindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
0.44% activity compared to D-glucose
-
-
?
D-glucose + 1,4-benzoquinone
D-glucono-1,5-lactone + 1,4-benzoquinol
-
-
-
-
?
D-glucose + 1,4-benzoquinone
D-glucono-1,5-lactone + 1,4-benzoquinol
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-gluconic acid + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-gluconic acid + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-gluconic acid + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-gluconic acid + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
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
-
-
-
-
r
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
100% activity
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
the enzyme has high specificity toward D-glucose
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
the enzyme has high specificity toward D-glucose
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
high substrate specificity for D-glucose
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
high substrate specificity for D-glucose
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
100% activity
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
100% activity
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
100% activity
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
high substrate specificity for D-glucose
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
high substrate specificity for D-glucose
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-glucose + a quinone
D-glucono-1,5-lactone + a quinol
-
-
-
-
?
D-glucose + a quinone
D-glucono-1,5-lactone + a quinol
-
-
-
-
?
D-glucose + a quinone
D-glucono-1,5-lactone + a quinol
-
-
-
-
?
D-glucose + a quinone
D-glucono-1,5-lactone + a quinol
-
-
-
-
?
D-glucose + a quinone
D-glucono-1,5-lactone + a quinol
-
-
-
-
?
D-glucose + a quinone
D-glucono-1,5-lactone + a quinol
-
-
-
-
?
D-glucose + a quinone
D-glucono-1,5-lactone + a reduced quinol
-
-
-
-
?
D-glucose + a quinone
D-glucono-1,5-lactone + a reduced quinol
-
-
-
-
?
D-glucose + ferricenium hexafluorophosphate
D-glucono-1,5-lactone + ferrocenium hexafluorophosphate
-
-
-
-
?
D-glucose + ferricenium hexafluorophosphate
D-glucono-1,5-lactone + ferrocenium hexafluorophosphate
-
-
-
-
?
D-glucose + ferricyanide
D-glucono-1,5-lactone + ferrocyanide
-
-
-
-
?
D-glucose + ferricyanide
D-glucono-1,5-lactone + ferrocyanide
-
-
-
-
?
D-glucose + ferricyanide
D-glucono-1,5-lactone + ferrocyanide
-
-
-
-
?
D-glucose + oxidized 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenol indophenol
-
with phenazine methosulfate
-
-
?
D-glucose + oxidized 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenol indophenol
-
with phenazine methosulfate
-
-
?
D-glucose + oxidized 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenol indophenol
-
-
-
-
?
D-glucose + oxidized 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenol indophenol
-
-
-
-
?
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + reduced phenazine methosulfate
-
-
-
-
?
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + reduced phenazine methosulfate
-
-
-
-
?
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + reduced phenazine methosulfate
-
-
-
-
?
D-lactose + 2,6-dichlorophenolindophenol
D-lactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
0.6% activity compared to D-glucose
-
-
?
D-lactose + 2,6-dichlorophenolindophenol
D-lactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
0.6% activity compared to D-glucose
-
-
?
D-raffinose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
about 3.2% activity compared to D-glucose
-
-
?
D-raffinose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
about 4.5% activity compared to D-glucose
-
-
?
D-xylose + 2,6-dichloroindophenol
D-xylono-1,5-lactone + 2,6-dichlorophenolindophenol
24.8% activity compared to D-glucose
-
-
?
D-xylose + 2,6-dichloroindophenol
D-xylono-1,5-lactone + 2,6-dichlorophenolindophenol
24.8% activity compared to D-glucose
-
-
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
17% activity compared to D-glucose
-
-
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
1.8% activity compared to D-glucose
-
-
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
7.4% activity compared to D-glucose
-
-
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
7.4% activity compared to D-glucose
-
-
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
1.53% activity compared to D-glucose
-
-
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
1.53% activity compared to D-glucose
-
-
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
about 50% activity compared to D-glucose
-
-
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
about 40% activity compared to D-glucose
-
-
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
about 50% activity compared to D-glucose
-
-
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
about 50% activity compared to D-glucose
-
-
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
27.6% activity compared to D-glucose
-
-
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
27.6% activity compared to D-glucose
-
-
?
D-xylose + oxidized 2,6-dichlorophenol indophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenol indophenol
-
with phenazine methosulfate
-
-
?
D-xylose + oxidized 2,6-dichlorophenol indophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenol indophenol
-
with phenazine methosulfate
-
-
?
maltose + 2,6-dichlorophenol indophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
1.09% activity compared to D-glucose
-
-
?
maltose + 2,6-dichlorophenol indophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
1.09% activity compared to D-glucose
-
-
?
maltose + 2,6-dichlorophenolindophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
17.7% activity compared to D-glucose
-
-
?
maltose + 2,6-dichlorophenolindophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
maltose + 2,6-dichlorophenolindophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
about 11% activity compared to D-glucose
-
-
?
maltose + 2,6-dichlorophenolindophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
about 21% activity compared to D-glucose
-
-
?
maltotriose + 2,6-dichlorophenolindophenol
maltotriono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
0.88% activity compared to D-glucose
-
-
?
maltotriose + 2,6-dichlorophenolindophenol
maltotriono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
3.4% activity compared to D-glucose
-
-
?
maltotriose + 2,6-dichlorophenolindophenol
maltotriono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
3.4% activity compared to D-glucose
-
-
?
maltotriose + 2,6-dichlorophenolindophenol
maltotriono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
6.8% activity compared to D-glucose
-
-
?
maltotriose + 2,6-dichlorophenolindophenol
maltotriono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
6.8% activity compared to D-glucose
-
-
?
additional information
?
-
less than 1% activity with D-mannose, D-maltose, D-galactose, D-allose, D-lactose, D-fructose, sucrose, and cellobiose
-
-
?
additional information
?
-
-
less than 1% activity with maltose, cellobiose, lactose, mannose, fructose, allose, galactose, and sucrose
-
-
?
additional information
?
-
-
substrate sppecificity, overview
-
-
?
additional information
?
-
-
substrate sppecificity, overview
-
-
?
additional information
?
-
no activity with D-fructose, S-sorbitol, and D-sucrose
-
-
?
additional information
?
-
-
no activity with D-fructose, S-sorbitol, and D-sucrose
-
-
?
additional information
?
-
no activity with D-fructose, S-sorbitol, and D-sucrose
-
-
?
additional information
?
-
-
no activity with D-fructose, S-sorbitol, and D-sucrose
-
-
?
additional information
?
-
-
substrate specificity, overview. Lactose, gluconic acid, mannose, mannitol, sorbitol, galactose, sucrose, maltose, arabinose, xylitol, rhamnose, fucose, trehalose, and fructose are poor or no substrates
-
-
?
additional information
?
-
-
suitable electron acceptors are quinones, phenoxy radicals, 2,6-dichloroindophenol, ferricyanide and ferrocenium hexafluorophosphate. Reduction of quinones and phenoxy radicals by extracellular enzyme, overview
-
-
?
additional information
?
-
-
suitable electron acceptors are quinones, phenoxy radicals, 2,6-dichloroindophenol, ferricyanide and ferrocenium hexafluorophosphate. Reduction of quinones and phenoxy radicals by extracellular enzyme, overview
-
-
?
additional information
?
-
-
enzyme participates in strengthening the encapsulation and in killing reaction, via reaction with quinones generated by phenolidase and subsequent production of free radicals
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
no activity with sucrose
-
-
?
additional information
?
-
-
no activity with sucrose
-
-
?
additional information
?
-
no substrate: maltose
-
-
?
additional information
?
-
-
no substrate: maltose
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
no activity with D-arabinose, D-cellobiose, D-fructose, D-galactose, lactitol, maltitol, D-mannitol, D-mannose, D-sorbitol, sucrose, and D-trehalose
-
-
?
additional information
?
-
-
no activity with D-arabinose, D-cellobiose, D-fructose, D-galactose, lactitol, maltitol, D-mannitol, D-mannose, D-sorbitol, sucrose, and D-trehalose
-
-
?
additional information
?
-
-
no activity with D-arabinose, D-cellobiose, D-fructose, D-galactose, lactitol, maltitol, D-mannitol, D-mannose, D-sorbitol, sucrose, and D-trehalose
-
-
?
additional information
?
-
no substrate: maltose
-
-
?
additional information
?
-
-
no substrate: maltose
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
no substrate: maltose
-
-
?
additional information
?
-
-
no substrate: maltose
-
-
?
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H505A
the mutant enzyme shows drastic decrease in the enzymatic activity
H548A
the mutant enzyme shows drastic decrease in the enzymatic activity
V149C/G190C
the mutant shows a 110 min half-life of thermal inactivation at 45°C, which is 13fold greater than that of the wild type enzyme
H505A
-
the mutant enzyme shows drastic decrease in the enzymatic activity
-
H548A
-
the mutant enzyme shows drastic decrease in the enzymatic activity
-
A472C
-
site directed mutagenesis
A472D
-
site directed mutagenesis
A472E
-
site directed mutagenesis
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
C213S
-
the mutant shows 68% of wild type activity
N475A
-
site directed mutagenesis
N475C
-
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
-
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
-
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/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
A472F
-
site directed mutagenesis
A472F
-
mutant with higher substrate specificity for glucose in relation to maltose, constructed by site-directed mutagenesis
N475D
-
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
-
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
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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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.
-
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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
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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
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Burkholderia cepacia
-
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Yamaoka, H.; Ferri, S.; Fujikawa, M.; Sode, K.
Essential role of the small subunit of thermostable glucose dehydrogenase from Burkholderia cepacia
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26
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Burkholderia cepacia, Burkholderia cepacia SM4
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Okuda-Shimazaki, J.; Kakehi, N.; Yamazaki, T.; Tomiyama, M.; Sode, K.
Biofuel cell system employing thermostable glucose dehydrogenase
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30
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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
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402
2069-2077
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Aspergillus sp., Colletotrichum gloeosporioides, Komagataella pastoris
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
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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
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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
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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, Thermoascus crustaceus NBRC 9129 (A0A1E1GL87), Thermoascus crustaceus NBRC 9129, Rasamsonia emersonii NBRC 31232 (A0A1E1GL61)
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
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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
Ozawa, K.; Iwasa, H.; Sasaki, N.; Kinoshita, N.; Hiratsuka, A.; Yokoyama, K.
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Aspergillus sp.
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Cohen, R.; Cohen, Y.; Mukha, D.; Yehezkeli, O.
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Aspergillus sp.
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Wearable glucose/oxygen biofuel cell fabricated using modified aminoferrocene and flavin adenine dinucleotide-dependent glucose dehydrogenase on poly(glycidyl methacrylate)-grafted MgO-templated carbon
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Aspergillus oryzae
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Milton, R.
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Aspergillus sp.
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