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2-amino-D-glucose + pyrroloquinoline quinone
2-amino-D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
2-deoxy-D-glucose + 2,6-dichlorophenolindolphenol
2-deoxy-D-glucono-1,5-lactone + ?
-
-
-
?
2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
2-deoxy-D-glucose + oxidized N-methylphenazonium methyl sulfate
2-deoxy-D-glucono-1,5-lactone + reduced N-methylphenazonium methyl sulfate
-
-
-
-
?
2-deoxy-D-glucose + phenazine methosulfate
2-deoxy-D-glucono-1,5-lactone + reduced phenazine methosulfate
2-deoxy-D-glucose + pyrroloquinoline quinone
2-deoxy-D-glucono-1,5-lactone + pyrroloquinoline quinol
2-deoxy-D-glucose + ubiquinone
2-deoxy-D-glucono-1,5-lactone + ubiquinol
3-deoxy-D-glucose + pyrroloquinoline quinone
3-deoxy-D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
3-methyl-alpha-methyl-D-glucopyranose + ubiquinone
D-xylono-1,5-lactone + ubiquinol
3-O-methyl-D-glucose + 2,6-dichlorophenolindolphenol
3-O-methyl-D-glucono-1,5-lactone + ?
3-O-methyl-D-glucose + pyrroloquinoline quinone
3-O-methyl-D-glucono-1,5-lactone + pyrroloquinoline quinol
3-O-methyl-D-glucose + ubiquinone
3-O-methyl-D-glucono-1,5-lactone + ubiquinol
6-deoxy-D-glucose + pyrroloquinoline quinone
6-deoxy-D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
allose + 2,6-dichlorophenolindolphenol
?
allose + ubiquinone
? + ubiquinol
alpha-D-lactose + phenazine methosulfate
alpha-D-lactono-1,5-lactone + reduced phenazine methosulfate
beta-D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
cellobiose + 2,6-dichlorophenolindolphenol
?
-
-
-
?
cellobiose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
58% of the activity as compared to D-glucose
-
-
?
cellobiose + pyrroloquinoline quinone
?
-
70% of the activity with D-glucose
-
-
?
cellobiose + ubiquinone
?
-
high activity
-
-
?
cellobiose + ubiquinone
? + ubiquinol
D-allose + 2,6-dichlorophenolindophenol
D-allono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
D-allose + pyrroloquinoline quinone
D-allono-1,5-lactone + pyrroloquinoline quinol
D-allose + ubiquinone
?
-
high activity
-
-
?
D-allose + ubiquinone
? + ubiquinol
-
-
-
-
?
D-arabinose + N-methylphenazonium methyl sulfate
D-arabinono-1,5-lactone + ?
D-cellobiose + 2,6-dichloroindophenol
D-cellobiono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-cellobiose + phenazine methosulfate
D-cellobiono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
D-fructose + 2,6-dichloroindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-fucose + N-ethylphenazonium ethyl sulfate
6-deoxy-D-galactono-1,5-lactone + ?
-
-
-
-
?
D-fucose + oxidized N-methylphenazonium methyl sulfate
6-deoxy-D-galactono-1,5-lactone + reduced N-methylphenazonium methyl sulfate
-
-
-
-
?
D-fucose + pyrrolquinoline quinone
6-deoxy-D-galactono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-fucose + ubiquinone
? + ubiquinol
-
-
-
-
?
D-galactose + 2,6-dichloroindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-galactose + 2,6-dichlorophenolindolphenol
D-galactono-1,5-lactone + ?
D-galactose + 2,6-dichlorophenolindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
D-galactose + N-methylphenazonium methyl sulfate
D-galactono-1,5-lactone + ?
D-galactose + oxidized N-methylphenazonium methyl sulfate
D-galactono-1,5-lactone + reduced N-methylphenazonium methyl sulfate
-
-
-
-
?
D-galactose + phenazine methosulfate
D-galactono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
D-galactose + pyrroloquinoline quinone
D-galactono-1,5-lactone + pyrroloquinoline quinol
D-galactose + ubiquinone
?
D-galactose + ubiquinone
D-galactono-1,5-lactone + ubiquinol
D-glucosamino-1,5-lactone + reduced phenazine methosulfate
D-glucosamine + reduced phenazine methosulfate
-
-
-
?
D-glucose + 1,4-naphthoquinone
D-glucono-1,5-lactone + ?
D-glucose + 2,3-dichloro-1,4-naphthoquinone
D-glucono-1,5-lactone + ?
D-glucose + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 2,6-dichloroindophenol
D-glucono-1,5-lactone + reduced 2,6-dichloroindophenol
-
-
-
-
?
D-glucose + 2,6-dichloroindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-glucose + 2,6-dichlorophenol-indophenol
D-glucono-1,5-lactone + ?
D-glucose + 2,6-dichlorophenolindolphenol
D-glucono-1,5-lactone + ?
D-glucose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
D-glucose + 2-methyl-6-methoxy-1,4-benzoquinone
D-glucono-1,5-lactone + ?
D-glucose + 4-(4-ferrocenylimino-methyl)phenol
D-glucono-1,5-lactone + ?
D-glucose + 4-ferrocenylnitrophenol
D-glucono-1,5-lactone + ?
D-glucose + 4-ferrocenylphenol
D-glucono-1,5-lactone + ?
D-glucose + 9,10-phenanthrenequinone
D-glucono-1,5-lactone + ?
-
9,10-phenanthrenequinone shows low effectivity as redox mediator
-
-
?
D-glucose + ?
D-glucono-1,5-lactone + ?
physiological electron acceptor in not known
-
-
?
D-glucose + decylubiquinone
D-glucono-1,5-lactone + decylubiquinol
-
-
-
-
?
D-glucose + ferricyanide
D-glucono-1,5-lactone + ferrocyanide
D-glucose + N,N,N,N-tetramethyl-o-phenylenediamine
?
-
-
-
-
r
D-glucose + N-ethylphenazonium ethyl sulfate
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + N-methylphenazonium methyl sulfate
D-glucono-1,5-lactone + ?
-
D-glucose is the preferred substrate
-
-
?
D-glucose + oxidized 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
D-glucose + oxidized N-methylphenazonium methyl sulfate
D-glucono-1,5-lactone + reduced N-methylphenazonium methyl sulfate
-
-
-
-
?
D-glucose + phenazine methosulfate
?
-
-
-
-
?
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + ?
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + reduced phenazine methosulfate
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
D-glucose + trimethyl-1,4-benzoquinone
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
D-glucose + ubiquinone Q1
D-glucono-1,5-lactone + ?
D-glucose + ubiquinone Q1
D-glucono-1,5-lactone + ubiquinol Q1
-
-
-
-
?
D-glucose + ubiquinone Q2
D-glucono-1,5-lactone + ?
D-glucose + ubiquinone Q2
D-glucono-1,5-lactone + ubiquinol Q2
-
-
-
-
?
D-glucose + ubiquinone Q4
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + ubiquinone Q6
D-glucono-1,5-lactone + ?
D-glucose + ubiquinone Q9
D-glucono-1,5-lactone + ubiquinol Q9
D-glucose 6-phosphate + phenazine methosulfate
6-phospho-D-glucono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
D-lactose + 2,6-dichlorophenolindophenol
D-lactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
D-lyxose + ubiquinone
?
-
very low activity
-
-
?
D-maltose + 2,6-dichlorophenolindophenol
D-maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
71% activity compared to D-glucose
-
-
?
D-maltose + pyrroloquinoline quinone
?
-
-
-
-
?
D-mannose + 2,6-dichloroindophenol
D-mannono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-mannose + 2,6-dichlorophenolindolphenol
?
-
-
-
?
D-mannose + 2,6-dichlorophenolindophenol
D-mannono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
36% activity compared to D-glucose
-
-
?
D-mannose + phenazine methosulfate
D-mannono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
D-mannose + pyrroloquinoline quinone
D-mannono-1,5-lactone + pyrroloquinoline quinol
D-mannose + ubiquinone
?
-
low activity
-
-
?
D-mannose + ubiquinone
? + ubiquinol
D-melibiose + pyrroloquinoline quinone
?
D-ribose + 2,6-dichloroindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-ribose + phenazine methosulfate
D-ribono-1,4-lactone + reduced phenazine methosulfate
-
-
-
?
D-ribose + pyrroloquinoline quinone
D-ribono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-ribose + ubiquinone
?
-
low activity
-
-
?
D-ribose + ubiquinone
? + ubiquinol
-
-
-
?
D-xylose + 2,6-dichloroindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-xylose + 2,6-dichlorophenolindolphenol
D-xylono-1,5-lactone + ?
-
-
-
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
D-xylose + N-ethylphenazonium ethyl sulfate
D-xylono-1,5-lactone + ?
-
-
-
-
?
D-xylose + N-methylphenazonium methyl sulfate
D-xylono-1,5-lactone + ?
-
22% activity compared to D-glucose
-
-
?
D-xylose + oxidized N-methylphenazonium methyl sulfate
D-xylono-1,5-lactone + reduced N-methylphenazonium methyl sulfate
-
-
-
-
?
D-xylose + phenazine methosulfate
D-xylono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
D-xylose + pyrroloquinoline quinone
D-xylono-1,5-lactone + pyrroloquinoline quinol
D-xylose + ubiquinone
?
-
low activity
-
-
?
D-xylose + ubiquinone
D-xylono-1,5-lactone + ubiquinol
ethanol + phenazine methosulfate
acetaldehyde + reduced phenazine methosulfate
L-arabinose + 2,6-dichloroindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
L-arabinose + 2,6-dichlorophenolindophenol
L-arabinono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
97% activity compared to D-glucose
-
-
?
L-arabinose + N-ethylphenazonium ethyl sulfate
L-arabino-1,5-lactone + ?
-
-
-
-
?
L-arabinose + oxidized N-methylphenazonium methyl sulfate
L-arabino-1,5-lactone + reduced N-methylphenazonium methyl sulfate
-
-
-
-
?
L-arabinose + phenazine methosulfate
D-arabinono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
L-arabinose + pyrroloquinoline quinone
L-arabino-1,5-lactone + pyrroloquinoline quinol
L-arabinose + ubiquinone
?
-
high activity
-
-
?
L-arabinose + ubiquinone
L-arabino-1,5-lactone + ubiquinol
L-lyxose + pyrroloquinoline quinone
?
-
-
-
-
?
L-rhamnose + pyrroloquinoline quinone
L-rhamnono-1,5-lactone + pyrroloquinoline quinol
lactose + 2,6-dichlorophenol-indophenol
?
-
-
-
-
?
lactose + 2,6-dichlorophenolindolphenol
?
lactose + 2,6-dichlorophenolindophenol
lactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
40% of the activity as compared to D-glucose
-
-
?
lactose + pyrroloquinoline quinone
?
lactose + ubiquinone
? + ubiquinol
maltose + 2,6-dichloroindophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
?
maltose + 2,6-dichlorophenolindolphenol
?
maltose + 2,6-dichlorophenolindophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
91% of the activity as compared to D-glucose
-
-
?
maltose + N-methylphenazonium methyl sulfate
maltono-1,5-lactone + ?
-
17% activity compared to D-glucose
-
-
?
maltose + phenazine methosulfate
D-maltono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
maltose + pyrroloquinoline quinone
?
maltose + ubiquinone
? + ubiquinol
maltotriose + 2,6-dichlorophenolindophenol
?
-
-
-
-
r
maltotriose + phenazine methosulfate
D-maltotriono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
mannitol + phenazine methosulfate
?
-
-
-
?
melibiose + 2,6-dichlorophenol-indophenol
?
-
-
-
-
?
melibiose + ubiquinone
?
-
low activity
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
phenazine methosulfate + 2,6-dichlorophenol indophenol
?
sucrose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
30% of the activity as compared to D-glucose
-
-
?
xylitol + phenazine methosulfate
?
-
-
-
?
additional information
?
-
2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
3% activity compared to D-glucose
-
-
?
2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
3% activity compared to D-glucose
-
-
?
2-deoxy-D-glucose + phenazine methosulfate
2-deoxy-D-glucono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
2-deoxy-D-glucose + phenazine methosulfate
2-deoxy-D-glucono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
2-deoxy-D-glucose + pyrroloquinoline quinone
2-deoxy-D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
2-deoxy-D-glucose + pyrroloquinoline quinone
2-deoxy-D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
2-deoxy-D-glucose + pyrroloquinoline quinone
2-deoxy-D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
2-deoxy-D-glucose + ubiquinone
2-deoxy-D-glucono-1,5-lactone + ubiquinol
-
low activity, recombinant isozyme PQQGDH-B
-
-
?
2-deoxy-D-glucose + ubiquinone
2-deoxy-D-glucono-1,5-lactone + ubiquinol
-
-
-
?
2-deoxy-D-glucose + ubiquinone
2-deoxy-D-glucono-1,5-lactone + ubiquinol
-
low activity
-
-
?
2-deoxy-D-glucose + ubiquinone
2-deoxy-D-glucono-1,5-lactone + ubiquinol
-
96% activity compared to D-glucose
-
-
?
2-deoxy-D-glucose + ubiquinone
2-deoxy-D-glucono-1,5-lactone + ubiquinol
-
96% activity compared to D-glucose
-
-
?
2-deoxy-D-glucose + ubiquinone
2-deoxy-D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
3-methyl-alpha-methyl-D-glucopyranose + ubiquinone
D-xylono-1,5-lactone + ubiquinol
-
20% activity compared to D-glucose
-
-
?
3-methyl-alpha-methyl-D-glucopyranose + ubiquinone
D-xylono-1,5-lactone + ubiquinol
-
20% activity compared to D-glucose
-
-
?
3-O-methyl-D-glucose + 2,6-dichlorophenolindolphenol
3-O-methyl-D-glucono-1,5-lactone + ?
-
-
-
-
?
3-O-methyl-D-glucose + 2,6-dichlorophenolindolphenol
3-O-methyl-D-glucono-1,5-lactone + ?
-
-
-
?
3-O-methyl-D-glucose + pyrroloquinoline quinone
3-O-methyl-D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
3-O-methyl-D-glucose + pyrroloquinoline quinone
3-O-methyl-D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
3-O-methyl-D-glucose + ubiquinone
3-O-methyl-D-glucono-1,5-lactone + ubiquinol
-
recombinant isozyme PQQGDH-B
-
-
?
3-O-methyl-D-glucose + ubiquinone
3-O-methyl-D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
3-O-methyl-D-glucose + ubiquinone
3-O-methyl-D-glucono-1,5-lactone + ubiquinol
-
-
-
?
allose + 2,6-dichlorophenolindolphenol
?
-
-
-
-
?
allose + 2,6-dichlorophenolindolphenol
?
-
-
-
?
allose + ubiquinone
? + ubiquinol
-
recombinant isozyme PQQGDH-B
-
-
?
allose + ubiquinone
? + ubiquinol
-
-
-
-
?
alpha-D-lactose + phenazine methosulfate
alpha-D-lactono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
alpha-D-lactose + phenazine methosulfate
alpha-D-lactono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
beta-D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
beta-D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
redox-related structural changes, overview
-
-
?
cellobiose + ubiquinone
? + ubiquinol
-
-
-
-
?
cellobiose + ubiquinone
? + ubiquinol
-
recombinant isozyme PQQGDH-B
-
-
?
cellobiose + ubiquinone
? + ubiquinol
-
-
-
-
?
D-allose + 2,6-dichlorophenolindophenol
D-allono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
85% activity compared to D-glucose
-
-
?
D-allose + 2,6-dichlorophenolindophenol
D-allono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
85% activity compared to D-glucose
-
-
?
D-allose + pyrroloquinoline quinone
D-allono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-allose + pyrroloquinoline quinone
D-allono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-arabinose + N-methylphenazonium methyl sulfate
D-arabinono-1,5-lactone + ?
-
8.0% activity compared to D-glucose
-
-
?
D-arabinose + N-methylphenazonium methyl sulfate
D-arabinono-1,5-lactone + ?
-
8.0% activity compared to D-glucose
-
-
?
D-galactose + 2,6-dichlorophenolindolphenol
D-galactono-1,5-lactone + ?
-
-
-
-
?
D-galactose + 2,6-dichlorophenolindolphenol
D-galactono-1,5-lactone + ?
-
-
-
?
D-galactose + 2,6-dichlorophenolindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
48% of the activity as compared to D-glucose
-
-
?
D-galactose + 2,6-dichlorophenolindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
71% activity compared to D-glucose
-
-
?
D-galactose + 2,6-dichlorophenolindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
71% activity compared to D-glucose
-
-
?
D-galactose + N-methylphenazonium methyl sulfate
D-galactono-1,5-lactone + ?
-
20% activity compared to D-glucose
-
-
?
D-galactose + N-methylphenazonium methyl sulfate
D-galactono-1,5-lactone + ?
-
20% activity compared to D-glucose
-
-
?
D-galactose + pyrroloquinoline quinone
D-galactono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-galactose + pyrroloquinoline quinone
D-galactono-1,5-lactone + pyrroloquinoline quinol
-
30% of the activity with D-glucose
-
-
?
D-galactose + pyrroloquinoline quinone
D-galactono-1,5-lactone + pyrroloquinoline quinol
-
30% of the activity with D-glucose
-
-
?
D-galactose + pyrroloquinoline quinone
D-galactono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-galactose + pyrroloquinoline quinone
D-galactono-1,5-lactone + pyrroloquinoline quinol
-
6.5% of the activity with D-glucose
-
-
?
D-galactose + ubiquinone
?
-
-
-
?
D-galactose + ubiquinone
?
-
low activity
-
-
?
D-galactose + ubiquinone
D-galactono-1,5-lactone + ubiquinol
-
-
-
-
?
D-galactose + ubiquinone
D-galactono-1,5-lactone + ubiquinol
-
recombinant isozyme PQQGDH-B
-
-
?
D-galactose + ubiquinone
D-galactono-1,5-lactone + ubiquinol
-
-
-
-
?
D-galactose + ubiquinone
D-galactono-1,5-lactone + ubiquinol
-
-
-
-
?
D-galactose + ubiquinone
D-galactono-1,5-lactone + ubiquinol
-
-
-
-
?
D-galactose + ubiquinone
D-galactono-1,5-lactone + ubiquinol
-
-
-
-
?
D-galactose + ubiquinone
D-galactono-1,5-lactone + ubiquinol
-
-
-
?
D-galactose + ubiquinone
D-galactono-1,5-lactone + ubiquinol
-
low activity, recombinant wild-type and mutant isozymes PQQGDH-B
-
-
?
D-galactose + ubiquinone
D-galactono-1,5-lactone + ubiquinol
-
86% activity compared to D-glucose
-
-
?
D-galactose + ubiquinone
D-galactono-1,5-lactone + ubiquinol
-
86% activity compared to D-glucose
-
-
?
D-glucose + 1,4-naphthoquinone
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 1,4-naphthoquinone
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 2,3-dichloro-1,4-naphthoquinone
D-glucono-1,5-lactone + ?
-
2,3-dichloro-1,4-naphthoquinone shows low effectivity as redox mediator
-
-
?
D-glucose + 2,3-dichloro-1,4-naphthoquinone
D-glucono-1,5-lactone + ?
-
2,3-dichloro-1,4-naphthoquinone shows low effectivity as redox mediator
-
-
?
D-glucose + 2,6-dichlorophenol-indophenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 2,6-dichlorophenol-indophenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 2,6-dichlorophenol-indophenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 2,6-dichlorophenol-indophenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindolphenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindolphenol
D-glucono-1,5-lactone + ?
-
-
-
?
D-glucose + 2,6-dichlorophenolindolphenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindolphenol
D-glucono-1,5-lactone + ?
best substrate
-
-
?
D-glucose + 2,6-dichlorophenolindolphenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
? + 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
-
100% activity
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
100% activity
-
-
?
D-glucose + 2-methyl-6-methoxy-1,4-benzoquinone
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 2-methyl-6-methoxy-1,4-benzoquinone
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 4-(4-ferrocenylimino-methyl)phenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 4-(4-ferrocenylimino-methyl)phenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 4-(4-ferrocenylimino-methyl)phenol
D-glucono-1,5-lactone + ?
-
-
-
-
r
D-glucose + 4-(4-ferrocenylimino-methyl)phenol
D-glucono-1,5-lactone + ?
-
-
-
-
r
D-glucose + 4-ferrocenylnitrophenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 4-ferrocenylnitrophenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 4-ferrocenylnitrophenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 4-ferrocenylphenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 4-ferrocenylphenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + ferricyanide
D-glucono-1,5-lactone + ferrocyanide
-
D-glucose is the preferred substrate
-
-
?
D-glucose + ferricyanide
D-glucono-1,5-lactone + ferrocyanide
-
D-glucose is the preferred substrate
-
-
?
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-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-glucose + oxidized 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-glucose + oxidized 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-glucose + oxidized 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + ?
-
-
-
-
?
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 + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
membrane-bound enzyme functions by linking to the respiratory chain via ubiquinone
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
membrane-bound enzyme functions by linking to the respiratory chain via ubiquinone
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
enzyme donates electrons directly to ubiquinone in the respiratory chain
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
linked to the respiratory chain of a wide variety of bacteria
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
654449, 655791, 655929, 671165, 725196, 739873, 740191, 740304, 740321, 740441, 740577, 740933 -
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
highest activity
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
best substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
best substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
preferred substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
recombinant isozyme PQQGDH-B
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
preferred substrate, assayed with the electron acceptors phenazine methosulfate and dichlorphenolindophenol
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
preferred substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
preferred substrate, assayed with the electron acceptors phenazine methosulfate and dichlorphenolindophenol
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
best substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
preferred substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
preferred substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
best substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
best substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
a pivotal PQQ-containing quinoprotein coupled to the respiratory chain in the periplasmic oxidation of alcohols and sugars
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
transfers electrons to the cytochrome oxidase through ubiquinone in the electron transport chain
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
best substrate, recombinant wild-type and mutant isozymes PQQGDH-B
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
with ubiquinone-8 as minor compound, PQQ acts in electron transfer between enzyme and ubiquinone
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
preferred substrate, assayed with the electron acceptors phenazine methosulfate and dichlorphenolindophenol
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
assayed with the electron acceptors phenazine methosulfate and dichlorphenolindophenol
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
assayed with the electron acceptors phenazine methosulfate and dichlorphenolindophenol
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
D-glucose + ubiquinone Q1
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + ubiquinone Q1
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + ubiquinone Q1
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + ubiquinone Q2
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + ubiquinone Q2
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + ubiquinone Q2
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + ubiquinone Q2
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + ubiquinone Q6
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + ubiquinone Q6
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + ubiquinone Q6
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + ubiquinone Q9
D-glucono-1,5-lactone + ubiquinol Q9
-
-
-
-
?
D-glucose + ubiquinone Q9
D-glucono-1,5-lactone + ubiquinol Q9
-
-
-
-
?
D-lactose + 2,6-dichlorophenolindophenol
D-lactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
91% activity compared to D-glucose
-
-
?
D-lactose + 2,6-dichlorophenolindophenol
D-lactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
91% activity compared to D-glucose
-
-
?
D-mannose + pyrroloquinoline quinone
D-mannono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-mannose + pyrroloquinoline quinone
D-mannono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-mannose + pyrroloquinoline quinone
D-mannono-1,5-lactone + pyrroloquinoline quinol
-
no activity
-
-
?
D-mannose + pyrroloquinoline quinone
D-mannono-1,5-lactone + pyrroloquinoline quinol
-
8.6% of the activity with D-glucose
-
-
?
D-mannose + ubiquinone
? + ubiquinol
-
recombinant isozyme PQQGDH-B
-
-
?
D-mannose + ubiquinone
? + ubiquinol
-
-
-
?
D-melibiose + pyrroloquinoline quinone
?
-
10% of the activity with D-glucose
-
-
?
D-melibiose + pyrroloquinoline quinone
?
-
-
-
-
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
32% of the activity as compared to D-glucose
-
-
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
86% activity compared to D-glucose
-
-
?
D-xylose + pyrroloquinoline quinone
D-xylono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-xylose + pyrroloquinoline quinone
D-xylono-1,5-lactone + pyrroloquinoline quinol
-
20% of the activity with D-glucose
-
-
?
D-xylose + pyrroloquinoline quinone
D-xylono-1,5-lactone + pyrroloquinoline quinol
-
20% of the activity with D-glucose
-
-
?
D-xylose + pyrroloquinoline quinone
D-xylono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-xylose + pyrroloquinoline quinone
D-xylono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-xylose + pyrroloquinoline quinone
D-xylono-1,5-lactone + pyrroloquinoline quinol
-
no activity
-
-
?
D-xylose + pyrroloquinoline quinone
D-xylono-1,5-lactone + pyrroloquinoline quinol
-
13% of the activity with D-glucose
-
-
?
D-xylose + ubiquinone
D-xylono-1,5-lactone + ubiquinol
-
recombinant isozyme PQQGDH-B
-
-
?
D-xylose + ubiquinone
D-xylono-1,5-lactone + ubiquinol
-
-
-
-
?
D-xylose + ubiquinone
D-xylono-1,5-lactone + ubiquinol
-
-
-
?
D-xylose + ubiquinone
D-xylono-1,5-lactone + ubiquinol
-
40% activity compared to D-glucose
-
-
?
D-xylose + ubiquinone
D-xylono-1,5-lactone + ubiquinol
-
40% activity compared to D-glucose
-
-
?
D-xylose + ubiquinone
D-xylono-1,5-lactone + ubiquinol
-
-
-
-
?
ethanol + phenazine methosulfate
acetaldehyde + reduced phenazine methosulfate
-
-
-
?
ethanol + phenazine methosulfate
acetaldehyde + reduced phenazine methosulfate
-
-
-
?
L-arabinose + pyrroloquinoline quinone
L-arabino-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
L-arabinose + pyrroloquinoline quinone
L-arabino-1,5-lactone + pyrroloquinoline quinol
-
35% of the activity with D-glucose
-
-
?
L-arabinose + pyrroloquinoline quinone
L-arabino-1,5-lactone + pyrroloquinoline quinol
-
35% of the activity with D-glucose
-
-
?
L-arabinose + pyrroloquinoline quinone
L-arabino-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
L-arabinose + pyrroloquinoline quinone
L-arabino-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
L-arabinose + pyrroloquinoline quinone
L-arabino-1,5-lactone + pyrroloquinoline quinol
-
2.8% of the activity with D-glucose
-
-
?
L-arabinose + ubiquinone
L-arabino-1,5-lactone + ubiquinol
-
-
-
-
?
L-arabinose + ubiquinone
L-arabino-1,5-lactone + ubiquinol
-
-
-
-
?
L-arabinose + ubiquinone
L-arabino-1,5-lactone + ubiquinol
-
-
-
?
L-rhamnose + pyrroloquinoline quinone
L-rhamnono-1,5-lactone + pyrroloquinoline quinol
-
7.5% of the activity with D-glucose
-
-
?
L-rhamnose + pyrroloquinoline quinone
L-rhamnono-1,5-lactone + pyrroloquinoline quinol
-
no activity
-
-
?
lactose + 2,6-dichlorophenolindolphenol
?
-
-
-
-
?
lactose + 2,6-dichlorophenolindolphenol
?
-
-
-
?
lactose + 2,6-dichlorophenolindolphenol
?
-
-
-
-
?
lactose + pyrroloquinoline quinone
?
-
-
-
-
?
lactose + pyrroloquinoline quinone
?
-
65% of the activity with D-glucose
-
-
?
lactose + pyrroloquinoline quinone
?
-
65% of the activity with D-glucose
-
-
?
lactose + pyrroloquinoline quinone
?
-
no activity
-
-
?
lactose + ubiquinone
?
-
-
-
-
?
lactose + ubiquinone
?
-
-
-
?
lactose + ubiquinone
? + ubiquinol
-
-
-
-
?
lactose + ubiquinone
? + ubiquinol
-
recombinant isozyme PQQGDH-B
-
-
?
lactose + ubiquinone
? + ubiquinol
-
-
-
-
?
maltose + 2,6-dichlorophenolindolphenol
?
-
-
-
-
?
maltose + 2,6-dichlorophenolindolphenol
?
-
-
-
?
maltose + 2,6-dichlorophenolindolphenol
?
-
-
-
-
?
maltose + pyrroloquinoline quinone
?
-
-
-
-
?
maltose + pyrroloquinoline quinone
?
-
90% of the activity with D-glucose
-
-
?
maltose + pyrroloquinoline quinone
?
-
5% of the activity with D-glucose
-
-
?
maltose + pyrroloquinoline quinone
?
-
-
-
-
?
maltose + pyrroloquinoline quinone
?
-
3.2% of the activity with D-glucose
-
-
?
maltose + ubiquinone
?
-
-
-
-
?
maltose + ubiquinone
?
-
-
-
?
maltose + ubiquinone
? + ubiquinol
-
-
-
-
?
maltose + ubiquinone
? + ubiquinol
-
recombinant isozyme PQQGDH-B
-
-
?
maltose + ubiquinone
? + ubiquinol
-
-
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
-
-
?
phenazine methosulfate + 2,6-dichlorophenol indophenol
?
-
-
-
-
?
phenazine methosulfate + 2,6-dichlorophenol indophenol
?
-
-
-
-
?
additional information
?
-
-
the oxidation of dissacharides by the enzyme can be considered as an in vitro artefact caused by the removal of the enzyme from its natural environment
-
-
?
additional information
?
-
-
absolute specificity with respect to the C1 position, only sugars are oxidized which have the same configuration of the H/OH substituents at this site as the beta-anomer of glucose. Absolute specificity with respect to the overall conformation of the sugar molecule, sugars with a 4C1 chair conformation are substrates, those with a 1C4 one are not. The nature and configuration of the substituents at the 3-position are hardly relevant for activity, and an equatorial pyranose group at the 4-position exhibits only a specific hindering of the binding of the aldose moiety of a disaccharide
-
-
?
additional information
?
-
evolutionary analysis of PQQ-containing proteins, overview
-
-
?
additional information
?
-
substrate specificities of recombinant wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
substrate specificity of native and immobilized enzyme
-
-
?
additional information
?
-
-
substrate specificity of the recombinant enzyme produced in Pichia pastoris
-
-
?
additional information
?
-
-
PQQ-GDH has a broad specificity toward the oxidation of aldose sugars (hexoses, pentoses, mono- and disaccharides) into the corresponding lactones and the reduction of artificial electron acceptors
-
-
?
additional information
?
-
-
no activity with D-glucosamine, L-altrose, L-lyxose, L-talose, L-mannose, D-altrose, D-arabinose, L-xylose, L-glucose, L-galactose, D-talose, and L-allose
-
-
?
additional information
?
-
-
substrate specificity of native and immobilized enzyme
-
-
?
additional information
?
-
-
the oxidation of dissacharides by the enzyme can be considered as an in vitro artefact caused by the removal of the enzyme from its natural environment
-
-
?
additional information
?
-
-
no activity with D-gluconate, D-sorbose, D-mannose, D-fructose, malic acid, sucrose, and citric acid
-
-
?
additional information
?
-
-
no activity with D-gluconate, D-sorbose, D-mannose, D-fructose, malic acid, sucrose, and citric acid
-
-
?
additional information
?
-
-
2-hydroxy-1,4-naphthoquinone, tetramethyl-1,4-benzoquinone, and 2-methyl-1,4-naphthoquinone are no redox mediators for the enzyme
-
-
?
additional information
?
-
-
substrate specificity of native and immobilized enzyme, maltose is a poor substrate
-
-
?
additional information
?
-
-
2-hydroxy-1,4-naphthoquinone, tetramethyl-1,4-benzoquinone, and 2-methyl-1,4-naphthoquinone are no redox mediators for the enzyme
-
-
?
additional information
?
-
-
substrate specificity of native and immobilized enzyme, maltose is a poor substrate
-
-
?
additional information
?
-
-
the membrane-bound enzyme donates electrons directly to ubiquinone during the oxidation of D-glucose, and these electrons are subsequently transferred to ubiquinol oxidase in the respiratory chain
-
-
?
additional information
?
-
-
the enzyme has a ubiquinone reacting site close to the periplasmic side of the membrane and thus its electron transfer to ubiquinone appears to be incapable of forming a proton electrochemical gradient across the inner membrane
-
-
?
additional information
?
-
-
evolutionary analysis of PQQ-containing proteins, overview
-
-
?
additional information
?
-
-
substrate specificities of wild-type and mutant isozyme PQQGDH-B, overview
-
-
?
additional information
?
-
substrate specificity of recombinant wild-type and mutant enzymes
-
-
?
additional information
?
-
-
substrate specificity of recombinant wild-type and mutant enzymes
-
-
?
additional information
?
-
-
substrate specificity of the enzyme in presence or absence of different recombinant peptide ligands, overview
-
-
?
additional information
?
-
-
less than 8% activity with D-mannitol, D-sorbitol, D-trehalose, D-arabinose, D-glucose 6-phosphate, methal-alpha-D-glucopyranose, D-mannose, sucrose, D-maltose, and D-lactose. No activity with gluconic acid and D-fructose
-
-
?
additional information
?
-
-
less than 8% activity with D-mannitol, D-sorbitol, D-trehalose, D-arabinose, D-glucose 6-phosphate, methal-alpha-D-glucopyranose, D-mannose, sucrose, D-maltose, and D-lactose. No activity with gluconic acid and D-fructose
-
-
?
additional information
?
-
-
the enzyme catalyzes only oxidation of D-aldoses and aldose derivatives
-
-
?
additional information
?
-
-
activity of the enzyme is regulated by both the glucose dehydrogenase apo-enzyme synthesis and the synthesis of the cofactor pyrroloquinoline quinone
-
-
?
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1.6
2,6-dichlorophenolindophenol
-
pH 8.8, 25°C
9.5
2-amino-D-glucose
-
wild-type enzyme
0.000004 - 90
2-deoxy-D-glucose
10.8
3-deoxy-D-glucose
-
wild-type enzyme
2 - 198
3-O-methyl-D-glucose
0.73 - 2.43
4-(4-ferrocenylimino-methyl)phenol
0.89 - 2.73
4-ferrocenylnitrophenol
0.83 - 1
4-ferrocenylphenol
1.3
6-deoxy-D-glucose
-
wild-type enzyme
0.00019 - 0.00065
alpha-D-lactose
0.00007 - 0.0003
D-cellobiose
390
D-fructose
in 50 mM Bis-Tris propane (pH 8.0), at 50°C
0.00011 - 390
D-galactose
0.00008
D-glucose 6-phosphate
pH 7.5, 70°C, wild-type enzyme
17.7
D-melibiose
-
wild-type enzyme
0.00018
ethanol
pH 7.5, 70°C, wild-type enzyme
0.69
ferricyanide
-
pH 8.8, 25°C
100
L-Lyxose
-
wild-type enzyme
0.00013 - 150
maltotriose
0.00009
mannitol
pH 7.5, 70°C, wild-type enzyme
0.00015
methanol
pH 7.5, 70°C, wild-type enzyme
0.56
N,N,N,N-tetramethyl-o-phenylenediamine
-
pH 8.8, 25°C
0.268 - 0.292
N-ethylphenazonium ethyl sulfate
0.064 - 0.4
N-methylphenazonium methyl sulfate
0.074 - 1.9
phenazine methosulfate
0.00011
pyrroliquinoline quinone
-
pH 7.0, 25°C, wild-type enzyme
0.00005 - 0.78
pyrroloquinoline quinone
0.83
sucrose
pH 5.5, 30°C
0.0001 - 0.00113
ubiquinone
0.06 - 0.178
ubiquinone Q1
0.012 - 0.061
ubiquinone Q2
0.028 - 0.031
ubiquinone Q4
0.0034 - 0.019
ubiquinone Q6
0.0044
ubiquinone Q9
-
membrane-bound enzyme form
0.00009
xylitol
pH 7.5, 70°C, wild-type enzyme
additional information
additional information
-
0.000004
2-deoxy-D-glucose
pH 7.5, 70°C, wild-type enzyme
0.00008
2-deoxy-D-glucose
pH 7.5, 70°C, mutant enzyme Y156A
0.00014
2-deoxy-D-glucose
pH 7.5, 70°C, mutant enzyme Y156K
0.5
2-deoxy-D-glucose
-
at pH 7.0 and 25°C
1.6
2-deoxy-D-glucose
-
wild-type enzyme
3.5
2-deoxy-D-glucose
recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C
13.6
2-deoxy-D-glucose
-
-
22
2-deoxy-D-glucose
-
pH 8.5, reaction with N-methylphenazonium methyl sulfate as electron acceptor
32
2-deoxy-D-glucose
-
mutant enzyme H262
88
2-deoxy-D-glucose
-
pH 7.0, mutant enzyme E277K
90
2-deoxy-D-glucose
-
pH 7.0, wild-type enzyme
2 - 3
3-O-methyl-D-glucose
-
recombinant Arg-tagged enzyme, pH 7.0
22
3-O-methyl-D-glucose
-
recombinant chimeric mutant enzyme, pH 7.0
27
3-O-methyl-D-glucose
-
pH 7.0, mutant enzyme E277K
27.6
3-O-methyl-D-glucose
-
N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C
27.6
3-O-methyl-D-glucose
recombinant mutant N452T, pH 7.0
28.7
3-O-methyl-D-glucose
recombinant wild-type isozyme PQQGDH-B, pH 7.0
28.7
3-O-methyl-D-glucose
-
wild-type isozyme PQQGDH-B, pH 7.0, 25°C
28.8
3-O-methyl-D-glucose
-
N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C
41
3-O-methyl-D-glucose
recombinant wild-type enzyme, pH 7.0, 25°C
46
3-O-methyl-D-glucose
-
pH 7.0, wild-type enzyme
53
3-O-methyl-D-glucose
recombinant tagged enzyme, pH 7.0, 25°C
56
3-O-methyl-D-glucose
recombinant triple mutant enzyme, pH 7.0, 25°C
79
3-O-methyl-D-glucose
-
wild-type enzyme
79
3-O-methyl-D-glucose
recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C
99
3-O-methyl-D-glucose
recombinant mutant D167E, pH 7.0
198
3-O-methyl-D-glucose
recombinant mutant D167E/N452T, pH 7.0
0.73
4-(4-ferrocenylimino-methyl)phenol
-
s-GDH
2.43
4-(4-ferrocenylimino-methyl)phenol
-
m-GDH
0.89
4-ferrocenylnitrophenol
-
s-GDH
2.73
4-ferrocenylnitrophenol
-
m-GDH
0.83
4-ferrocenylphenol
-
m-GDH
1
4-ferrocenylphenol
-
s-GDH
21
allose
-
pH 7.0, mutant enzyme E277K
32.5
allose
-
N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C
34
allose
-
recombinant Arg-tagged enzyme, pH 7.0
35.5
allose
recombinant wild-type isozyme PQQGDH-B, pH 7.0
35.5
allose
-
wild-type isozyme PQQGDH-B, pH 7.0, 25°C
36
allose
-
recombinant chimeric mutant enzyme, pH 7.0
38.7
allose
-
N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C
38.7
allose
recombinant mutant N452T, pH 7.0
63
allose
recombinant wild-type enzyme, pH 7.0, 25°C
75
allose
recombinant tagged enzyme, pH 7.0, 25°C
76
allose
recombinant triple mutant enzyme, pH 7.0, 25°C
182
allose
recombinant mutant D167E/N452T, pH 7.0
199
allose
recombinant mutant D167E, pH 7.0
0.00019
alpha-D-lactose
pH 7.5, 70°C, wild-type enzyme
0.00064
alpha-D-lactose
pH 7.5, 70°C, mutant enzyme Y156A
0.00065
alpha-D-lactose
pH 7.5, 70°C, mutant enzyme Y156K
0.54
cellobiose
pH 5.5, 30°C
14
cellobiose
recombinant wild-type isozyme PQQGDH-B and mutant N452T, pH 7.0
16
cellobiose
recombinant mutant D167E/N452T, pH 7.0
17
cellobiose
recombinant mutant D167E, pH 7.0
1.5
D-allose
-
-
2.5
D-allose
-
wild-type enzyme
29
D-allose
-
pH 7.0, wild-type enzyme
810
D-allose
-
mutant enzyme H262Y
0.00007
D-cellobiose
pH 7.5, 70°C, wild-type enzyme
0.00023
D-cellobiose
pH 7.5, 70°C, mutant enzyme Y156K
0.0003
D-cellobiose
pH 7.5, 70°C, mutant enzyme Y156A
5
D-fucose
-
pH 8.5, reaction with N-ethylphenazonium ethyl sulfate as electron acceptor
8.3
D-fucose
-
wild-type enzyme
12
D-fucose
-
pH 8.5, reaction with N-methylphenazonium methyl sulfate as electron acceptor
0.00011
D-galactose
pH 7.5, 70°C, wild-type enzyme
0.0002
D-galactose
pH 7.5, 70°C, mutant enzyme Y156K
0.00038
D-galactose
pH 7.5, 70°C, mutant enzyme Y156A
0.46
D-galactose
-
at pH 5.0 and 45°C
0.6
D-galactose
pH 5.5, 30°C
2
D-galactose
recombinant wild-type enzyme, pH 7.0, 25°C
2.7
D-galactose
-
N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C
3.7
D-galactose
-
N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C
3.7
D-galactose
recombinant mutant N452T, pH 7.0
4
D-galactose
recombinant tagged enzyme, pH 7.0, 25°C
5
D-galactose
recombinant triple mutant enzyme, pH 7.0, 25°C
5.3
D-galactose
recombinant wild-type isozyme PQQGDH-B, pH 7.0
5.3
D-galactose
-
wild-type isozyme PQQGDH-B, pH 7.0, 25°C
6.8
D-galactose
-
pH 7.0, wild-type enzyme and mutant enzyme E277K
8
D-galactose
-
recombinant Arg-tagged enzyme, pH 7.0
9
D-galactose
-
recombinant chimeric mutant enzyme, pH 7.0
17.5
D-galactose
recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C
19
D-galactose
-
pH 8.5, reaction with N-methylphenazonium methyl sulfate as electron acceptor
39
D-galactose
-
wild-type enzyme
40
D-galactose
-
at pH 7.0 and 25°C
145
D-galactose
recombinant mutant D167E/N452T, pH 7.0
390
D-galactose
in 50 mM Bis-Tris propane (pH 8.0), at 50°C
0.00002
D-glucosamine
pH 7.5, 70°C, wild-type enzyme
0.00002
D-glucosamine
pH 7.5, 70°C, mutant enzyme Y156A
0.00002
D-glucosamine
pH 7.5, 70°C, mutant enzyme Y156K
0.00021
D-glucose
pH 7.5, 70°C, wild-type enzyme
0.00025
D-glucose
pH 7.5, 70°C, mutant enzyme Y156K
0.00047
D-glucose
pH 7.5, 70°C, mutant enzyme Y156A
0.1
D-glucose
-
at pH 7.0 and 25°C
0.21
D-glucose
-
at pH 5.0 and 45°C
0.23
D-glucose
-
pH 8.5, reaction with 2,6-dichlorophenolindophenol as electron acceptor
0.3
D-glucose
-
pH 7.0, mutant enzyme E277G
0.41
D-glucose
pH 5.5, 30°C
0.47
D-glucose
-
pH 6.0, 25°C, reaction with 2,6-dichlorophenolindophenol
0.8
D-glucose
-
pH 7.0, 25°C, mutant enzyme N607A
0.8
D-glucose
-
25°C, mutant enzyme D730 N
0.9
D-glucose
-
pH 7.0, 25°C, wild-type enzyme
0.91
D-glucose
-
25°C, wild-type enzyme
0.95
D-glucose
-
wild-type enzyme
0.98
D-glucose
-
C-terminal periplasmic domain of glucose dehydrogenase
1
D-glucose
-
25°C, mutant enzyme S357L
1.2
D-glucose
-
pH 7.0, 25°C, mutant W404A
1.2
D-glucose
-
mutant E277N
1.3
D-glucose
-
25°C, mutant enzyme H775R
1.4
D-glucose
-
25°C, mutant enzyme G689D
1.4
D-glucose
-
pH 7.0, 25°C, mutant K493A
1.5
D-glucose
-
pH 7.0, 25°C, mutant K493R
1.5
D-glucose
-
mutant enzyme E277A
2
D-glucose
-
pH 7.0, 21°C, mutant W404F
2 - 3
D-glucose
-
recombinant Arg-tagged enzyme, pH 7.0
2 - 3
D-glucose
-
recombinant cytochrome c-fusion protein, pH 7.0
2.1
D-glucose
-
wild-type enzyme
2.4
D-glucose
-
wild type enzyme, in 42 mM sodium phosphate buffer pH 7.5 at 37°C
2.5
D-glucose
-
pH 7.0, mutant enzyme E277V
2.71
D-glucose
-
recombinant enzyme, at pH 7.5 and 28°C
2.8
D-glucose
recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C
3
D-glucose
-
pH 7.0, 25°C, mutant D466E
4
D-glucose
-
pH 8.5, reaction with N-methylphenazonium methyl sulfate or N-ethylphenazonium ethal sulfate as electron acceptor
4.2
D-glucose
-
membrane-bound enzyme form
4.3
D-glucose
-
pH 7.0, mutant enzyme E277Q
4.91
D-glucose
-
native enzyme, at pH 7.5 and 28°C
5.9
D-glucose
-
pH 8.5, reaction with Wurster Blue as electron acceptor
5.9
D-glucose
-
recombinant Strep-tagged enzyme, pH 6.0, 25°C
7
D-glucose
-
pH 7.0, mutant enzyme I278F
7.2
D-glucose
-
mutant enzyme Q219K/F220C, in 42 mM sodium phosphate buffer pH 7.5 at 37°C
7.4
D-glucose
-
pH 7.0, mutant enzyme E277D
7.6
D-glucose
-
mutant enzyme Q219K/F220K, in 42 mM sodium phosphate buffer pH 7.5 at 37°C
7.7
D-glucose
-
pH 7.0, mutant enzyme E277H
8.8
D-glucose
-
pH 7.0, mutant enzyme E277K
8.9
D-glucose
-
pH 7.0, mutant enzyme E277K
10
D-glucose
-
pH 7.0, 25°C, mutant H262A
10.6
D-glucose
-
mutant enzyme Q219N/F220K, in 42 mM sodium phosphate buffer pH 7.5 at 37°C
11
D-glucose
-
mutant enzyme Q126E, in 42 mM sodium phosphate buffer pH 7.5 at 37°C
11.3
D-glucose
-
mutant enzyme Q219E/F220E, in 42 mM sodium phosphate buffer pH 7.5 at 37°C
12
D-glucose
-
pH 7.0, 25°C, mutant D466N
12.3
D-glucose
-
N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C
12.5
D-glucose
-
N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C
12.5
D-glucose
recombinant mutant N452T, pH 7.0
15.7
D-glucose
-
pH 7.0, mutant enzyme N279H
16
D-glucose
recombinant mutant T416V/T417V, pH 7.0, 25°C
20
D-glucose
-
pH 7.0, 25°C, linked dimeric enzyme
20
D-glucose
recombinant wild-type enzyme and mutants N340F/Y418F and N340F/Y418I, pH 7.0, 25°C
22
D-glucose
-
recombinant chimeric mutant enzyme, pH 7.0
22.6
D-glucose
-
mutant enzyme Q126S, in 42 mM sodium phosphate buffer pH 7.5 at 37°C
24
D-glucose
-
pH 7.0, mutant enzyme D275E and D276E
24.5
D-glucose
-
soluble enzyme
25
D-glucose
recombinant triple mutant enzyme, pH 7.0, 25°C
25
D-glucose
recombinant wild-type isozyme PQQGDH-B, pH 7.0
25
D-glucose
-
wild-type isozyme PQQGDH-B, pH 7.0, 25°C
26
D-glucose
-
pH 7.0, wild-type enzyme
27
D-glucose
recombinant wild-type enzyme and tagged enzyme, pH 7.0, 25°C
41.4
D-glucose
-
mutant enzyme Q126R, in 42 mM sodium phosphate buffer pH 7.5 at 37°C
48
D-glucose
recombinant mutant D167E/N452T, pH 7.0
55
D-glucose
recombinant mutant D167E, pH 7.0
154
D-glucose
recombinant mutant H168Q, pH 7.0
193
D-glucose
recombinant mutant H168C, pH 7.0
460
D-glucose
-
mutant enzyme H262Y
680
D-glucose
in 50 mM Bis-Tris propane (pH 8.0), at 50°C
0.00013
D-mannose
pH 7.5, 70°C, wild-type enzyme
0.00014
D-mannose
pH 7.5, 70°C, mutant enzyme Y156A
0.00016
D-mannose
pH 7.5, 70°C, mutant enzyme Y156K
22
D-mannose
-
pH 7.0, wild-type enzyme and mutant enzyme E277K
78
D-mannose
-
wild-type enzyme
116
D-mannose
recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C
910
D-mannose
in 50 mM Bis-Tris propane (pH 8.0), at 50°C
0.00007
D-ribose
pH 7.5, 70°C, mutant enzyme Y156A
0.00013
D-ribose
pH 7.5, 70°C, wild-type enzyme
0.00044
D-ribose
pH 7.5, 70°C, mutant enzyme Y156K
110
D-ribose
-
wild-type enzyme
166
D-ribose
recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C
0.00014
D-xylose
pH 7.5, 70°C, wild-type enzyme
0.00023
D-xylose
pH 7.5, 70°C, mutant enzyme Y156K
0.00046
D-xylose
pH 7.5, 70°C, mutant enzyme Y156A
0.34
D-xylose
-
at pH 5.0 and 45°C
0.67
D-xylose
pH 5.5, 30°C
7
D-xylose
-
pH 8.5, reaction with N-ethylphenazonium ethyl sulfate as electron acceptor
12
D-xylose
-
pH 8.5, reaction with N-methylphenazonium methyl sulfate as electron acceptor
14.3
D-xylose
-
pH 7.0, wild-type enzyme
17
D-xylose
recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C
22
D-xylose
-
wild-type enzyme
34
D-xylose
-
pH 7.0, mutant enzyme E277K
500
D-xylose
in 50 mM Bis-Tris propane (pH 8.0), at 50°C
0.00014
L-arabinose
pH 7.5, 70°C, mutant enzyme Y156K
0.00016
L-arabinose
pH 7.5, 70°C, wild-type enzyme
0.00017
L-arabinose
pH 7.5, 70°C, mutant enzyme Y156A
0.118
L-arabinose
-
pH 8.5, reaction with D-glucose
18
L-arabinose
-
pH 8.5, reaction with N-methylphenazonium methyl sulfate as electron acceptor
19
L-arabinose
-
pH 8.5, reaction with N-ethylphenazonium ethyl sulfate as electron acceptor
31
L-arabinose
recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C
46
L-arabinose
-
wild-type enzyme
0.63
lactose
pH 5.5, 30°C
7.5
lactose
-
pH 7.0, mutant enzyme E277K
12
lactose
-
pH 7.0, 25°C, linked dimeric enzyme
14.3
lactose
-
pH 7.0, wild-type enzyme
18
lactose
-
N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C
18.9
lactose
recombinant wild-type isozyme PQQGDH-B, pH 7.0
18.9
lactose
-
wild-type isozyme PQQGDH-B, pH 7.0, 25°C
19
lactose
-
recombinant cytochrome c-fusion protein, pH 7.0
20
lactose
-
recombinant Arg-tagged enzyme, and recombinant chimeric mutant enzyme, pH 7.0
25
lactose
recombinant wild-type enzyme, pH 7.0, 25°C
26
lactose
recombinant tagged enzyme, pH 7.0, 25°C
26.7
lactose
-
soluble enzyme
33.6
lactose
-
N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C
33.6
lactose
recombinant mutant N452T, pH 7.0
36
lactose
recombinant triple mutant enzyme, pH 7.0, 25°C
55
lactose
recombinant mutant D167E/N452T, pH 7.0
77
lactose
recombinant mutant D167E, pH 7.0
0.00017
maltose
pH 7.5, 70°C, wild-type enzyme
0.00026
maltose
pH 7.5, 70°C, mutant enzyme Y156K
0.00037
maltose
pH 7.5, 70°C, mutant enzyme Y156A
0.46
maltose
pH 5.5, 30°C
0.59
maltose
-
at pH 5.0 and 45°C
10
maltose
recombinant wild-type enzyme, pH 7.0, 25°C
11
maltose
recombinant tagged enzyme, pH 7.0, 25°C
13
maltose
-
recombinant chimeric mutant enzyme, pH 7.0
13
maltose
recombinant triple mutant enzyme, pH 7.0, 25°C
14
maltose
-
recombinant Arg-tagged enzyme, pH 7.0
14.3
maltose
-
pH 7.0, mutant enzyme E277K
15
maltose
-
recombinant cytochrome c-fusion protein, pH 7.0
16
maltose
-
N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C
16
maltose
recombinant mutant D167E/N452T, pH 7.0
26
maltose
recombinant wild-type isozyme PQQGDH-B, pH 7.0
26
maltose
-
wild-type isozyme PQQGDH-B, pH 7.0, 25°C
30.9
maltose
-
pH 7.0, wild-type enzyme
46.5
maltose
-
N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C
46.5
maltose
recombinant mutant N452T, pH 7.0
156
maltose
recombinant mutant D167E, pH 7.0
600
maltose
in 50 mM Bis-Tris propane (pH 8.0), at 50°C
0.00013
maltotriose
pH 7.5, 70°C, wild-type enzyme
0.00016
maltotriose
pH 7.5, 70°C, mutant enzyme Y156K
0.0006
maltotriose
pH 7.5, 70°C, mutant enzyme Y156A
0.268
N-ethylphenazonium ethyl sulfate
-
pH 8.5, reaction with D-xylose
0.278
N-ethylphenazonium ethyl sulfate
-
pH 8.5, reaction with D-glucose
0.291
N-ethylphenazonium ethyl sulfate
-
pH 8.5, reaction with D-fucose
0.292
N-ethylphenazonium ethyl sulfate
-
pH 8.5, reaction with L-arabinose
0.064
N-methylphenazonium methyl sulfate
-
pH 8.5, reaction with D-galactose
0.156
N-methylphenazonium methyl sulfate
-
pH 8.5, reaction with D-xylose
0.178
N-methylphenazonium methyl sulfate
-
pH 8.5, reaction with D-glucose
0.22
N-methylphenazonium methyl sulfate
-
pH 8.5, reaction with D-fucose
0.362
N-methylphenazonium methyl sulfate
-
pH 8.5, reaction with 2-deoxy-D-glucose
0.4
N-methylphenazonium methyl sulfate
-
with D-glucose as cosubstrate, at pH 5.0 and 45°C
0.074
phenazine methosulfate
-
membrane-bound enzyme form
0.13
phenazine methosulfate
-
pH 8.8, 25°C
1.9
phenazine methosulfate
-
soluble enzyme form
0.00005
pyrroloquinoline quinone
-
,pH 7.0, 25°C, mutant K493A
0.00009
pyrroloquinoline quinone
-
25°C, wild-type enzyme
0.00012
pyrroloquinoline quinone
-
C-terminal periplasmic domain of glucose dehydrogenase
0.00012
pyrroloquinoline quinone
-
25°C, mutant enzyme D730N
0.00014
pyrroloquinoline quinone
-
pH 7.0, 21°C, mutant D466E and D466N
0.00022
pyrroloquinoline quinone
-
pH 7.0, 25°C, mutant W607A
0.0005
pyrroloquinoline quinone
-
25°C, mutant enzyme S357L
0.00064
pyrroloquinoline quinone
-
25°C, mutant enzyme G689D
0.00088
pyrroloquinoline quinone
-
pH 7.0, 25°C, mutant H262A
0.006
pyrroloquinoline quinone
-
pH 7.0, 25°C, mutant W404A
0.016
pyrroloquinoline quinone
-
pH 7.0, 25°C, mutant K493R
0.02
pyrroloquinoline quinone
-
pH 7.0, 25°C, mutant W404F
0.021
pyrroloquinoline quinone
-
25°C, mutant enzyme H775R
0.12
pyrroloquinoline quinone
-
-
0.78
pyrroloquinoline quinone
-
-
0.0001
ubiquinone
-
Km below 0.0002 mM, native enzyme, at pH 7.5 and 28°C
0.00113
ubiquinone
-
recombinant enzyme, at pH 7.5 and 28°C
0.06
ubiquinone Q1
-
pH 8.8, 25°C
0.148
ubiquinone Q1
-
membrane-bound enzyme form
0.178
ubiquinone Q1
-
soluble enzyme form
0.012
ubiquinone Q2
-
membrane-bound enzyme form
0.0177
ubiquinone Q2
-
soluble enzyme form
0.025
ubiquinone Q2
-
wild-type enzyme
0.03
ubiquinone Q2
-
C-terminal periplasmic domain of glucose dehydrogenase
0.04
ubiquinone Q2
-
pH 6.5, 25°C
0.061
ubiquinone Q2
-
pH 8.8, 25°C
0.028
ubiquinone Q4
-
pH 6.5, 25°C
0.031
ubiquinone Q4
-
pH 8.8, 25°C
0.0034
ubiquinone Q6
-
membrane-bound enzyme form
0.0097
ubiquinone Q6
-
pH 8.8, 25°C
0.019
ubiquinone Q6
-
pH 6.5, 25°C
additional information
additional information
kinetics
-
additional information
additional information
-
electrochemical data and kinetics for quinone derivatives as redocx mediators
-
additional information
additional information
-
kinetic study, enzyme follows Michaelis-Menten kinetics using artificial electron transfer mediator system based on ruthenium(III) compounds for activity assays
-
additional information
additional information
-
kinetics, cooperativity in the recombinant chimeric mutant enzyme which possesses only 1 active subunit derived from the wild-type enzyme
-
additional information
additional information
metal binding kinetics, wild-type and mutant enzymes, Km for the different substrates of mutant enzymes with different metal ions bound, overview
-
additional information
additional information
-
metal binding kinetics, wild-type and mutant enzymes, Km for the different substrates of mutant enzymes with different metal ions bound, overview
-
additional information
additional information
predicted binding energy of wild-type and mutant enzymes
-
additional information
additional information
-
predicted binding energy of wild-type and mutant enzymes
-
additional information
additional information
-
detailed kinetic analysis of wild-type and mutant enzymes, substrate inhibition and cooperativity effects, overview
-
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A71P/N454S
mutant, relative activity vs wild type, substrate glucose 0.95, substrate maltose 0.75
A98G/K126R/L445I/N454S
mutant, relative activity vs wild type, substrate glucose 1.00, substrate maltose 0.78
D167A
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167C
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167E
site-directed mutagenesis, substrate binding residue mutation, slightly reduced activity compared to the wild-type enzyme
D167E/N452T
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
D167G
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167H
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167K
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167N
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167Q
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167R
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167S
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167V
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167W
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167Y
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D276E
-
drastic decrease in EDTA tolerance
E277A
-
decreased Km value for glucose and altered substrate specificity, thermal stability is less than 20% of that of the wild-type enzyme
E277D
-
decreased Km value for glucose and altered substrate specificity, thermal stability is less than 20% of that of the wild-type enzyme
E277G
-
drastic decrease in EDTA tolerance
E277H
-
decreased Km values for glucose and altered substrate specificity, thermal stability is less than 20% of that of the wild-type enzyme
E277K
-
decreased Km value for glucose and altered substrate specificity, significantly increased catalytic efficiency compared with the wild-type enzyme
E277N
-
decreased Km values for glucose and altered substrate specificity, thermal stability is less than 20% of that of the wild-type enzyme
E277Q
-
decreased Km values for glucose and altered substrate specificity, thermal stability is less than 20% of that of the wild-type enzyme
E277V
-
decreased Km values for glucose and altered substrate specificity, thermal stability is less than 20% of that of the wild-type enzyme
G100R
mutant, relative activity vs wild type, substrate glucose 0.35, substrate maltose 0.26
G100W/G320E/M367P/A376T
mutant, relative activity vs wild type, substrate glucose 0.55, substrate maltose 0.20
G320E
mutant, relative activity vs wild type, substrate glucose 0.92, substrate maltose 0.70
G320E/M367P/A376T
mutant, relative activity vs wild type, substrate glucose 0.69, substrate maltose 0.25
G320F/M367P/A376T
mutant, relative activity vs wild type, substrate glucose 0.48, substrate maltose 0.17
G320Y/M367P/A376T
mutant, relative activity vs wild type, substrate glucose 0.49, substrate maltose 0.16
H168C
site-directed mutagenesis, catalytic residue mutation, highly reduced activity compared to the wild-type enzyme
K166E
site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme
K166G
site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme
K166I
site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme
K3E/E278G/G392C
mutant, relative activity vs wild type, substrate glucose 0.92, substrate maltose 0.53
L194F/A376T
mutant, relative activity vs wild type, substrate glucose 0.39, substrate maltose 0.075
L194F/G320E/M367P
mutant, relative activity vs wild type, substrate glucose 0.38, substrate maltose 0.14
L194F/G320E/M367P/A376T
mutant, relative activity vs wild type, substrate glucose 0.36, substrate maltose 0.051
L194F/G320F
mutant, relative activity vs wild type, substrate glucose 0.38, substrate maltose 0.060
L194Q
mutant, relative activity vs wild type, substrate glucose 0.22, substrate maltose 0.15
M367P/A376T
mutant, relative activity vs wild type, substrate glucose 0.65, substrate maltose 0.24
N275E
-
drastic decrease in EDTA tolerance
N340F/Y418F
site-directed mutagenesis, mutation of residues at the dimer interface, 2fold increased thermal stability at 55°C and unaltered catalytic efficiency compared to the wild-type enzyme
N340F/Y418I
site-directed mutagenesis, mutation of residues at the dimer interface, 2fold increased thermal stability at 55°C and unaltered catalytic efficiency compared to the wild-type enzyme
N428C
-
site-directed mutagenesis, at relatively high concentrations of mediator and substrate, catalysis by the mutant type may be more efficient than with the wild-type
N452T
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
N454S
mutant, relative activity vs wild type, substrate glucose 0.87, substrate maltose 0.69
Q169E
site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme
Q169K
site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme
Q193H
mutant, relative activity vs wild type, substrate glucose 0.41, substrate maltose 0.23
Q193S/G320E
mutant, relative activity vs wild type, substrate glucose 0.56, substrate maltose 0.19
Q209R/N240R/T389R
site-directed mutagenesis, increased thermal stability compared to the wild-type enzyme
S231C
-
increase in thermal stability
S231D
-
increase in thermal stability
S231H
-
increase in thermal stability
S231K
-
more than 8fold increase in its half-life during the thermal inactivation at 55 C compared with the wild-type enzyme, retains catalytic activity similar to the wild-type enzyme
S231L
-
increase in thermal stability
S231M
-
increase in thermal stability
S231N
-
increase in thermal stability
T348G
-
mutant crystallized by microseeding, data set is collected at 2.36 A resolution
T348G/N428P
-
mutant crystallized by microseeding, data set is collected at 2.15 A resolution
T416V/T417V
site-directed mutagenesis, mutation of resides of the hydrophobic region, 2fold increased thermal stability at 55°C and unaltered catalytic efficiency compared to the wild-type enzyme
V157I/M367V/T463S
mutant, relative activity vs wild type, substrate glucose 1.00, substrate maltose 0.78
V91A/W372R
mutant, relative activity vs wild type, substrate glucose 0.44, substrate maltose 0.22
Y171G/E245D/M341V/T348G/N428P
-
mutant crystallized by microseeding, data set is collected at 2.20 A resolution
Y248F/N342D/A376T/A418V
mutant, relative activity vs wild type, substrate glucose 0.74, substrate maltose 0.43
Y302H
mutant, relative activity vs wild type, substrate glucose 0.47, substrate maltose 0.35
D354N/N355D
site-directed mutagenesis, 10% of wild-type activity, mutant enzyme can be reconstituted with PQQ and Ca2+, Sr2+, or Ba2+, but not with Mg2+, which functions as a competitive inhibitor, in contrary to the wild-type enzyme
D448N
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
D456N
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
D457N
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
D730A
-
low glucose oxidase activity without influence on the affinity for pyrroloquinoline quinone, Mg2+ or substrate
D730N
-
low glucose oxidase activity without influence on the affinity for pyrroloquinoline quinone, Mg2+ or substrate
D730R
-
reduced affnity for pyrroloquinoline quinone
E217Q
-
the mutant retains its function similar to that of wild type GDH
E742G/P757L
-
slightly higher Km value for Mg2+
G689D
-
significantly increased Km for pyrroloquinoline quinone, slightly higher Km value for Mg2+
G776A
-
the mutant retains its function similar to that of wild type GDH
H262A
-
reduced affinity both for glucose, 11fold, and pyrroloquinoline quinone, 8fold, without significant effect on glucose oxidase activity
H262Y
-
greatly diminished catalytic efficiency for all substrates, rate of electron transfer to oxygen is unaffected, 230fold increased Km value for glucose
H775A
-
pronounced reduction of affinity for the prosthetic group pyrroloquinoline quinone
H775R
-
pronounced reduction of affinity for the prosthetic group pyrroloquinoline quinone, 230fold higher Km than wild-type enzyme
N355D
site-directed mutagenesis, 25% of wild-type activity, mutant enzyme can be reconstituted with PQQ and Ca2+, Sr2+, or Ba2+, but not with Mg2+, which functions as a competitive inhibitor, in contrary to the wild-type enzyme
N452D
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
N452H
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
N452I
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
N452K
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
N452T
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows narrowed substrate specificity, but unaltered catalytic efficiency, thermal stability, and EDTA tolerance compared to the wild-type isozyme PQQGDH-B
N462D
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
N462H
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
N462K
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
N462Y
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
S145C
-
site-directed mutagenesis, introduction of a Cys residue in each monomer of the enzyme leads to formation of an intersubunit disulfide bridge at the dimer interface resulting in 30fold increased thermal stability at 55°C compared to the wild-type enzyme
S357L
-
significantly increased Km for pyrroloquinoline quinone, slightly higher Km value for Mg2+
W404A
-
pronounced reduction of affinity for pyrroloquinoline quinone, very low glucose oxidase activity and phenazine methosulfate reductase activity compared with wild-type enzyme
W404F
-
pronounced reduction of affinity for pyrroloquinoline quinone, very weak activity of phenazine methosulfate reductase but still retains glucose oxidase activity equivalent to that of the wild-type
D354N
-
mutant retains a conformation almost unaltered compared to the wild type mGDH and strongly reduced activity
-
D466E
-
mutant shows no significant difference in molecular structure from that of the wild type mGDH but has remarkably reduced content of bound ubiquinone and less than 0.04% activity compared to the wild type enzyme
-
D466N
-
mutant shows no significant difference in molecular structure from that of the wild type mGDH but has remarkably reduced content of bound ubiquinone and less than 0.04% activity compared to the wild type enzyme
-
K493A
-
mutant shows no significant difference in molecular structure from that of the wild type mGDH but has remarkably reduced content of bound ubiquinone and less than 0.04% activity compared to the wild type enzyme
-
K493R
-
mutant retains a conformation almost unaltered compared to the wild type mGDH, the rate of ubiquinone to pyrroloquinoline electron transfer is about 4fold slower than that of the wild type enzyme, shows less than 0.04% activity compared to the wild type enzyme
-
Q126E
-
the mutant shows 25.6% relative activity on maltose
Q126R
-
the mutant shows 11.4% relative activity on maltose
Q126S
-
the mutant shows 12.4% relative activity on maltose
Q219E/F220E
-
the mutant shows 5.2% relative activity on maltose
Q219K/F220C
-
the mutant shows 20% relative activity on maltose
Q219K/F220K
-
the mutant shows 29.3% relative activity on maltose
Q219N/F220K
-
the mutant shows 11.7% relative activity on maltose
Q126E
-
the mutant shows 25.6% relative activity on maltose
-
Q126R
-
the mutant shows 11.4% relative activity on maltose
-
Q126S
-
the mutant shows 12.4% relative activity on maltose
-
Q219E/F220E
-
the mutant shows 5.2% relative activity on maltose
-
Q219K/F220K
-
the mutant shows 29.3% relative activity on maltose
-
Y156A
impaired activities and affinities for all substrates and completely loses the activity for alcohols. The catalytic efficiency of the Y156A mutant is lower than that of the Y156K mutant for most substrates
Y156K
impaired activities and affinities for all substrates and completely loses the activity for alcohols. The catalytic efficiency of the Y156A mutant is lower than that of the Y156K mutant for most substrates
Y156A
-
impaired activities and affinities for all substrates and completely loses the activity for alcohols. The catalytic efficiency of the Y156A mutant is lower than that of the Y156K mutant for most substrates
-
Y156K
-
impaired activities and affinities for all substrates and completely loses the activity for alcohols. The catalytic efficiency of the Y156A mutant is lower than that of the Y156K mutant for most substrates
-
G320D/M367P/A376T
mutant, relative activity vs wild type, substrate glucose 0.51, substrate maltose 0.16
G320D/M367P/A376T
mutant, relative activity vs wild type, substrate glucose 0.69, substrate maltose 0.24
H168Q
site-directed mutagenesis, catalytic residue mutation, nearly inactive mutant
H168Q
-
site-directed mutagenesis, inactive mutant, a heterodimeric chimeric enzyme consisiting of 1 wild-type subunit and 1 mutant subunit shows decreased activity and a substrate specificity similar to the wild-type enzyme
D354N
site-directed mutagenesis, 9% of wild-type activity, mutant enzyme can be reconstituted with PQQ and Ca2+, Sr2+, or Ba2+, but not with Mg2+, which functions as a competitive inhibitor, in contrary to the wild-type enzyme
D354N
-
mutant retains a conformation almost unaltered compared to the wild type mGDH and strongly reduced activity
D466E
-
very low glucose oxidase activity without influence on the affinity for pyrroloquinoline quinone, very low activity with ubiquinone Q2 compared with the wild-type enzyme
D466E
-
mutant shows no significant difference in molecular structure from that of the wild type mGDH but has remarkably reduced content of bound ubiquinone and less than 0.04% activity compared to the wild type enzyme
D466N
-
very low glucose oxidase activity without influence on the affinity for pyrroloquinoline quinone
D466N
-
mutant shows no significant difference in molecular structure from that of the wild type mGDH but has remarkably reduced content of bound ubiquinone and less than 0.04% activity compared to the wild type enzyme
K493A
-
very low glucose oxidase activity, without influence on the affinity for pyrroloquinoline quinone, very low activity with ubiquinone Q2 compared with the wild-type enzyme, very low activity of both phenazine methosulfate reductase and glucose oxidase in the membrane fractions compared with the wild type
K493A
-
mutant shows no significant difference in molecular structure from that of the wild type mGDH but has remarkably reduced content of bound ubiquinone and less than 0.04% activity compared to the wild type enzyme
K493R
-
pronounced reduction of affinity for pyrroloquinoline quinone, very low activity of both phenazine methosulfate reductase and glucose oxidase in the membrane fractions compared with the wild type
K493R
-
mutant retains a conformation almost unaltered compared to the wild type mGDH, the rate of ubiquinone to pyrroloquinoline electron transfer is about 4fold slower than that of the wild type enzyme, shows less than 0.04% activity compared to the wild type enzyme
additional information
-
improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins
additional information
engineering PQQ glucose dehydrogenase with improved substrate specificity
additional information
-
the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview
additional information
-
the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview
-
additional information
-
improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins
additional information
-
construction of a gene consisting of two identical subunits linked together by a DNA segment coding linker peptide region and production of a linked-dimeric enzyme, the linked-dimeric enzyme shows higher thermal stability than native dimeric enzyme
additional information
-
co-expression of peptide ligands in a random phage diplay modifies the substrate specificity of the enzyme towards mono- and disaccharides, overview
additional information
-
studies on mGDH mutants with substitutions for amino acid residues around pyrroloquinoline quinone show that Asp-466 and Lys-493, which are crucial for catalytic activity, interact with bound ubiquinone. It is proposed that the bound ubiquinone is involved in the catalytic reaction in addition to the intramolecular electron transfer in mGDH
additional information
construction of DELTAgcd and DELTApqq mutants. qqqABCDEF is cloned in vivo and integrated into the chromosomes of Pantoea ananatis and Escherichia coli according to the Dual In/Out strategy. Introduction of a second copy of pqqABCDEF to Pantoea ananatis strain SC17(0) doubles the accumulation of PQQ. Integration of the operon into Escherichia coli strain MG1655DptsGDmanXY restores the growth of bacteria on glucose, overview
additional information
-
construction of DELTAgcd and DELTApqq mutants. qqqABCDEF is cloned in vivo and integrated into the chromosomes of Pantoea ananatis and Escherichia coli according to the Dual In/Out strategy. Introduction of a second copy of pqqABCDEF to Pantoea ananatis strain SC17(0) doubles the accumulation of PQQ. Integration of the operon into Escherichia coli strain MG1655DptsGDmanXY restores the growth of bacteria on glucose, overview
additional information
-
construction of DELTAgcd and DELTApqq mutants. qqqABCDEF is cloned in vivo and integrated into the chromosomes of Pantoea ananatis and Escherichia coli according to the Dual In/Out strategy. Introduction of a second copy of pqqABCDEF to Pantoea ananatis strain SC17(0) doubles the accumulation of PQQ. Integration of the operon into Escherichia coli strain MG1655DptsGDmanXY restores the growth of bacteria on glucose, overview
-
additional information
-
complementation of the rig-10 mutant, DELTAcrp gdhS, glucose insensitivity phenotype using the wild-type Serratia marcescens gdhS gene or the Escherichia coli gcd gene expressed from a medium-copy-number plasmid
additional information
-
complementation of the rig-10 mutant, DELTAcrp gdhS, glucose insensitivity phenotype using the wild-type Serratia marcescens gdhS gene or the Escherichia coli gcd gene expressed from a medium-copy-number plasmid
-
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Puehringer, S.; RoseFigura, J.; Metlitzky, M.; Toyama, H.; Klinman, J.P.; Schwarzenbacher, R.
Structural studies of mutant forms of the PQQ-forming enzyme PqqC in the presence of product and substrate
Proteins
78
2554-2562
2010
Klebsiella pneumoniae, Klebsiella pneumoniae MGH 78578
brenda
Sakamoto, H.; Uchii, T.; Yamaguchi, K.; Koto, A.; Takamura, E.; Satomura, T.; Sakuraba, H.; Ohshima, T.; Suye, S.
Construction of a biocathode using the multicopper oxidase from the hyperthermophilic archaeon, Pyrobaculum aerophilum: towards a long-life biobattery
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2015
Pyrobaculum aerophilum (Q8ZUN8), Pyrobaculum aerophilum DSM 7523 (Q8ZUN8)
brenda
Ben Farhat, M.; Fourati, A.; Chouayekh, H.
Coexpression of the pyrroloquinoline quinone and glucose dehydrogenase genes from Serratia marcescens CTM 50650 conferred high mineral phosphate-solubilizing ability to Escherichia coli
Appl. Biochem. Biotechnol.
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1738-1750
2013
Serratia marcescens, Serratia marcescens CTM 50650
brenda
Stredansky, M.; Monosik, R.; Mastihuba, V.; Sturdik, E.
Monitoring of PQQ-dependent glucose dehydrogenase substrate specificity for its potential use in biocatalysis and bioanalysis
Appl. Biochem. Biotechnol.
171
1032-1041
2013
Acinetobacter calcoaceticus
brenda
An, R.; Moe, L.A.
Regulation of pyrroloquinoline quinone-dependent glucose dehydrogenase activity in the model rhizosphere-dwelling bacterium Pseudomonas putida KT2440
Appl. Environ. Microbiol.
82
4955-4964
2016
Pseudomonas putida, Pseudomonas putida KT 2240
brenda
Scherbahn, V.; Putze, M.T.; Dietzel, B.; Heinlein, T.; Schneider, J.J.; Lisdat, F.
Biofuel cells based on direct enzyme-electrode contacts using PQQ-dependent glucose dehydrogenase/bilirubin oxidase and modified carbon nanotube materials
Biosens. Bioelectron.
61
631-638
2014
Acinetobacter calcoaceticus
brenda
Guo, Z.; Johnston, W.A.; Stein, V.; Kalimuthu, P.; Perez-Alcala, S.; Bernhardt, P.V.; Alexandrov, K.
Engineering PQQ-glucose dehydrogenase into an allosteric electrochemical Ca(2+) sensor
Chem. Commun. (Camb.)
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485-488
2016
Acinetobacter calcoaceticus
brenda
Babanova, S.; Matanovic, I.; Atanassov, P.
Quinone-modified surfaces for enhanced enzyme-electrode interactions in pyrroloquinoline-quinone-dependent glucose dehydrogenase anodes
ChemElectroChem
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2017-2028
2014
Acinetobacter calcoaceticus
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brenda
Duine, J.A.; Strampraad, M.J.; Hagen, W.R.; de Vries, S.
The cooperativity effect in the reaction of soluble quinoprotein (PQQ-containing) glucose dehydrogenase is not due to subunit interaction but to substrate-assisted catalysis
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283
3604-3612
2016
Acinetobacter calcoaceticus
brenda
Guo, Z.; Murphy, L.; Stein, V.; Johnston, W.A.; Alcala-Perez, S.; Alexandrov, K.
Engineered PQQ-glucose dehydrogenase as a universal biosensor platform
J. Am. Chem. Soc.
138
10108-10111
2016
Acinetobacter calcoaceticus
brenda
Nakashima, Y.; Mizoshita, N.; Tanaka, H.; Nakaoki, Y.
Amphiphilic polymer mediators promoting electron transfer on bioanodes with PQQ-dependent glucose dehydrogenase
Langmuir
32
12986-12994
2016
Acinetobacter calcoaceticus
brenda
Xue, Q.; Wei, Z.; Sun, W.; Cui, F.; Yu, S.; Zhou, Q.; Liu, J.
2-Keto-D-gluconate-yielding membrane-bound D-glucose dehydrogenase from Arthrobacter globiformis C224: purification and characterization
Molecules
20
846-862
2015
Arthrobacter globiformis, Arthrobacter globiformis C224
brenda
Sara-Paez, M.; Contreras-Zentella, M.; Gomez-Manzo, S.; Gonzalez-Valdez, A.A.; Gasca-Licea, R.; Mendoza-Hernandez, G.; Escamilla, J.E.; Reyes-Vivas, H.
Purification and characterization of the membrane-bound quinoprotein glucose dehydrogenase of Gluconacetobacter diazotrophicus PAL 5
Protein J.
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48-59
2015
Gluconacetobacter diazotrophicus, Gluconacetobacter diazotrophicus PAL 5
brenda
Kim, H.; Wang, J.; Lee, J.; Park, A.; Park, H.; Jeon, S.
Biochemical and structural characterization of quinoprotein aldose sugar dehydrogenase from Thermus thermophilus HJ6 Mutational analysis of Tyr156 in the substrate-binding site
Arch. Biochem. Biophys.
608
20-26
2016
Thermus thermophilus (I7A144), Thermus thermophilus HJ6 (I7A144), Thermus thermophilus HJ6
brenda
Bharwad, K.; Rajkumar, S.
Modulation of PQQ-dependent glucose dehydrogenase (mGDH and sGDH) activity by succinate in phosphate solubilizing plant growth promoting Acinetobacter sp. SK2
3 Biotech
10
5
2020
Acinetobacter sp. SK2
brenda
Lisdat, F.
PQQ-GDH - Structure, function and application in bioelectrochemistry
Bioelectrochemistry
134
107496
2020
Gluconacetobacter diazotrophicus, Acinetobacter calcoaceticus (P13650)
brenda
Oh, Y.R.; Jang, Y.A.; Lee, S.S.; Kim, J.H.; Hong, S.H.; Han, J.J.; Eom, G.T.
Enhancement of lactobionic acid productivity by homologous expression of quinoprotein glucose dehydrogenase in Pseudomonas taetrolens
J. Agric. Food Chem.
68
12336-12344
2020
Pseudomonas taetrolens (A0A0J6JEN3), Pseudomonas taetrolens
brenda