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1,5-anhydro-D-fructose + O2
1,5-anhydro-3-keto-D-fructose + H2O2
-
-
yield of 1,5-anhydro-3-keto-D-fructose: 33%
?
1,5-anhydro-D-glucitol + O2
1,5-anhydro-D-fructose + H2O2
Phanerochaete gigantea
-
8% relative activity to D-glucose
yield of 1,5-anhydro-D-fructose: 100%
?
1,5-anhydro-D-glucitol + O2
?
-
18.4% of the activity with D-glucose
-
-
?
1,5-anhydro-D-sorbitol + O2
?
-
-
-
-
?
1,6-anhydro-D-glucose + O2
?
-
-
-
-
?
1-beta-aurothioglucose + O2
?
-
91% relative activity to D-glucose
-
-
?
2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) + O2
? + H2O2
-
-
-
?
2,6-dichloroindophenol + O2
? + H2O2
-
-
-
?
2,6-dimethyl-1,4-benzoquinone + O2
? + H2O2
2-chloro-1,4-benzoquinone + O2
? + H2O2
-
-
-
?
2-deoxy-2-fluoro-D-glucose + O2
2-deoxy-3-dehydro-D-glucose + H2O2
slow substrate
-
-
?
2-deoxy-D-galactose + O2
?
selectivity of pyranose 2-oxidase-based biosensor system for different sugar substrates analyzed
-
-
?
2-deoxy-D-glucose + O2
2-deoxy-3-dehydro-D-glucose + H2O2
-
-
-
r
2-deoxy-D-glucose + O2
2-deoxy-3-keto-D-glucose + H2O2
2-deoxy-D-glucose + O2
?
selectivity of pyranose 2-oxidase-based biosensor system for different sugar substrates analyzed
-
-
?
2-keto-D-glucose + O2
2,3-diketo-D-glucose + H2O2
2-methoxy-1,4-benzoquinone + O2
? + H2O2
-
-
-
?
3-deoxy-3-fluoro-beta-D-glucose + H2O2
?
3-deoxy-D-glucose + O2
2-keto-3-deoxy-D-glucose + H2O2
3-O-methyl-D-glucose + O2
2-keto-3-O-methyl-D-glucose + H2O2
-
8.6% relative activity to D-glucose
-
?
5-thioglucose + O2
2-keto-5-thioglucose + H2O2
6-deoxy-D-glucose + O2
2-keto-6-deoxy-D-glucose + H2O2
allose + O2
?
-
38% relative activity to D-glucose
-
-
?
alpha-D-glucose + O2
2-dehydro-D-glucose + H2O2
alpha-D-melibiose + O2
? + H2O2
beta-D-galactose + O2
2-dehydro-D-galactose + H2O2
poor substrate
-
-
?
beta-D-glucose + O2
beta-2-dehydro-D-glucose + H2O2
cellobiose + O2
2-dehydrocellobiose + H2O2
-
17.8% activity compared to D-glucose
-
-
?
D-arabinose + O2
?
-
1.87% of the activity with D-glucose
-
-
?
D-fructose + O2
2-dehydro-D-fructose + H2O2
D-fucono-1,5-lactone + O2
2-keto-D-gluconate + D-araboascorbate + H2O2
D-galactose + 1,4-benzoquinone
2-dehydro-D-galactose + 1,4-hydroquinone
D-galactose + 1,4-benzoquinone
2-dehydro-D-galactose + hydroquinone
-
-
-
?
D-galactose + 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) cation radical
2-dehydro-D-galactose + 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
-
?
D-galactose + ferricenium hexafluorophosphate
2-dehydro-D-galactose + ferrocenium hexafluorophosphate
-
-
-
-
r
D-galactose + ferricenium ion
2-dehydro-D-galactose + ferrocenium ion
-
-
-
r
D-galactose + ferrocenium hexafluorophosphate
2-dehydro-D-galactose + ferrocene
-
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
D-glucono-1,5-lactone + 3-methyl-2-benzothiazolinone hydrazone
2-dehydro-D-glucono-1,5-lactone
D-glucono-1,5-lactone + O2
2-dehydro-D-glucono-1,5-lactone + H2O2
-
107% activity compared to D-glucose
-
-
?
D-glucono-1,5-lactone + O2
?
D-gluconolactone + O2
? + H2O2
D-glucose + 1,4-benzoquinone
2-dehydro-D-glucose + 1,4-hydroquinone
D-glucose + 1,4-benzoquinone
2-dehydro-D-glucose + hydroquinone
D-glucose + 1,4-benzoquinone
?
D-glucose + 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
2-dehydro-D-glucose + ?
-
-
-
-
?
D-glucose + 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) cation radical
2-dehydro-D-glucose + 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
D-glucose + 2,6-dichloroindophenol
2-dehydro-D-glucose + ?
-
-
-
?
D-glucose + 2,6-dichloroindophenol
?
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
2-dehydro-D-glucose + reduced 2,6-dichlorophenolindophenol
D-glucose + 2,6-dimethyl-1,4-benzoquinone
?
-
-
-
-
?
D-glucose + 2-chloro-1,4-benzoquinone
?
-
-
-
-
?
D-glucose + 2-methoxy-1,4-benzoquinone
?
-
-
-
-
?
D-glucose + 2-methyl-1,4-benzoquinone
2-dehydro-D-glucose + 2-methylhydroquinone
-
-
-
r
D-glucose + 2-methyl-1,4-benzoquinone
?
-
-
-
-
?
D-glucose + 3-methyl-2-benzothiazolinone hydrazone
2-dehydro-D-glucose + ?
D-glucose + ferricenium hexafluorophosphate
2-dehydro-D-glucose + ferrocenium hexafluorophosphate
-
-
-
-
r
D-glucose + ferricenium hexafluorophosphate
?
D-glucose + ferricenium ion
2-dehydro-D-glucose + ferrocenium ion
D-glucose + ferricyanide
2-dehydro-D-glucose + ferrocyanide
-
-
-
r
D-glucose + ferrocenium hexafluorophosphate
2-dehydro-D-glucose + ferrocene
-
-
-
?
D-glucose + ferrocenium ion
2-dehydro-D-glucose + ?
-
-
-
?
D-glucose + methyl-1,4-benzoquinone
2-dehydro-D-glucose + methylhydroquinone
-
-
-
-
r
D-glucose + O2
2-dehydro-D-glucose + H2O2
D-glucose + O2
D-arabino-2-hexosulose + H2O2
-
the enzyme is produced during glucose starvation
-
?
D-glucose + O2
D-arabino-hexos-2-ulose + H2O2
D-glucose + O2
D-glucosone + H2O2
D-glucose + tetrabromo-1,4-benzoquinone
2-dehydro-D-glucose + tetrabromohydroquinone
-
-
-
-
r
D-glucose + tetrafluoro-1,4-benzoquinone
?
-
-
-
-
?
D-maltoheptaose + O2
?
selectivity of pyranose 2-oxidase-based biosensor system for different sugar substrates analyzed
-
-
?
D-maltopentaose + O2
?
selectivity of pyranose 2-oxidase-based biosensor system for different sugar substrates analyzed
-
-
?
D-maltose + O2
?
-
15.1% of the activity with D-glucose
-
-
?
D-maltotriose + O2
?
selectivity of pyranose 2-oxidase-based biosensor system for different sugar substrates analyzed
-
-
?
D-mannoheptose + O2
?
-
8.2% relative activity to D-glucose
-
-
?
D-mannose + O2
2-dehydro-D-mannose + H2O2
-
18.4% activity compared to D-glucose
-
-
?
D-mannose + O2
2-keto-D-mannose + H2O2
-
0.9% relative activity to D-glucose
-
?
D-mannose + O2
?
-
6.02% of the activity with D-glucose
-
-
?
D-ribose + 1,4-benzoquinone
2-dehydro-D-ribose + 1,4-hydroquinone
-
-
-
-
?
D-ribose + O2
2-dehydro-D-ribose + H2O2
-
-
-
-
?
D-trehalose + O2
?
selectivity of pyranose 2-oxidase-based biosensor system for different sugar substrates analyzed
-
-
?
D-xylose + 1,4-benzoquinone
2-dehydro-D-xylose + 1,4-hydroquinone
-
-
-
-
?
D-xylose + 3-methyl-2-benzothiazolinone hydrazone
2-dehydro-D-xylose + ?
D-xylose + O2
2-dehydro-D-xylose + H2O2
D-xylose + O2
D-threo-pentos-2-ulose + H2O2
D-xylose + O2
D-xylosone + H2O2
ferricenium hexafluorophosphate + O2
? + H2O2
-
-
-
?
gentibiose + O2
2-keto-D-gentibiose + H2O2
L-arabinose + 1,4-benzoquinone
2-dehydro-L-arabinose + 1,4-hydroquinone
-
-
-
-
?
L-arabinose + O2
2-dehydro-L-arabinose + H2O2
-
-
-
-
?
L-sorbose + 3-methyl-2-benzothiazolinone hydrazone
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
L-sorbose D-allose + O2
?
-
-
-
?
lactose + O2
2-dehydrolactose + H2O2
-
0.71% activity compared to D-glucose
-
-
?
maltose + O2
2-dehydro-D-maltose + H2O2
-
92.2% activity compared to D-glucose
-
-
?
methyl alpha-D-glucoside + O2
2-dehydro-alpha-D-methylglucoside + H2O2
methyl beta-D-glucoside + O2
2-dehydro-beta-D-methylglucoside + H2O2
methyl-beta-D-glucoside + O2
?
-
-
-
?
sucrose + O2
? + H2O2
-
82.8% activity compared to D-glucose
-
-
?
tetrafluoro-1,4-benzoquinone + O2
? + H2O2
trehalose + O2
?
-
14.3% of the activity with D-glucose
-
-
?
wheat flour + O2
?
-
-
-
?
additional information
?
-
2,6-dimethyl-1,4-benzoquinone + O2
? + H2O2
-
-
-
?
2,6-dimethyl-1,4-benzoquinone + O2
? + H2O2
-
-
-
-
?
2-deoxy-D-glucose + O2
2-deoxy-3-keto-D-glucose + H2O2
Phanerochaete gigantea
-
1% relative activity to D-glucose
yield: 75%
?
2-deoxy-D-glucose + O2
2-deoxy-3-keto-D-glucose + H2O2
-
-
-
?
2-deoxy-D-glucose + O2
2-deoxy-3-keto-D-glucose + H2O2
-
25% relative activity to D-glucose
-
?
2-deoxy-D-glucose + O2
2-deoxy-3-keto-D-glucose + H2O2
-
18% relative activity to D-glucose
-
?
2-deoxy-D-glucose + O2
2-deoxy-3-keto-D-glucose + H2O2
-
18% relative activity to D-glucose
-
?
2-keto-D-glucose + O2
2,3-diketo-D-glucose + H2O2
-
-
-
?
2-keto-D-glucose + O2
2,3-diketo-D-glucose + H2O2
-
-
-
?
2-keto-D-glucose + O2
2,3-diketo-D-glucose + H2O2
-
-
-
?
3-deoxy-3-fluoro-beta-D-glucose + H2O2
?
slow substrate
-
-
?
3-deoxy-3-fluoro-beta-D-glucose + H2O2
?
slow substrate
-
-
?
3-deoxy-D-glucose + O2
2-keto-3-deoxy-D-glucose + H2O2
Phanerochaete gigantea
-
96% relative activity to D-glucose
-
?
3-deoxy-D-glucose + O2
2-keto-3-deoxy-D-glucose + H2O2
-
-
-
?
5-thioglucose + O2
2-keto-5-thioglucose + H2O2
-
30% relative activity to D-glucose
-
?
5-thioglucose + O2
2-keto-5-thioglucose + H2O2
-
24% relative activity to D-glucose
-
?
6-deoxy-D-glucose + O2
2-keto-6-deoxy-D-glucose + H2O2
-
-
-
?
6-deoxy-D-glucose + O2
2-keto-6-deoxy-D-glucose + H2O2
-
-
-
?
6-deoxy-D-glucose + O2
2-keto-6-deoxy-D-glucose + H2O2
Phanerochaete gigantea
-
15% relative activity to D-glucose
-
?
6-deoxy-D-glucose + O2
2-keto-6-deoxy-D-glucose + H2O2
-
-
-
?
6-deoxy-D-glucose + O2
2-keto-6-deoxy-D-glucose + H2O2
-
76% relative activity to D-glucose
-
?
6-deoxy-D-glucose + O2
2-keto-6-deoxy-D-glucose + H2O2
-
73% relative activity to D-glucose
-
?
6-deoxy-D-glucose + O2
2-keto-6-deoxy-D-glucose + H2O2
-
73% relative activity to D-glucose
-
?
6-deoxy-D-glucose + O2
2-keto-6-deoxy-D-glucose + H2O2
-
-
-
?
alpha-D-glucose + O2
2-dehydro-D-glucose + H2O2
Coriolus sp.
-
-
-
-
?
alpha-D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
-
?
alpha-D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
-
?
alpha-D-melibiose + O2
? + H2O2
-
-
-
?
alpha-D-melibiose + O2
? + H2O2
-
1.9% relative activity to D-glucose
-
?
alpha-D-melibiose + O2
? + H2O2
-
-
-
?
beta-D-glucose + O2
beta-2-dehydro-D-glucose + H2O2
-
-
-
-
r
beta-D-glucose + O2
beta-2-dehydro-D-glucose + H2O2
-
-
-
-
r
D-allose + O2
?
-
-
-
-
?
D-cellobiose + O2
?
17% of the activity with D-glucose
-
-
?
D-cellobiose + O2
?
17% of the activity with D-glucose
-
-
?
D-cellobiose + O2
?
selectivity of pyranose 2-oxidase-based biosensor system for different sugar substrates analyzed
-
-
?
D-fructose + O2
2-dehydro-D-fructose + H2O2
-
-
-
-
?
D-fructose + O2
2-dehydro-D-fructose + H2O2
-
12.4% activity compared to D-glucose
-
-
?
D-fructose + O2
? + H2O2
-
-
-
?
D-fructose + O2
? + H2O2
-
6.5% relative activity to D-glucose
-
?
D-fucono-1,5-lactone + O2
2-keto-D-gluconate + D-araboascorbate + H2O2
-
-
-
-
?
D-fucono-1,5-lactone + O2
2-keto-D-gluconate + D-araboascorbate + H2O2
-
-
-
-
?
D-fucono-1,5-lactone + O2
2-keto-D-gluconate + D-araboascorbate + H2O2
Polyporus obtusus
-
-
-
-
?
D-fucono-1,5-lactone + O2
2-keto-D-gluconate + D-araboascorbate + H2O2
Polyporus obtusus
-
-
-
?
D-fucono-1,5-lactone + O2
2-keto-D-gluconate + D-araboascorbate + H2O2
Polyporus obtusus
-
-
-
-
?
D-fucono-1,5-lactone + O2
2-keto-D-gluconate + D-araboascorbate + H2O2
Polyporus obtusus
-
-
-
?
D-fucose + O2
?
-
2.9% relative activity to D-glucose
-
-
?
D-fucose + O2
?
-
-
-
-
?
D-fucose + O2
?
selectivity of pyranose 2-oxidase-based biosensor system for different sugar substrates analyzed
-
-
?
D-galactose + 1,4-benzoquinone
2-dehydro-D-galactose + 1,4-hydroquinone
-
-
-
?
D-galactose + 1,4-benzoquinone
2-dehydro-D-galactose + 1,4-hydroquinone
-
-
-
-
?
D-galactose + 1,4-benzoquinone
2-dehydro-D-galactose + 1,4-hydroquinone
-
-
-
-
?
D-galactose + 1,4-benzoquinone
2-dehydro-D-galactose + 1,4-hydroquinone
-
-
-
-
?
D-galactose + 1,4-benzoquinone
2-dehydro-D-galactose + 1,4-hydroquinone
-
-
-
?
D-galactose + 1,4-benzoquinone
2-dehydro-D-galactose + 1,4-hydroquinone
-
-
-
-
?
D-galactose + 1,4-benzoquinone
2-dehydro-D-galactose + 1,4-hydroquinone
-
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
-
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
-
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
38.8% activity compared to D-glucose
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
38.8% activity compared to D-glucose
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
5% relative activity to D-glucose
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
5% relative activity to D-glucose
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
4% relative activity to D-glucose
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
7.7% relative activity to D-glucose
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
8.5% relative activity to D-glucose
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
-
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
-
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
-
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
-
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
-
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
5.7% relative activity to D-glucose
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
His-tagged recombinant wild type enzyme strongly prefers D-glucose to D-galactose as its substrate
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
mutants T169S, T169N, and T169G
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
-
-
?
D-galactose + O2
2-dehydro-D-galactose + H2O2
-
0.9% relative activity to D-glucose
-
?
D-galactose + O2
?
-
-
-
-
?
D-galactose + O2
?
-
-
-
?
D-galactose + O2
?
selectivity of pyranose 2-oxidase-based biosensor system for different sugar substrates analyzed
-
-
?
D-galactose + O2
?
-
5.41% of the activity with D-glucose
-
-
?
D-glucono-1,5-lactone + 3-methyl-2-benzothiazolinone hydrazone
2-dehydro-D-glucono-1,5-lactone
-
-
-
?
D-glucono-1,5-lactone + 3-methyl-2-benzothiazolinone hydrazone
2-dehydro-D-glucono-1,5-lactone
-
-
-
?
D-glucono-1,5-lactone + O2
?
68% of the activity with D-glucose
-
-
?
D-glucono-1,5-lactone + O2
?
68% of the activity with D-glucose
-
-
?
D-gluconolactone + O2
? + H2O2
-
activity about 10% that of D-glucose
-
?
D-gluconolactone + O2
? + H2O2
-
60% relative activity to D-glucose
-
?
D-gluconolactone + O2
? + H2O2
-
60% relative activity to D-glucose
-
?
D-gluconolactone + O2
? + H2O2
-
44% relative activity to D-glucose
-
?
D-gluconolactone + O2
? + H2O2
-
1.5% relative activity to D-glucose
-
?
D-gluconolactone + O2
? + H2O2
Polyporus obtusus
-
-
-
?
D-gluconolactone + O2
? + H2O2
Polyporus obtusus
-
14% relative activity to D-glucose, two main products, i.e., 2-ketogluconic acid and araboascorbic acid are formed
-
?
D-gluconolactone + O2
? + H2O2
-
64% relative activity to D-glucose
-
?
D-glucose + 1,4-benzoquinone
2-dehydro-D-glucose + 1,4-hydroquinone
-
-
-
?
D-glucose + 1,4-benzoquinone
2-dehydro-D-glucose + 1,4-hydroquinone
-
-
-
?
D-glucose + 1,4-benzoquinone
2-dehydro-D-glucose + 1,4-hydroquinone
-
-
-
-
?
D-glucose + 1,4-benzoquinone
2-dehydro-D-glucose + 1,4-hydroquinone
-
-
-
-
?
D-glucose + 1,4-benzoquinone
2-dehydro-D-glucose + 1,4-hydroquinone
-
-
-
?
D-glucose + 1,4-benzoquinone
2-dehydro-D-glucose + 1,4-hydroquinone
-
-
-
-
?
D-glucose + 1,4-benzoquinone
2-dehydro-D-glucose + 1,4-hydroquinone
-
-
-
?
D-glucose + 1,4-benzoquinone
2-dehydro-D-glucose + 1,4-hydroquinone
-
-
-
-
?
D-glucose + 1,4-benzoquinone
2-dehydro-D-glucose + hydroquinone
-
-
-
?
D-glucose + 1,4-benzoquinone
2-dehydro-D-glucose + hydroquinone
1,4-benzoquinone is a physiologically relevant alternative electron acceptor in the oxidative half-reaction
-
-
?
D-glucose + 1,4-benzoquinone
?
-
-
-
-
?
D-glucose + 1,4-benzoquinone
?
-
-
-
-
?
D-glucose + 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) cation radical
2-dehydro-D-glucose + 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
-
-
?
D-glucose + 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) cation radical
2-dehydro-D-glucose + 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
-
?
D-glucose + 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) cation radical
2-dehydro-D-glucose + 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
2-dehydro-D-glucose + reduced 2,6-dichlorophenolindophenol
-
-
-
-
r
D-glucose + 2,6-dichlorophenolindophenol
2-dehydro-D-glucose + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
2-dehydro-D-glucose + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-glucose + 3-methyl-2-benzothiazolinone hydrazone
2-dehydro-D-glucose + ?
-
-
-
?
D-glucose + 3-methyl-2-benzothiazolinone hydrazone
2-dehydro-D-glucose + ?
-
-
-
-
?
D-glucose + 3-methyl-2-benzothiazolinone hydrazone
2-dehydro-D-glucose + ?
-
-
-
?
D-glucose + ferricenium hexafluorophosphate
?
-
-
-
-
?
D-glucose + ferricenium hexafluorophosphate
?
-
-
-
-
?
D-glucose + ferricenium ion
2-dehydro-D-glucose + ferrocenium ion
-
-
-
?
D-glucose + ferricenium ion
2-dehydro-D-glucose + ferrocenium ion
-
-
-
-
?
D-glucose + ferricenium ion
2-dehydro-D-glucose + ferrocenium ion
-
-
-
r
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
Coriolus sp.
-
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
preferred substrate
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
100% activity
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
preferred substrate
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
100% activity
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
D-glucose is the best substrate
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
D-glucose is the best substrate
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
656544, 695870, 696791, 699076, 711239, 712500, 724369, 724753, 724979, 725776, 741113, 741252 -
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
-
r
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
immobilized and soluble pyranose 2-oxidase analyzed
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
recombinant pyranose 2-oxidase analyzed
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
selectivity of pyranose 2-oxidase-based biosensor system for different sugar substrates analyzed
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
His-tagged recombinant wild type enzyme strongly prefers D-glucose to D-galactose as its substrate
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
the wild type enzyme displays a clear preference for D-glucose over D-galactose
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
highly regioselective mechanism
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
recombinant pyranose 2-oxidase analyzed
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
?
D-glucose + O2
2-dehydro-D-glucose + H2O2
-
-
-
-
?
D-glucose + O2
D-arabino-hexos-2-ulose + H2O2
Polyporus obtusus
-
-
the product is a specific tautomeric form of D-arabino-hexos-2-ulose (form IV, 20%) being in equilibrium with three other forms of D-arabinohexos-2-ulose in solution
-
?
D-glucose + O2
D-arabino-hexos-2-ulose + H2O2
Polyporus obtusus AU124PD
-
-
the product is a specific tautomeric form of D-arabino-hexos-2-ulose (form IV, 20%) being in equilibrium with three other forms of D-arabinohexos-2-ulose in solution
-
?
D-glucose + O2
D-glucosone + H2O2
-
-
-
?
D-glucose + O2
D-glucosone + H2O2
-
-
-
?
D-glucose + O2
D-glucosone + H2O2
-
-
D-glucosone is identical with D-arabino-2-hexosulose
?
D-glucose + O2
D-glucosone + H2O2
-
-
-
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
Corticium caeruleum
-
-
-
?
D-glucose + O2
D-glucosone + H2O2
-
-
-
?
D-glucose + O2
D-glucosone + H2O2
-
-
D-glucosone is identical with D-arabino-2-hexosulose
?
D-glucose + O2
D-glucosone + H2O2
-
-
D-glucosone is identical with D-arabino-2-hexosulose
?
D-glucose + O2
D-glucosone + H2O2
Lenzites styracinus
-
-
-
?
D-glucose + O2
D-glucosone + H2O2
-
-
-
?
D-glucose + O2
D-glucosone + H2O2
-
-
-
?
D-glucose + O2
D-glucosone + H2O2
-
-
-
?
D-glucose + O2
D-glucosone + H2O2
Phanerochaete gigantea
-
-
-
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
D-glucosone is identical with D-arabino-2-hexosulose
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
D-glucosone is identical with D-arabino-2-hexosulose
?
D-glucose + O2
D-glucosone + H2O2
-
alpha-D-glucose has a 104% relative activity compared to D-glucose, beta-D-glucose has a 80% relative activity compared to D-glucose
-
?
D-glucose + O2
D-glucosone + H2O2
-
100% relative activity
-
?
D-glucose + O2
D-glucosone + H2O2
-
the activation energy for D-glucose activation is 24.7 kJ/mol
-
?
D-glucose + O2
D-glucosone + H2O2
-
activation energy for the conversion of D-glucose is 34.6 kJ/mol
-
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
-
-
-
?
D-glucose + O2
D-glucosone + H2O2
Polyporus obtusus
-
-
-
?
D-glucose + O2
D-glucosone + H2O2
Polyporus obtusus
-
-
D-glucosone is identical with D-arabino-2-hexosulose
?
D-glucose + O2
D-glucosone + H2O2
Polyporus obtusus
-
other electron acceptors: 2,6-dichlorophenolindophenol, cytochrome c
D-glucosone is identical with D-arabino-2-hexosulose
?
D-glucose + O2
D-glucosone + H2O2
Polyporus obtusus
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
Polyporus obtusus
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
Polyporus obtusus
-
D-glucose is the preferred substrate
D-glucosone is identical with D-arabino-2-hexosulose
?
D-glucose + O2
D-glucosone + H2O2
Polyporus obtusus
-
D-glucose is the preferred substrate
D-glucosone is identical with D-arabino-2-hexosulose
?
D-glucose + O2
D-glucosone + H2O2
Saxidomus giganteus
-
-
-
?
D-glucose + O2
D-glucosone + H2O2
-
-
-
?
D-glucose + O2
D-glucosone + H2O2
Trametes cinnabarinus
-
-
D-glucosone is identical with D-arabino-2-hexosulose
?
D-glucose + O2
D-glucosone + H2O2
-
-
-
?
D-glucose + O2
D-glucosone + H2O2
-
100% relative activity
-
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
-
-
-
-
?
D-glucose + O2
D-glucosone + H2O2
-
-
D-glucosone is identical with D-arabino-2-hexosulose
?
D-glucose + O2
D-glucosone + H2O2
-
both alpha- and beta-anomeric forms can serve almost equally as substrate
-
?
D-glucose + O2
D-glucosone + H2O2
-
other electron acceptors: 2,6-dichlorophenolindophenol, cytochrome c
-
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
-
?
D-glucose + O2
D-glucosone + H2O2
-
D-glucose is the preferred substrate
D-glucosone is identical with D-arabino-2-hexosulose
?
D-glucose + O2
D-glucosone + H2O2
-
-
-
-
?
D-melibiose + O2
?
-
-
-
-
?
D-melibiose + O2
?
-
-
-
?
D-xylose + 3-methyl-2-benzothiazolinone hydrazone
2-dehydro-D-xylose + ?
-
-
-
?
D-xylose + 3-methyl-2-benzothiazolinone hydrazone
2-dehydro-D-xylose + ?
-
-
-
?
D-xylose + O2
2-dehydro-D-xylose + H2O2
-
-
-
-
?
D-xylose + O2
2-dehydro-D-xylose + H2O2
-
-
-
-
?
D-xylose + O2
2-dehydro-D-xylose + H2O2
-
75.1% activity compared to D-glucose
-
-
?
D-xylose + O2
2-dehydro-D-xylose + H2O2
-
-
-
-
?
D-xylose + O2
2-dehydro-D-xylose + H2O2
-
-
-
?
D-xylose + O2
2-dehydro-D-xylose + H2O2
-
-
-
?
D-xylose + O2
?
-
-
-
?
D-xylose + O2
?
35% of the activity with D-glucose
-
-
?
D-xylose + O2
?
35% of the activity with D-glucose
-
-
?
D-xylose + O2
?
-
-
-
-
?
D-xylose + O2
?
selectivity of pyranose 2-oxidase-based biosensor system for different sugar substrates analyzed
-
-
?
D-xylose + O2
?
-
13.4% of the activity with D-glucose
-
-
?
D-xylose + O2
D-threo-pentos-2-ulose + H2O2
Polyporus obtusus
-
-
-
-
?
D-xylose + O2
D-threo-pentos-2-ulose + H2O2
Polyporus obtusus AU124PD
-
-
-
-
?
D-xylose + O2
D-xylosone + H2O2
-
-
-
?
D-xylose + O2
D-xylosone + H2O2
-
-
-
?
D-xylose + O2
D-xylosone + H2O2
-
activity about 10% that of D-glucose
-
?
D-xylose + O2
D-xylosone + H2O2
Coriolus sp.
-
-
-
-
?
D-xylose + O2
D-xylosone + H2O2
-
-
-
?
D-xylose + O2
D-xylosone + H2O2
-
-
-
?
D-xylose + O2
D-xylosone + H2O2
-
-
-
?
D-xylose + O2
D-xylosone + H2O2
-
-
-
?
D-xylose + O2
D-xylosone + H2O2
-
30% relative activity to D-glucose
-
?
D-xylose + O2
D-xylosone + H2O2
-
37% relative activity to D-glucose
-
?
D-xylose + O2
D-xylosone + H2O2
-
37% relative activity to D-glucose
-
?
D-xylose + O2
D-xylosone + H2O2
-
-
-
?
D-xylose + O2
D-xylosone + H2O2
-
50% relative activity to D-glucose
-
?
D-xylose + O2
D-xylosone + H2O2
-
43.7% relative activity to D-glucose
-
?
D-xylose + O2
D-xylosone + H2O2
Polyporus obtusus
-
-
-
?
D-xylose + O2
D-xylosone + H2O2
Polyporus obtusus
-
-
-
?
D-xylose + O2
D-xylosone + H2O2
Polyporus obtusus
-
-
-
?
D-xylose + O2
D-xylosone + H2O2
Polyporus obtusus
-
-
-
?
D-xylose + O2
D-xylosone + H2O2
Polyporus obtusus
-
38% relative activity to D-glucose
-
?
D-xylose + O2
D-xylosone + H2O2
-
56% relative activity to D-glucose
-
?
D-xylose + O2
D-xylosone + H2O2
-
-
-
?
D-xylose + O2
D-xylosone + H2O2
-
-
-
?
D-xylose + O2
D-xylosone + H2O2
-
2.6% relative activity to D-glucose
-
?
gentibiose + O2
2-keto-D-gentibiose + H2O2
-
-
-
?
gentibiose + O2
2-keto-D-gentibiose + H2O2
-
-
-
?
gentibiose + O2
2-keto-D-gentibiose + H2O2
-
23% relative activity to D-glucose
-
?
L-arabinose + O2
?
-
1.5% relative activity to D-glucose
-
-
?
L-arabinose + O2
?
selectivity of pyranose 2-oxidase-based biosensor system for different sugar substrates analyzed
-
-
?
L-sorbose + 3-methyl-2-benzothiazolinone hydrazone
?
-
-
-
?
L-sorbose + 3-methyl-2-benzothiazolinone hydrazone
?
-
-
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
-
-
-
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
-
-
-
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
-
-
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
-
activity about 10% that of D-glucose
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
Coriolus sp.
-
-
-
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
-
122% activity compared to D-glucose
-
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
-
122% activity compared to D-glucose
-
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
-
-
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
-
-
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
-
68% relative activity to D-glucose
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
-
52% relative activity to D-glucose
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
-
52% relative activity to D-glucose
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
-
96.3% relative activity to D-glucose
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
-
109% relative activity to D-glucose
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
Polyporus obtusus
-
-
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
Polyporus obtusus
-
-
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
Polyporus obtusus
-
-
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
Polyporus obtusus
-
59% relative activity to D-glucose
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
-
99% relative activity to D-glucose
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
-
-
-
?
L-sorbose + O2
5-dehydro-D-fructose + H2O2
-
3.4% relative activity to D-glucose
-
?
L-sorbose + O2
?
-
-
-
?
L-sorbose + O2
?
-
-
-
-
?
L-sorbose + O2
?
-
17.9% of the activity with D-glucose
-
-
?
maltose + O2
? + H2O2
-
26% relative activity to D-glucose
-
?
maltose + O2
? + H2O2
-
8.2% relative activity to D-glucose
-
?
methyl alpha-D-glucoside + O2
2-dehydro-alpha-D-methylglucoside + H2O2
-
3% relative activity to D-glucose
-
-
?
methyl alpha-D-glucoside + O2
2-dehydro-alpha-D-methylglucoside + H2O2
-
1.9% relative activity to D-glucose
-
-
?
methyl beta-D-glucoside + O2
2-dehydro-beta-D-methylglucoside + H2O2
-
26.3% relative activity to D-glucose
-
-
?
methyl beta-D-glucoside + O2
2-dehydro-beta-D-methylglucoside + H2O2
-
9.6% relative activity to D-glucose
-
-
?
tetrafluoro-1,4-benzoquinone + O2
? + H2O2
-
-
-
?
tetrafluoro-1,4-benzoquinone + O2
? + H2O2
-
-
-
-
?
additional information
?
-
-
no activity with mannose and lactose as substrates. The enzyme catalyzes the two-electron reduction of 1,4-benzoquinone, several substituted benzoquinones and 2,6-dichloroindophenol. Some of these quinone electron acceptors are better substrates for pyranose oxidase than oxygen. Peroxidase-coupled assay using [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)] as the chromogen
-
-
?
additional information
?
-
-
no activity with D-fructose, mannose and lactose as substrates. Peroxidase-coupled assay using [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)] as the chromogen
-
-
?
additional information
?
-
-
no activity with D-arabinose
-
-
?
additional information
?
-
-
no activity with D-arabinose
-
-
?
additional information
?
-
evidence that the enzyme has a role in lignocellulose degradation
-
-
?
additional information
?
-
-
evidence that the enzyme has a role in lignocellulose degradation
-
-
?
additional information
?
-
at 10 mM concentration, glucose is the best substrate, but xylose, sorbose, and D-glucono-1,5-lactone have more than half of its activity
-
-
?
additional information
?
-
-
at 10 mM concentration, glucose is the best substrate, but xylose, sorbose, and D-glucono-1,5-lactone have more than half of its activity
-
-
?
additional information
?
-
evidence that the enzyme has a role in lignocellulose degradation
-
-
?
additional information
?
-
at 10 mM concentration, glucose is the best substrate, but xylose, sorbose, and D-glucono-1,5-lactone have more than half of its activity
-
-
?
additional information
?
-
-
no activity in the presence of D-mannose, D-fructose, maltose, trehalose, lactose and D-melibiose
-
-
?
additional information
?
-
-
no activity in the presence of D-mannose, D-fructose, maltose, trehalose, lactose and D-melibiose
-
-
?
additional information
?
-
-
pyranose 2-oxidase from Trametes multicolor is a flavoenzyme that catalyzes the oxidation of D-glucose and other aldopyranose sugars at the C2 position by using O2 as an electron acceptor to form the corresponding 2-oxo-sugars and H2O2
-
-
?
additional information
?
-
ferulic acid oxidation in a model system and of thiol oxidation in a wheat flour extract, overview. L-arabinose is a poor substrate. Dehydroascorbic acid does not act as electron acceptor
-
-
?
additional information
?
-
-
most of the catalytic dehydrogenation of substrates by flavoprotein oxidases in the GMC class is initiated by the removal of a hydroxyl proton followed by the transfer of a hydride moiety. Pyranose 2-oxidase catalyzes the oxidation of several aldopyranoses by molecular oxygen at the C2 position to yield the corresponding 2-keto-aldoses and hydrogen peroxide
-
-
?
additional information
?
-
ferulic acid oxidation in a model system and of thiol oxidation in a wheat flour extract, overview. L-arabinose is a poor substrate. Dehydroascorbic acid does not act as electron acceptor
-
-
?
additional information
?
-
-
the rate of bioconversion of D-glucose by glucose 2-oxidase in the presence of either nitrogen or supercritical CO2 at 110 bar is very low compared with the use of compressed air at the same pressure
-
-
?
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0.0052 - 2
1,4-benzoquinone
10.7
1,5-anhydro-D-glucitol
-
pH 7.0, 37°C
0.07 - 0.09
2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) cation radical
0.051 - 0.39
2,6-dichloroindophenol
0.065 - 0.094
2,6-dichlorophenolindophenol
0.4 - 2.1
2,6-dimethyl-1,4-benzoquinone
0.31 - 0.48
2-chloro-1,4-benzoquinone
10.32
2-deoxy-D-galactose
100 mM ethanolamine buffer, pH 10.5
11.3 - 99.3
2-deoxy-D-glucose
0.21 - 0.42
2-methoxy-1,4-benzoquinone
0.11 - 0.51
2-methyl-1,4-benzoquinone
120
6-O-alpha-D-galactopyranosyl-beta-D-glucopyranose
-
-
0.57 - 0.97
beta-D-glucose
290
cellobiose
-
at pH 6.5 and 25°C
174
D-arabinose
-
pH 7.0, 37°C
0.71
D-cellobiose
100 mM ethanolamine buffer, pH 10.5
6.25
D-fucose
100 mM ethanolamine buffer, pH 10.5
51.1
D-glucono-1,5-lactone
-
at pH 6.5 and 25°C
6.02
D-maltoheptaose
100 mM ethanolamine buffer, pH 10.5
6.14
D-maltopentaose
100 mM ethanolamine buffer, pH 10.5
329
D-maltose
-
pH 7.0, 37°C
6.61
D-maltotriose
100 mM ethanolamine buffer, pH 10.5
180
D-ribose
-
with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 37°C
7.51
D-trehalose
100 mM ethanolamine buffer, pH 10.5
0.092 - 1.12
ferricenium hexafluorophosphate
0.054 - 0.408
ferricenium ion
3.43
ferricyanide
substrate ferricyanide (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.015 - 0.4
ferrocenium hexafluorophosphate
0.187
ferrocenium ion
using D-glucose as cosubstrate, at 30°C, pH 6.5
72.8
melibiose
at 30°C, pH 6.5
0.35 - 0.4
methyl-1,4-benzoquinone
50 - 289
methyl-beta-D-glucoside
902
sucrose
-
at pH 6.5 and 25°C
0.09
tetrabromo-1,4-benzoquinone
0.088
tetrachloro-1,4-benzoquinone
-
pH 6.5, substrate: D-glucose
0.22 - 9.42
tetrafluoro-1,4-benzoquinone
192
trehalose
-
pH 7.0, 37°C
additional information
additional information
-
0.0052
1,4-benzoquinone
mutant enzyme F454N, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.0071
1,4-benzoquinone
mutant enzyme F454P, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.0089
1,4-benzoquinone
mutant enzyme F454A/S455A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.01
1,4-benzoquinone
mutant enzyme Y456W, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.013
1,4-benzoquinone
mutant enzyme H450Q, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.027
1,4-benzoquinone
wild type enzyme, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.029
1,4-benzoquinone
mutant enzyme F454A/S455A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.029
1,4-benzoquinone
mutant enzyme F454A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.032
1,4-benzoquinone
L537W/E542R mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.033
1,4-benzoquinone
using D-glucose as cosubstrate, at 30°C, pH 6.5
0.036
1,4-benzoquinone
L537W mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.037
1,4-benzoquinone
L537G/E542R mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.038
1,4-benzoquinone
L537W/E542K mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.04
1,4-benzoquinone
E542R mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.04
1,4-benzoquinone
L537G/E542K mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.042
1,4-benzoquinone
substrate 1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 4.5
0.043
1,4-benzoquinone
-
V546C/T169G mutant, substrate 1,4-benzoquinone (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.048
1,4-benzoquinone
L537G mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.049
1,4-benzoquinone
E542K mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.052
1,4-benzoquinone
mutant enzyme F454N, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.065
1,4-benzoquinone
wild-type, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.072
1,4-benzoquinone
-
V546C/T169G/L537W mutant, substrate 1,4-benzoquinone (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.072
1,4-benzoquinone
mutant enzyme F454P, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.072
1,4-benzoquinone
mutant enzyme Y456W, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.078
1,4-benzoquinone
mutant enzyme F454A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.11
1,4-benzoquinone
substrate 1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.12
1,4-benzoquinone
-
with D-glucose as cosubstrate, at pH 6.5 and 37°C
0.13
1,4-benzoquinone
L537W mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.136
1,4-benzoquinone
E542R mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.137
1,4-benzoquinone
L537W/E542R mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.14
1,4-benzoquinone
L537W/E542K mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.14
1,4-benzoquinone
wild type enzyme, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.15
1,4-benzoquinone
L537G/E542K mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.15
1,4-benzoquinone
-
pH 6.5, 30°C, recombinant enzyme
0.155
1,4-benzoquinone
L537G/E542R mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.176
1,4-benzoquinone
L537G mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.182
1,4-benzoquinone
E542K mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.24
1,4-benzoquinone
mutant enzyme H450Q, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.241
1,4-benzoquinone
wild-type, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.28
1,4-benzoquinone
-
V546C/T169G mutant, substrate 1,4-benzoquinone (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.3
1,4-benzoquinone
-
pH 4.5, substrate: D-glucose
0.3
1,4-benzoquinone
-
soluble enzyme, 500 mM glucose used as electron acceptor, pH 5.0
0.31
1,4-benzoquinone
-
pH 6.5, substrate: D-glucose
0.32
1,4-benzoquinone
-
pH 6.5, 30°C, recombinant enzyme
0.37
1,4-benzoquinone
-
V546C/E542K mutant, substrate 1,4-benzoquinone (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
1.18
1,4-benzoquinone
-
V546C/T169G/L537W mutant, substrate 1,4-benzoquinone (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
1.5 - 2
1,4-benzoquinone
-
V546C/E542K mutant, substrate 1,4-benzoquinone (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.07
2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) cation radical
-
pH 6.5, substrate: D-glucose
0.09
2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) cation radical
substrate 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) cation radical (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.051
2,6-dichloroindophenol
substrate 2,6-dichloroindophenol (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.187
2,6-dichloroindophenol
using D-glucose as cosubstrate, at 30°C, pH 6.5
0.39
2,6-dichloroindophenol
-
pH 6.5, 30°C, recombinant enzyme
0.065
2,6-dichlorophenolindophenol
-
pH 6.5, substrate: D-glucose
0.065
2,6-dichlorophenolindophenol
-
at pH 6.5 and 30°C
0.094
2,6-dichlorophenolindophenol
-
pH 4.5, substrate: D-glucose
0.094
2,6-dichlorophenolindophenol
-
at pH 4.5 and 30°C
0.4
2,6-dimethyl-1,4-benzoquinone
-
pH 6.5, 30°C, recombinant enzyme
0.83
2,6-dimethyl-1,4-benzoquinone
-
pH 4.5, substrate: D-glucose
1.59
2,6-dimethyl-1,4-benzoquinone
substrate 2,6-dimethyl-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
2.1
2,6-dimethyl-1,4-benzoquinone
-
pH 6.5, substrate: D-glucose
0.31
2-chloro-1,4-benzoquinone
substrate 2-chloro-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.48
2-chloro-1,4-benzoquinone
-
pH 6.5, 30°C, recombinant enzyme
11.3
2-deoxy-D-glucose
pH 7.3, 22°C, wild-type enzyme
11.85
2-deoxy-D-glucose
100 mM ethanolamine buffer, pH 10.5
55
2-deoxy-D-glucose
-
oxygen concentration 1.07 mM
79
2-deoxy-D-glucose
pH 7.3, 22°C, mutant enzyme E540K with a C-terminal His6-tag
99.3
2-deoxy-D-glucose
pH 7.3, 22°C, mutant enzyme K312E with a C-terminal His6-tag
0.21
2-methoxy-1,4-benzoquinone
substrate 2-methoxy-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.42
2-methoxy-1,4-benzoquinone
-
pH 6.5, 30°C, recombinant enzyme
0.11
2-methyl-1,4-benzoquinone
-
pH 6.5, 30°C, recombinant enzyme
0.51
2-methyl-1,4-benzoquinone
substrate 2-methyl-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
1
alpha-D-glucose
-
-
1.53
alpha-D-glucose
-
oxygen concentration 1.07 mM
0.57
beta-D-glucose
-
-
0.97
beta-D-glucose
-
oxygen concentration 1.07 mM
22.1
D-allose
pH 7.3, 22°C, mutant enzyme E540K with a C-terminal His6-tag
22.3
D-allose
pH 7.3, 22°C, mutant enzyme E540K
55.7
D-allose
pH 7.3, 22°C, wild-type enzyme
68
D-allose
pH 7.3, 22°C, mutant enzyme K312E with a C-terminal His6-tag
103
D-fructose
substrate D-fructose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
727
D-fructose
-
at pH 6.5 and 25°C
2558
D-fructose
-
pH 6.5, 30°C, recombinant enzyme
0.093
D-galactose
T169G/E542K/V546C, mutant, 30°C, substrate D-galactose (1,4-benzoquinone saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
0.19
D-galactose
T169G/E542K/V546C, mutant, 50°C, substrate D-galactose (1,4-benzoquinone saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
0.23
D-galactose
wild-type, mutant, 50°C, substrate D-galactose (1,4-benzoquinone saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
0.25
D-galactose
wild-type, mutant, 30°C, substrate D-galactose (1,4-benzoquinone saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
0.4
D-galactose
-
V546C/T169G mutant, substrate D-galactose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.4
D-galactose
mutant enzyme T196G/V546C, pH and temperature not specified in the publication
0.86
D-galactose
-
V546C/T169G/L537W mutant, substrate D-galactose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.983
D-galactose
V546P/T169G, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
1.66
D-galactose
T169G/E542K/V546C, mutant, 30°C, substrate D-galactose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
2.45
D-galactose
mutant enzyme H450G, in 50 mM phosphate buffer (pH 6.5) at 60°C
2.45
D-galactose
mutant enzyme H450G, pH and temperature not specified in the publication
2.48
D-galactose
T169G, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
2.48
D-galactose
mutant enzyme T169G, pH and temperature not specified in the publication
2.76
D-galactose
T169G/E542K/V546C, mutant, 50°C, substrate D-galactose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
2.94
D-galactose
substrate D-galactose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
3.1
D-galactose
-
mutant enzyme T169G, in 50 mM sodium phosphate (pH 7.0), at 25°C
3.56
D-galactose
T169N, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
3.7
D-galactose
-
pH 7.0, 25°C, reductive half-reaction, wild-type enzyme
3.84
D-galactose
at 30°C, pH 6.5
3.87
D-galactose
E542K mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
3.87
D-galactose
mutant enzyme E542K, in 50 mM phosphate buffer (pH 6.5) at 60°C
4.2
D-galactose
-
pH 7.0, 25°C, reductive half-reaction, mutant T169G
4.26
D-galactose
E542R mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
5.19
D-galactose
L537W/E542K mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
5.2
D-galactose
pH 7.3, 22°C, mutant enzyme E540K
5.49
D-galactose
L537W/E542R mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
5.77
D-galactose
L537G/E542R mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
5.9
D-galactose
-
pH 7.0, 25°C, reductive half-reaction, mutant T169S
6.01
D-galactose
L537G/E542K mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
6.1
D-galactose
pH 7.3, 22°C, mutant enzyme K312E with a C-terminal His6-tag
6.1
D-galactose
wild type enzyme, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
6.3
D-galactose
pH 7.3, 22°C, mutant enzyme E540K with a C-terminal His6-tag
6.38
D-galactose
R472G, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
6.6
D-galactose
-
pH 7.0, 25°C, reductive half-reaction, mutant T169N
7.21
D-galactose
R472L, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
7.39
D-galactose
N593R, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
7.73
D-galactose
-
at pH 6.5 and 25°C
7.8
D-galactose
mutant enzyme H450G/E542K/V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C
7.94
D-galactose
wild-type, mutant, 30°C, substrate D-galactose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
8.09
D-galactose
wild-type, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
8.2
D-galactose
pH 7.3, 22°C, wild-type enzyme
8.79
D-galactose
wild-type, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
8.79
D-galactose
His-tagged recombinant wild type enzyme, in 50 mM phosphate buffer (pH 6.5) at 60°C
8.79
D-galactose
wild type enzyme, pH and temperature not specified in the publication
9.27
D-galactose
H548R, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
9.4
D-galactose
L537W mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
9.47
D-galactose
L537G mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
9.89
D-galactose
H548I, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
10
D-galactose
mutant enzyme F454A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
10.4
D-galactose
V546C/T169N, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
11.81
D-galactose
100 mM ethanolamine buffer, pH 10.5
12
D-galactose
mutant enzyme H450G/V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C
12
D-galactose
mutant enzyme H450G/V546C, pH and temperature not specified in the publication
12.9
D-galactose
T169S, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
13
D-galactose
mutant enzyme F454A/S455A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
13
D-galactose
mutant enzyme F454P, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
13
D-galactose
-
pH 6.5, 30°C, recombinant enzyme
14.6
D-galactose
wild-type, mutant, 50°C, substrate D-galactose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
15
D-galactose
-
wild type enzyme, in 50 mM sodium phosphate (pH 7.0), at 25°C
16
D-galactose
-
mutant enzyme T169N, in 50 mM sodium phosphate (pH 7.0), at 25°C
16.2
D-galactose
-
mutant enzyme T169S, in 50 mM sodium phosphate (pH 7.0), at 25°C
24.6
D-galactose
-
V546C/E542K mutant, substrate D-galactose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
26
D-galactose
mutant enzyme F454N, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
29
D-galactose
mutant enzyme Y456W, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
29.4
D-galactose
V546G/T169G, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
34
D-galactose
mutant enzyme H450Q, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
45
D-galactose
-
pH 7.0, 37°C
46.2
D-galactose
V546C, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
46.2
D-galactose
mutant enzyme V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C
46.2
D-galactose
mutant enzyme V546C, pH and temperature not specified in the publication
50
D-galactose
-
mutant enzyme T169A, in 50 mM sodium phosphate (pH 7.0), at 25°C
50.6
D-galactose
V546P, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
101
D-galactose
-
with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 37°C
192
D-galactose
-
pH 6.5, 30°C, recombinant enzyme
200
D-galactose
V546G, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
750
D-galactose
Q448S, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
940
D-galactose
Q448N, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
1260
D-galactose
Q448C, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.018
D-glucose
mutant enzyme L547R, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C
0.042
D-glucose
mutant enzyme L545C, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C
0.046
D-glucose
mutant enzyme L545C, with O2 as electron acceptor, at pH 6.5 and 30°C
0.057
D-glucose
mutant enzyme Q448H, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C
0.082
D-glucose
mutant enzyme Q448H, with O2 as electron acceptor, at pH 6.5 and 30°C
0.092
D-glucose
mutant enzyme T166R, with O2 as electron acceptor, at pH 6.5 and 30°C
0.12
D-glucose
mutant enzyme L545C, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C
0.13
D-glucose
wild type enzyme, with O2 as electron acceptor, at pH 6.5 and 30°C
0.14
D-glucose
mutant enzyme N593C, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C
0.14
D-glucose
mutant enzyme T166R, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C
0.18
D-glucose
mutant enzyme N593C, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C
0.22
D-glucose
T169G/E542K/V546C, mutant, 30°C, substrate D-glucose (1,4-benzoquinone saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
0.23
D-glucose
mutant enzyme L547R, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C
0.24
D-glucose
mutant enzyme Q448H, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C
0.24
D-glucose
wild type enzyme, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C
0.25
D-glucose
wild type enzyme, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C
0.31
D-glucose
T169G/E542K/V546C, mutant, 50°C, substrate D-glucose (1,4-benzoquinone saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
0.314
D-glucose
at 30°C, pH 6.5
0.32
D-glucose
wild-type protein, 0.1 M ethanolamine buffer at pH 10.5
0.327
D-glucose
T169N, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.35
D-glucose
recombinant protein with a hexa-histidine tag, 0.1 M ethanolamine buffer at pH 10.5
0.394
D-glucose
T169S, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.4
D-glucose
pH 7.3, 22°C, mutant enzyme K312E with a C-terminal His6-tag
0.4
D-glucose
wild-type, mutant, 30°C, substrate D-glucose (1,4-benzoquinone saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
0.4
D-glucose
mutant enzyme L547R, with O2 as electron acceptor, at pH 6.5 and 30°C
0.419
D-glucose
L537W/E542R mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.432
D-glucose
L537W/E542K mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.44
D-glucose
-
V546C/T169G mutant, substrate D-glucose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.44
D-glucose
mutant enzyme T196G/V546C, pH and temperature not specified in the publication
0.441
D-glucose
L537G/E542R mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.487
D-glucose
L537G/E542K mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.489
D-glucose
E542R mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.49
D-glucose
-
V546C/T169G/L537W mutant, substrate D-glucose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.5
D-glucose
mutant T166A/E539K, pH 6.5, 30°C
0.521
D-glucose
E542K mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.521
D-glucose
mutant enzyme E542K, in 50 mM phosphate buffer (pH 6.5) at 60°C
0.527
D-glucose
N593R, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.56
D-glucose
mutant enzyme Q448H, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C
0.58
D-glucose
immobilized enzyme, pH 6.5, 25°C
0.6
D-glucose
pH 7.3, 22°C, mutant enzyme E540K
0.6
D-glucose
pH 7.3, 22°C, mutant enzyme E540K with a C-terminal His6-tag
0.6
D-glucose
mutant K312E/E539K, pH 6.5, 30°C
0.61
D-glucose
-
pH 6.5, 30°C
0.64
D-glucose
T169G/E542K/V546C, mutant, 30°C, substrate D-glucose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
0.658
D-glucose
V546P/T169G, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.69
D-glucose
mutant enzyme T169G, pH and temperature not specified in the publication
0.691
D-glucose
T169G, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.698
D-glucose
wild-type, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.7
D-glucose
mutant E359K, pH 6.5, 30°C
0.712
D-glucose
-
mutant enzyme F454A, at pH 6.5 and 30°C
0.72
D-glucose
mutant enzyme L545C, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C
0.74
D-glucose
-
at pH 6.5 and 25°C
0.749
D-glucose
L537W mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.76
D-glucose
wild-type, mutant, 30°C, substrate D-glucose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
0.76
D-glucose
wild type enzyme, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.77
D-glucose
mutant enzyme H450G/E542K/V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C
0.773
D-glucose
R472G, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.78
D-glucose
wild-type, mutant, 50°C, substrate D-glucose (1,4-benzoquinone saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
0.8
D-glucose
pH 7.3, 22°C, recombinant wild-type enzyme
0.8
D-glucose
mutant K312E, pH 6.5, 30°C
0.8 - 11
D-glucose
H548I, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.81
D-glucose
mutant enzyme N593C, with 1 ferrocenium ion as electron acceptor, at pH 6.5 and 30°C
0.82
D-glucose
-
oxygen concentration 0.25 mM
0.84
D-glucose
substrate D-glucose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.851
D-glucose
L537G mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.851
D-glucose
-
wild type enzyme, at pH 6.5 and 30°C
0.88
D-glucose
H548R, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.886
D-glucose
R472L, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.9
D-glucose
-
mutant enzyme T169G, in 50 mM sodium phosphate (pH 7.0), at 4°C
0.93
D-glucose
native enzyme, pH 6.5, 25°C
0.939
D-glucose
wild-type, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.939
D-glucose
wild type enzyme, pH and temperature not specified in the publication
0.948
D-glucose
-
wild type enzyme F454Y, at pH 6.5 and 30°C
0.952
D-glucose
V546C/T169N, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.98
D-glucose
mutant enzyme N593C, with O2 as electron acceptor, at pH 6.5 and 30°C
0.984
D-glucose
V546G/T169G, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.987
D-glucose
mutant enzyme H450G, in 50 mM phosphate buffer (pH 6.5) at 60°C
0.987
D-glucose
mutant enzyme H450G, pH and temperature not specified in the publication
0.99
D-glucose
His-tagged recombinant wild type enzyme, in 50 mM phosphate buffer (pH 6.5) at 60°C
1
D-glucose
Lenzites styracinus
-
-
1.09
D-glucose
-
oxygen concentration 1.07 mM
1.1
D-glucose
pH 7.3, 22°C, wild-type enzyme
1.1
D-glucose
-
with O2 as electron acceptor, at pH 6.5 and 37°C
1.13
D-glucose
-
wild type enzyme, in 50 mM sodium phosphate (pH 7.0), at 4°C
1.15
D-glucose
T169G/E542K/V546C, mutant, 50°C, substrate D-glucose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
1.18
D-glucose
wild-type, mutant, 50°C, substrate D-glucose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
1.2
D-glucose
wild-type, pH 6.5, 30°C
1.28
D-glucose
-
pH 7.0, 37°C
1.5
D-glucose
mutant enzyme F454A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
1.5
D-glucose
mutant enzyme F454N, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
1.5 - 2
D-glucose
-
V546C/E542K mutant, substrate D-glucose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
1.51
D-glucose
E542K with a hexa-histidine tag, 0.1 M ethanolamine buffer at pH 10.5
1.6
D-glucose
mutant enzyme T166R, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C
1.7
D-glucose
-
mutant enzyme T169S, in 50 mM sodium phosphate (pH 7.0), at 4°C
1.7
D-glucose
mutant enzyme Y456W, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
1.7
D-glucose
mutant enzyme L547R, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C
1.77
D-glucose
-
pH 6.5, 30°C, recombinant enzyme
1.8
D-glucose
mutant enzyme F454P, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
1.9
D-glucose
-
O2 concentration constant, pH 7.0, absorbance at 420 nm resulting from the oxidation of diammonium-2,2'-azinobis-(3-ethylbenzthiazolin-6-sulfonic acid) by H2O2
1.9
D-glucose
wild type enzyme, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C
2.1
D-glucose
mutant enzyme F454A/S455A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
2.1
D-glucose
mutant enzyme T166R, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C
2.1
D-glucose
-
with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 37°C
2.2
D-glucose
V546P, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
2.3
D-glucose
-
wild type enzyme, at pH 6.5, temperature not specified in the publication
2.43
D-glucose
mutant enzyme H450G/V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C
2.43
D-glucose
mutant enzyme H450G/V546C, pH and temperature not specified in the publication
2.5
D-glucose
mutant enzyme H450Q, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
2.5
D-glucose
-
mutant enzyme N593C, at pH 6.5, temperature not specified in the publication
2.72
D-glucose
recombinant protein, 0.1 M PBS buffer at pH 8
2.86
D-glucose
-
pH 6.5, 30°C, recombinant enzyme
3.06
D-glucose
V546C, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
3.06
D-glucose
mutant enzyme V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C
3.06
D-glucose
mutant enzyme V546C, pH and temperature not specified in the publication
3.1
D-glucose
pH and temperature not specified in the publication
3.2
D-glucose
-
O2 concentration constant, pH 7.0, calculated with kinetic equation
4.6
D-glucose
-
mutant enzyme T169N, in 50 mM sodium phosphate (pH 7.0), at 4°C
5.7
D-glucose
V546G, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
5.97
D-glucose
mutant enzyme H167A, pH and temperature not specified in the publication
28
D-glucose
Q448N, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
30
D-glucose
Q448S, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
30
D-glucose
-
mutant enzyme T169A, in 50 mM sodium phosphate (pH 7.0), at 4°C
45
D-glucose
-
pH 7.0, 25°C, reductive half-reaction, wild-type enzyme and mutant T169S
47
D-glucose
-
pH 7.0, 25°C, reductive half-reaction, mutant T169N
100
D-glucose
Q448C, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
240
D-glucose
-
at pH 4.5
295
D-mannose
-
pH 7.0, 37°C
370
D-mannose
-
at pH 6.5 and 25°C
2 - 3
D-melibiose
mutant enzyme F454A/S455A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
50
D-melibiose
mutant enzyme F454P, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
240
D-melibiose
mutant enzyme F454N, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
260
D-melibiose
mutant enzyme Y456W, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
350
D-melibiose
mutant enzyme F454A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
390
D-melibiose
mutant enzyme H450Q, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
1500
D-melibiose
wild type enzyme, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
2.4
D-xylose
pH 7.3, 22°C, mutant enzyme K312E with a C-terminal His6-tag
6.21
D-xylose
100 mM ethanolamine buffer, pH 10.5
6.3
D-xylose
at 30°C, pH 6.5
6.3
D-xylose
immobilized enzyme, pH 6.5, 25°C
6.6
D-xylose
pH 7.3, 22°C, mutant enzyme E540K with a C-terminal His6-tag
7.9
D-xylose
pH 7.3, 22°C, mutant enzyme E540K
18.1
D-xylose
-
pH 6.5, 30°C, recombinant enzyme
18.4
D-xylose
native enzyme, pH 6.5, 25°C
20.9
D-xylose
substrate D-xylose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
25
D-xylose
-
oxygen concentration 1.07 mM
25
D-xylose
pH 7.3, 22°C, recombinant wild-type enzyme
25.9
D-xylose
-
at pH 6.5 and 25°C
29.4
D-xylose
pH 7.3, 22°C, wild-type enzyme
45.8
D-xylose
-
pH 7.0, 37°C
66.9
D-xylose
-
pH 6.5, 30°C, recombinant enzyme
73
D-xylose
-
with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 37°C
78.4
D-xylose
pH and temperature not specified in the publication
0.092
ferricenium hexafluorophosphate
-
V546C/T169G/L537W mutant, substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.092
ferricenium hexafluorophosphate
-
mutant enzyme V546C/T169G/L537W, at pH 6.5 and 30°C
0.15
ferricenium hexafluorophosphate
-
V546C/E542K mutant, substrate ferricenium hexafluorophosphate (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.15
ferricenium hexafluorophosphate
-
mutant enzyme V546C/E542K, at pH 6.5 and 30°C
0.22
ferricenium hexafluorophosphate
-
V546C/T169G/L537W mutant, substrate ferricenium hexafluorophosphate (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.22
ferricenium hexafluorophosphate
-
mutant enzyme V546C/T169G/L537W, at pH 6.5 and 30°C
0.29
ferricenium hexafluorophosphate
substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 8.0
0.31
ferricenium hexafluorophosphate
-
V546C/T169G mutant, substrate ferricenium hexafluorophosphate (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.31
ferricenium hexafluorophosphate
-
mutant enzyme V546C/T169G, at pH 6.5 and 30°C
0.33
ferricenium hexafluorophosphate
substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.5
ferricenium hexafluorophosphate
-
V546C/T169G mutant, substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.5
ferricenium hexafluorophosphate
-
mutant enzyme V546C/T169G, at pH 6.5 and 30°C
0.67
ferricenium hexafluorophosphate
-
pH 8.0, 30°C, recombinant enzyme
1.06
ferricenium hexafluorophosphate
-
V546C/E542K mutant, substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
1.12
ferricenium hexafluorophosphate
-
pH 8.0, 30°C, recombinant enzyme
0.054
ferricenium ion
L537G/E542R mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.054
ferricenium ion
mutant enzyme L537G/E542R, at pH 6.5 and 30°C
0.063
ferricenium ion
L537W mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.063
ferricenium ion
mutant enzyme L537W, at pH 6.5 and °C
0.068
ferricenium ion
E542K mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.068
ferricenium ion
mutant enzyme E542K, at pH 6.5 and 30°C
0.07
ferricenium ion
wild-type, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.07
ferricenium ion
wild type enzyme, at pH 6.5 and 30°C
0.072
ferricenium ion
L537G/E542K mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.072
ferricenium ion
mutant enzyme L537G/E542K, at pH 6.5 and 30°C
0.074
ferricenium ion
L537W/E542R mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.074
ferricenium ion
mutant enzyme L537W/E542R, at pH 6.5 and 30°C
0.086
ferricenium ion
L537G mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.086
ferricenium ion
mutant enzyme L537G, at pH 6.5 and 30°C
0.09
ferricenium ion
L537W/E542K mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.09
ferricenium ion
mutant enzyme L537W/E542K, at pH 6.5 and 30°C
0.183
ferricenium ion
E542R mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.183
ferricenium ion
mutant enzyme E542R, at pH 6.5 and 30°C
0.253
ferricenium ion
L537W mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.253
ferricenium ion
mutant enzyme L537W, at pH 6.5 and 30°C
0.254
ferricenium ion
wild-type, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.254
ferricenium ion
wild type enzyme, at pH 6.5 and 30°C
0.281
ferricenium ion
L537W/E542R mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.281
ferricenium ion
mutant enzyme L537W/E542R, at pH 6.5 and 30°C
0.289
ferricenium ion
L537G mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.289
ferricenium ion
mutant enzyme L537G, at pH 6.5 and 30°C
0.29
ferricenium ion
E542K mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.29
ferricenium ion
mutant enzyme E542K, at pH 6.5 and 30°C
0.296
ferricenium ion
L537G/E542K mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.296
ferricenium ion
mutant enzyme L537G/E542K, at pH 6.5 and 30°C
0.319
ferricenium ion
E542R mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.319
ferricenium ion
mutant enzyme E542R, at pH 6.5 and 30°C
0.328
ferricenium ion
L537G/E542R mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.328
ferricenium ion
mutant enzyme L537G/E542K, at pH 6.5 and 30°C
0.408
ferricenium ion
L537W/E542K mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
0.408
ferricenium ion
mutant enzyme L537W/E542K, at pH 6.5 and 30°C
0.015
ferrocenium hexafluorophosphate
mutant enzyme F454A/S455A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.016
ferrocenium hexafluorophosphate
mutant enzyme F454A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.023
ferrocenium hexafluorophosphate
mutant enzyme F454P, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.025
ferrocenium hexafluorophosphate
mutant enzyme F454N, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.041
ferrocenium hexafluorophosphate
mutant enzyme Y456W, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.049
ferrocenium hexafluorophosphate
mutant enzyme H450Q, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.1
ferrocenium hexafluorophosphate
wild type enzyme, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.14
ferrocenium hexafluorophosphate
mutant enzyme F454P, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.15
ferrocenium hexafluorophosphate
mutant enzyme F454A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.24
ferrocenium hexafluorophosphate
mutant enzyme Y456W, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.28
ferrocenium hexafluorophosphate
mutant enzyme F454A/S455A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.35
ferrocenium hexafluorophosphate
mutant enzyme F454N, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.38
ferrocenium hexafluorophosphate
mutant enzyme H450Q, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.4
ferrocenium hexafluorophosphate
wild type enzyme, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.79
glucose
-
immobilized enzyme, O2 used as electron acceptor, determined in cuvette assay, pH 5.0
0.85
glucose
-
soluble enzyme, O2 used as electron acceptor, determined in cuvette assay, pH 5.0
1.55
L-arabinose
100 mM ethanolamine buffer, pH 10.5
14
L-arabinose
-
with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 37°C
2.9
L-sorbose
pH 7.3, 22°C, mutant enzyme K312E with a C-terminal His6-tag
5
L-sorbose
pH 7.3, 22°C, mutant enzyme E540K
5.4
L-sorbose
pH 7.3, 22°C, mutant enzyme E540K with a C-terminal His6-tag
14.7
L-sorbose
at 30°C, pH 6.5
23.5
L-sorbose
substrate L-sorbose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
26.4
L-sorbose
-
pH 7.0, 37°C
32.6
L-sorbose
-
pH 6.5, 30°C, recombinant enzyme
39.3
L-sorbose
-
at pH 6.5 and 25°C
47
L-sorbose
pH 7.3, 22°C, recombinant wild-type enzyme
50
L-sorbose
pH 7.3, 22°C, wild-type enzyme
108
L-sorbose
-
oxygen concentration 1.07 mM
176
L-sorbose
-
pH 6.5, 30°C, recombinant enzyme
46.4
maltose
-
at pH 6.5 and 25°C
257
maltose
-
oxygen concentration 1.07 mM
0.35
methyl-1,4-benzoquinone
-
pH 4.5, substrate: D-glucose
0.35
methyl-1,4-benzoquinone
-
at pH 4.5 and 30°C
0.4
methyl-1,4-benzoquinone
-
pH 6.5, substrate: D-glucose
0.4
methyl-1,4-benzoquinone
-
at pH 6.5 and 30°C
50
methyl-beta-D-glucoside
pH 7.3, 22°C, mutant enzyme K312E with a C-terminal His6-tag
256
methyl-beta-D-glucoside
pH 7.3, 22°C, mutant enzyme E540K
261
methyl-beta-D-glucoside
pH 7.3, 22°C, mutant enzyme E540K with a C-terminal His6-tag
289
methyl-beta-D-glucoside
pH 7.3, 22°C, wild-type enzyme
0.03
O2
-
wild type enzyme, using D-galactose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 25°C
0.04
O2
-
pH 5.5, substrate oxygen limited (D-glucose excess), measuring oxygen consumption (computer-interfaced Oxy-32 oxygen-monitoring system), 30°C
0.04
O2
-
pH 8.5, substrate D-glucose limited (oxygen excess), measuring oxygen consumption (computer-interfaced Oxy-32 oxygen-monitoring system), 30°C
0.07
O2
-
mutant enzyme T169S, using D-galactose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 25°C
0.09
O2
-
wild type enzyme, using D-glucose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 4°C
0.1
O2
-
pH 6.5, substrate oxygen limited (D-glucose excess), measuring oxygen consumption (computer-interfaced Oxy-32 oxygen-monitoring system), 30°C
0.1
O2
-
pH 7.5, substrate oxygen limited (D-glucose excess), measuring oxygen consumption (computer-interfaced Oxy-32 oxygen-monitoring system), 30°C
0.11
O2
-
soluble enzyme, 500 mM glucose used as electron acceptor, pH 5.0
0.132
O2
-
glucose concentration constant, pH 7.0, calculated with kinetic equation
0.2
O2
-
pH 7.5, substrate D-glucose limited (oxygen excess), measuring oxygen consumption (computer-interfaced Oxy-32 oxygen-monitoring system), 30°C
0.2
O2
-
mutant enzyme T169A, using D-glucose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 4°C
0.22
O2
-
D-glucose concentration constant, pH 7.0, absorbance at 420 nm resulting from the oxidation of diammonium-2,2'-azinobis-(3-ethylbenzthiazolin-6-sulfonic acid) by H2O2
0.3
O2
-
pH 5.5, substrate D-glucose limited (oxygen excess), measuring oxygen consumption (computer-interfaced Oxy-32 oxygen-monitoring system), 30°C
0.4
O2
-
mutant enzyme T169A, using D-galactose as cosubstrate,in 50 mM sodium phosphate (pH 7.0), at 25°C
0.46
O2
pH and temperature not specified in the publication
0.5
O2
-
pH 8.5, substrate oxygen limited (D-glucose excess), measuring oxygen consumption (computer-interfaced Oxy-32 oxygen-monitoring system), 30°C
0.9
O2
-
pH 6.5, substrate D-glucose limited (oxygen excess), measuring oxygen consumption (computer-interfaced Oxy-32 oxygen-monitoring system), 30°C
0.99
O2
-
mutant enzyme T169S, using D-glucose as cosubstrate ,in 50 mM sodium phosphate (pH 7.0), at 4°C
1.22
O2
substrate O2 (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
1.32
O2
-
mutant enzyme T169N, using D-galactose as cosubstrate,in 50 mM sodium phosphate (pH 7.0), at 25°C
3.7
O2
-
mutant enzyme T169G, using D-galactose as cosubstrate,in 50 mM sodium phosphate (pH 7.0), at 25°C
4.5
O2
-
mutant enzyme T169G, using D-glucose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 4°C
4.8
O2
-
mutant enzyme T169N, using D-glucose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 4°C
0.0832
oxygen
-
-
0.09
oxygen
-
pH 6.5, substrate: D-glucose
0.65
oxygen
-
in the presence of glucose
0.09
tetrabromo-1,4-benzoquinone
-
pH 6.5, substrate: D-glucose
0.09
tetrabromo-1,4-benzoquinone
-
at pH 6.5 and 30°C
0.22
tetrafluoro-1,4-benzoquinone
-
pH 6.5, substrate: D-glucose
0.64
tetrafluoro-1,4-benzoquinone
substrate tetrafluoro-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
9.42
tetrafluoro-1,4-benzoquinone
-
pH 6.5, 30°C, recombinant enzyme
additional information
additional information
Michaelis-Menten kinetics, overview
-
additional information
additional information
D-mannose, glucosamine, beta-lactose, sucrose and D-maltose lack response signal, higher maltooligosaccharides good substrates for pyranose 2-oxidase-based biosensor
-
additional information
additional information
-
kinetic parameters of the reaction measured (substrates D-glucose or 2-deoxy-D-glucose), pH 7.0
-
additional information
additional information
-
steady-state and pre-steady-state kinetics, and kinetic isotope effects, of oxidative half-reaction and overall reaction, overview
-
additional information
additional information
-
the steady-state kinetics of P2O can be classified as a ping pong bi-bi type, because the 2-keto-sugar product is released prior to the oxygen reaction, transient kinetics and isotope effects, overview
-
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0.39 - 477
1,4-benzoquinone
76.7
1,5-anhydro-D-glucitol
-
pH 7.0, 37°C
1.33
2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) cation radical
substrate 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) cation radical (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
13.1 - 108
2,6-dichloroindophenol
0.4 - 8.69
2,6-dimethyl-1,4-benzoquinone
0.15 - 16.3
2-chloro-1,4-benzoquinone
40.1 - 47.2
2-methoxy-1,4-benzoquinone
0.12 - 10.1
2-methyl-1,4-benzoquinone
6.01
cellobiose
-
at pH 6.5 and 25°C
7.79
D-arabinose
-
pH 7.0, 37°C
36.1
D-glucono-1,5-lactone
-
at pH 6.5 and 25°C
62.9
D-maltose
-
pH 7.0, 37°C
0.38
D-ribose
-
with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 37°C
1.7 - 549
ferricenium hexafluorophosphate
1.44 - 334
ferricenium ion
0.3
ferricyanide
substrate ferricyanide (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
2.9 - 470
ferrocenium hexafluorophosphate
39.9
ferrocenium ion
using D-glucose as cosubstrate, at 30°C, pH 6.5
49
glucose
-
soluble enzyme, O2 used as electron acceptor, determined in cuvette assay, pH 5.0
0.19
L-arabinose
-
with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 37°C
31.1
maltose
-
at pH 6.5 and 25°C
0.839
melibiose
at 30°C, pH 6.5
27.9
sucrose
-
at pH 6.5 and 25°C
6.61 - 129
tetrafluoro-1,4-benzoquinone
59.6
trehalose
-
pH 7.0, 37°C
0.39
1,4-benzoquinone
-
with D-glucose as cosubstrate, at pH 6.5 and 37°C
1.2
1,4-benzoquinone
mutant enzyme F454A/S455A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
2
1,4-benzoquinone
mutant enzyme F454P, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
2.7
1,4-benzoquinone
mutant enzyme F454N, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
2.9
1,4-benzoquinone
mutant enzyme F454A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
3
1,4-benzoquinone
mutant enzyme H450Q, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
3.04
1,4-benzoquinone
-
pH 6.5, 30°C, recombinant enzyme
3.3
1,4-benzoquinone
mutant enzyme Y456W, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
3.8
1,4-benzoquinone
wild type enzyme, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
4.37
1,4-benzoquinone
E542R mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
4.64
1,4-benzoquinone
L537G mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
4.72
1,4-benzoquinone
L537G/E542K mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
4.75
1,4-benzoquinone
L537G/E542R mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
4.77
1,4-benzoquinone
L537W/E542R mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
4.79
1,4-benzoquinone
wild-type, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
5.09
1,4-benzoquinone
L537W/E542K mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
5.37
1,4-benzoquinone
L537W mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
5.52
1,4-benzoquinone
E542K mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
15
1,4-benzoquinone
mutant enzyme F454A/S455A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
30
1,4-benzoquinone
mutant enzyme F454P, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
61
1,4-benzoquinone
mutant enzyme F454A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
92.3
1,4-benzoquinone
using D-glucose as cosubstrate, at 30°C, pH 6.5
127
1,4-benzoquinone
E542R mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
130
1,4-benzoquinone
mutant enzyme F454N, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
152
1,4-benzoquinone
wild-type, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
160
1,4-benzoquinone
wild type enzyme, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
173
1,4-benzoquinone
L537G/E542K mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
173
1,4-benzoquinone
L537G/E542R mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
175
1,4-benzoquinone
L537W/E542R mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
181
1,4-benzoquinone
L537W/E542K mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
184
1,4-benzoquinone
L537G mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
186
1,4-benzoquinone
-
pH 6.5, 30°C, recombinant enzyme
189
1,4-benzoquinone
E542K mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
205
1,4-benzoquinone
L537W mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
220
1,4-benzoquinone
mutant enzyme H450Q, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
220
1,4-benzoquinone
mutant enzyme Y456W, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
324
1,4-benzoquinone
-
soluble enzyme, 500 mM glucose used as electron acceptor, pH 5.0
400
1,4-benzoquinone
substrate 1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
477
1,4-benzoquinone
substrate 1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 4.5
13.1
2,6-dichloroindophenol
-
pH 6.5, 30°C, recombinant enzyme
67.3
2,6-dichloroindophenol
using D-glucose as cosubstrate, at 30°C, pH 6.5
108
2,6-dichloroindophenol
substrate 2,6-dichloroindophenol (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.4
2,6-dimethyl-1,4-benzoquinone
-
pH 6.5, 30°C, recombinant enzyme
8.69
2,6-dimethyl-1,4-benzoquinone
substrate 2,6-dimethyl-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
0.15
2-chloro-1,4-benzoquinone
substrate 2-chloro-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
16.3
2-chloro-1,4-benzoquinone
-
pH 6.5, 30°C, recombinant enzyme
40.1
2-methoxy-1,4-benzoquinone
substrate 2-methoxy-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
47.2
2-methoxy-1,4-benzoquinone
-
pH 6.5, 30°C, recombinant enzyme
0.12
2-methyl-1,4-benzoquinone
substrate 2-methyl-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
10.1
2-methyl-1,4-benzoquinone
-
pH 6.5, 30°C, recombinant enzyme
1.88
D-fructose
substrate D-fructose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
4.19
D-fructose
-
at pH 6.5 and 25°C
5.55
D-fructose
-
pH 6.5, 30°C, recombinant enzyme
0.02
D-galactose
-
pH 6.5, 30°C, recombinant enzyme
0.14
D-galactose
mutant enzyme F454A/S455A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.245
D-galactose
V546P/T169G, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.27
D-galactose
T169G/E542K/V546C, mutant, 30°C, substrate D-galactose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
0.27
D-galactose
mutant enzyme T169G, pH and temperature not specified in the publication
0.273
D-galactose
T169G, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.3
D-galactose
mutant enzyme F454P, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.3
D-galactose
-
pH 7.0, 25°C, reductive half-reaction, wild-type enzyme
0.331
D-galactose
V546G/T169G, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.356
D-galactose
H548R, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.38
D-galactose
mutant enzyme T196G/V546C, pH and temperature not specified in the publication
0.433
D-galactose
Q448N, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.5
D-galactose
-
pH 7.0, 25°C, reductive half-reaction, mutant T169S
0.57
D-galactose
-
with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 37°C
0.622
D-galactose
Q448C, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.64
D-galactose
mutant enzyme F454A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.654
D-galactose
V546C/T169N, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.7
D-galactose
-
mutant enzyme T169G, in 50 mM sodium phosphate (pH 7.0), at 25°C
0.74
D-galactose
T169G/E542K/V546C, mutant, 50°C, substrate D-galactose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
0.9
D-galactose
-
pH 7.0, 25°C, reductive half-reaction, mutant T169N
1.02
D-galactose
at 30°C, pH 6.5
1.2
D-galactose
mutant enzyme F454N, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
1.2
D-galactose
-
wild type enzyme, in 50 mM sodium phosphate (pH 7.0), at 25°C
1.5
D-galactose
mutant enzyme Y456W, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
1.53
D-galactose
Q448S, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
1.57
D-galactose
N593R, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
1.6
D-galactose
V546P, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
1.69
D-galactose
R472L, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
1.7
D-galactose
wild type enzyme, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
1.95
D-galactose
-
pH 6.5, 30°C, recombinant enzyme
1.96
D-galactose
T169N, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
1.99
D-galactose
E542R mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
2
D-galactose
mutant enzyme H450Q, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
2.07
D-galactose
R472G, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
2.1
D-galactose
wild-type, mutant, 30°C, substrate D-galactose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
2.34
D-galactose
L537G/E542K mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
2.36
D-galactose
L537G/E542R mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
2.48
D-galactose
L537W/E542R mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
2.51
D-galactose
L537W/E542K mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
2.51
D-galactose
wild-type, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
2.51
D-galactose
His-tagged recombinant wild type enzyme, in 50 mM phosphate buffer (pH 6.5) at 60°C
2.51
D-galactose
wild type enzyme, pH and temperature not specified in the publication
2.56
D-galactose
L537G mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
2.59
D-galactose
E542K mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
2.59
D-galactose
mutant enzyme E542K, in 50 mM phosphate buffer (pH 6.5) at 60°C
2.66
D-galactose
H548I, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
2.7
D-galactose
-
pH 7.0, 25°C, reductive half-reaction, mutant T169G
2.73
D-galactose
wild-type, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
2.84
D-galactose
mutant enzyme H450G/E542K/V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C
2.9
D-galactose
L537W mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
3.51
D-galactose
mutant enzyme H450G, in 50 mM phosphate buffer (pH 6.5) at 60°C
3.51
D-galactose
mutant enzyme H450G, pH and temperature not specified in the publication
4.51
D-galactose
V546G, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
4.87
D-galactose
substrate D-galactose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
5.51
D-galactose
wild-type, mutant, 50°C, substrate D-galactose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
5.53
D-galactose
T169S, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
5.92
D-galactose
mutant enzyme H450G/V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C
5.92
D-galactose
mutant enzyme H450G/V546C, pH and temperature not specified in the publication
6.57
D-galactose
V546C, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
6.57
D-galactose
mutant enzyme V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C
6.57
D-galactose
mutant enzyme V546C, pH and temperature not specified in the publication
6.61
D-galactose
wild-type, mutant, 30°C, substrate D-galactose (1,4-benzoquinone saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
13.1
D-galactose
-
at pH 6.5 and 25°C
13.7
D-galactose
-
mutant enzyme T169S, in 50 mM sodium phosphate (pH 7.0), at 25°C
14.6
D-galactose
wild-type, mutant, 50°C, substrate D-galactose (1,4-benzoquinone saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
22.5
D-galactose
-
pH 7.0, 37°C
171
D-galactose
T169G/E542K/V546C, mutant, 50°C, substrate D-galactose (1,4-benzoquinone saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
0.006
D-glucose
-
pH 6.0, 25°C, mutant H167A/H548R
0.018
D-glucose
-
pH 7.0, 25°C, mutant H167A/H548R
0.057
D-glucose
-
pH 8.0, 25°C, mutant H167A/H548R
0.06
D-glucose
-
mutant enzyme T169A, in 50 mM sodium phosphate (pH 7.0), at 4°C
0.072
D-glucose
T169G/E542K/V546C, mutant, 30°C, substrate D-glucose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
0.119
D-glucose
V546G/T169G, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.153
D-glucose
-
with O2 as electron acceptor, at pH 6.5 and 37°C
0.18
D-glucose
mutant enzyme N593C, with O2 as electron acceptor, at pH 6.5 and 30°C
0.2
D-glucose
mutant enzyme F454A/S455A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.232
D-glucose
V546P/T169G, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.26
D-glucose
mutant enzyme T169G, pH and temperature not specified in the publication
0.262
D-glucose
T169G, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.35
D-glucose
T169G/E542K/V546C, mutant, 50°C, substrate D-glucose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
0.38
D-glucose
mutant enzyme Q448H, with O2 as electron acceptor, at pH 6.5 and 30°C
0.43
D-glucose
mutant enzyme T196G/V546C, pH and temperature not specified in the publication
0.479
D-glucose
-
mutant enzyme F454A, at pH 6.5 and 30°C
0.48
D-glucose
-
with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 37°C
0.63
D-glucose
-
pH 9.5, 25°C, mutant H167A/H548R
0.7
D-glucose
-
pH 7.0, 25°C, reductive half-reaction, mutant T169G
0.963
D-glucose
V546C/T169N, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
0.99
D-glucose
mutant enzyme F454P, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
1.1
D-glucose
mutant enzyme L547R, with O2 as electron acceptor, at pH 6.5 and 30°C
1.48
D-glucose
-
pH 6.5, 30°C, recombinant enzyme
1.51
D-glucose
Q448C, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
1.6
D-glucose
-
pH 10.25, 25°C, mutant H167A/H548R
2.06
D-glucose
mutant enzyme H167A, pH and temperature not specified in the publication
2.13
D-glucose
-
pH 10.5, 25°C, mutant H167A/H548R
2.41
D-glucose
T169N, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
2.7
D-glucose
-
substrate 1,4-benzoquinone (100 mM D-glucose), pH 4.5
2.7
D-glucose
mutant enzyme L545C, with O2 as electron acceptor, at pH 6.5 and 30°C
2.9
D-glucose
mutant T166A/E539K, pH 6.5, 30°C
3.9
D-glucose
mutant enzyme N593C, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C
4.6
D-glucose
mutant enzyme N593C, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C
4.73
D-glucose
Q448N, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
5.4
D-glucose
-
substrate D-glucose (air saturated), pH 6.5
5.42
D-glucose
Q448S, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
5.6
D-glucose
-
mutant enzyme T169N, in 50 mM sodium phosphate (pH 7.0), at 4°C
6.1
D-glucose
wild-type, pH 6.5, 30°C
6.81
D-glucose
mutant enzyme H450G/E542K/V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C
6.92
D-glucose
at 30°C, pH 6.5
7.1
D-glucose
-
substrate O2 (100 mM D-glucose), pH 6.5
7.1
D-glucose
mutant enzyme F454A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
7.6
D-glucose
mutant E359K, pH 6.5, 30°C
7.6
D-glucose
mutant K312E/E539K, pH 6.5, 30°C
7.67
D-glucose
-
pH 7.0, calculated with kinetic equation
8.1
D-glucose
mutant enzyme Q448H, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C
8.15
D-glucose
-
pH 7.0, absorbance at 420 nm resulting from the oxidation of diammonium-2,2'-azinobis-(3-ethylbenzthiazolin-6-sulfonic acid) by H2O2
8.5
D-glucose
mutant K312E, pH 6.5, 30°C
9.2
D-glucose
H548R, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
9.7
D-glucose
-
wild type enzyme, in 50 mM sodium phosphate (pH 7.0), at 4°C
9.7
D-glucose
-
pH 7.0, 25°C, reductive half-reaction, mutant T169N
11
D-glucose
mutant enzyme T166R, with O2 as electron acceptor, at pH 6.5 and 30°C
12
D-glucose
mutant enzyme F454N, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
12
D-glucose
mutant enzyme Q448H, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C
12.5
D-glucose
mutant enzyme H450G, in 50 mM phosphate buffer (pH 6.5) at 60°C
12.5
D-glucose
mutant enzyme H450G, pH and temperature not specified in the publication
13.8
D-glucose
-
pH 7.0, 25°C, reductive half-reaction, mutant T169S
15.3
D-glucose
-
pH 7.0, 25°C, reductive half-reaction, wild-type enzyme
15.6
D-glucose
N593R, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
15.8
D-glucose
V546P, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
16.3
D-glucose
-
wild type enzyme F454Y, at pH 6.5 and 30°C
16.8
D-glucose
mutant enzyme H450G/V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C
16.8
D-glucose
mutant enzyme H450G/V546C, pH and temperature not specified in the publication
17
D-glucose
mutant enzyme H450Q, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
21.16
D-glucose
T169G/E542K/V546C, mutant, 30°C, substrate D-glucose (1,4-benzoquinone saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
21.8
D-glucose
T169S, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
22
D-glucose
mutant enzyme N593C, with 1 ferrocenium ion as electron acceptor, at pH 6.5 and 30°C
23.6
D-glucose
V546G, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
26
D-glucose
mutant enzyme Y456W, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
26
D-glucose
mutant enzyme L547R, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C
27
D-glucose
mutant enzyme Q448H, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C
28.5
D-glucose
E542R mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
30.9
D-glucose
R472L, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
31.6
D-glucose
H548I, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
31.7
D-glucose
L537W/E542R mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
32.2
D-glucose
R472G, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
33
D-glucose
wild type enzyme, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
33.1
D-glucose
L537G/E542R mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
33.8
D-glucose
-
at pH 6.5 and 25°C
34
D-glucose
wild-type, mutant, 30°C, substrate D-glucose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
35.4
D-glucose
wild-type, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
35.44
D-glucose
-
pH 6.5, 30°C, recombinant enzyme
35.9
D-glucose
E542K mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
35.9
D-glucose
mutant enzyme E542K, in 50 mM phosphate buffer (pH 6.5) at 60°C
42
D-glucose
wild type enzyme, with O2 as electron acceptor, at pH 6.5 and 30°C
43.9
D-glucose
L537G/E542K mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
46.5
D-glucose
L537W/E542K mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
48.1
D-glucose
wild-type, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
48.1
D-glucose
His-tagged recombinant wild type enzyme, in 50 mM phosphate buffer (pH 6.5) at 60°C
48.1
D-glucose
wild type enzyme, pH and temperature not specified in the publication
49
D-glucose
-
wild type enzyme, at pH 6.5 and 30°C
50
D-glucose
mutant enzyme L545C, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C
52.1
D-glucose
L537G mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
58.9
D-glucose
wild-type, mutant, 50°C, substrate D-glucose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
59
D-glucose
L537W mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
70
D-glucose
wild type enzyme, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C
79.3
D-glucose
T169G/E542K/V546C, mutant, 50°C, substrate D-glucose (1,4-benzoquinone saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
83.1
D-glucose
substrate D-glucose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
88.6
D-glucose
V546C, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay
88.6
D-glucose
mutant enzyme V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C
88.6
D-glucose
mutant enzyme V546C, pH and temperature not specified in the publication
110
D-glucose
mutant enzyme L545C, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C
111
D-glucose
-
pH 7.0, 37°C
134
D-glucose
mutant enzyme L547R, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C
134
D-glucose
mutant enzyme L547R, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C
142
D-glucose
mutant enzyme L545C, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C
151
D-glucose
wild type enzyme, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C
152
D-glucose
wild type enzyme, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C
166
D-glucose
mutant enzyme T166R, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C
265
D-glucose
mutant enzyme T166R, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C
349
D-glucose
wild-type, mutant, 30°C, substrate D-glucose (1,4-benzoquinone saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
442
D-glucose
mutant enzyme T166R, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C
615
D-glucose
wild-type, mutant, 50°C, substrate D-glucose (1,4-benzoquinone saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay
6.2
D-mannose
-
at pH 6.5 and 25°C
25.1
D-mannose
-
pH 7.0, 37°C
0.19
D-melibiose
mutant enzyme F454A/S455A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.29
D-melibiose
mutant enzyme F454P, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
1.3
D-melibiose
mutant enzyme F454A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
2.7
D-melibiose
mutant enzyme F454N, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
3.3
D-melibiose
mutant enzyme H450Q, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
4.4
D-melibiose
mutant enzyme Y456W, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
7.6
D-melibiose
wild type enzyme, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.27
D-xylose
-
pH 6.5, 30°C, recombinant enzyme
0.91
D-xylose
-
with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 37°C
1.39
D-xylose
-
pH 6.5, 30°C, recombinant enzyme
5.48
D-xylose
at 30°C, pH 6.5
25.4
D-xylose
-
at pH 6.5 and 25°C
44.9
D-xylose
substrate D-xylose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
55.8
D-xylose
-
pH 7.0, 37°C
1.7
ferricenium hexafluorophosphate
-
pH 8.0, 30°C, recombinant enzyme
158
ferricenium hexafluorophosphate
-
pH 8.0, 30°C, recombinant enzyme
228
ferricenium hexafluorophosphate
substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
549
ferricenium hexafluorophosphate
substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 8.0
1.44
ferricenium ion
E542K mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
1.81
ferricenium ion
L537G/E542R mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
2.08
ferricenium ion
E542R mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
2.11
ferricenium ion
L537G/E542K mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
2.47
ferricenium ion
L537W/E542R mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
2.68
ferricenium ion
L537W/E542K mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
5.34
ferricenium ion
wild-type, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
7.07
ferricenium ion
L537G mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
8.18
ferricenium ion
L537W mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
46.7
ferricenium ion
E542R mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
54.4
ferricenium ion
E542K mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
86.3
ferricenium ion
L537W/E542R mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
86.7
ferricenium ion
L537G/E542K mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
102
ferricenium ion
L537G/E542R mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
127
ferricenium ion
L537W/E542K mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
151
ferricenium ion
wild-type, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
282
ferricenium ion
L537G mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
334
ferricenium ion
L537W mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C
2.9
ferrocenium hexafluorophosphate
mutant enzyme F454A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
4.5
ferrocenium hexafluorophosphate
mutant enzyme F454P, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
5.4
ferrocenium hexafluorophosphate
mutant enzyme F454A/S455A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
6.6
ferrocenium hexafluorophosphate
wild type enzyme, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
7.3
ferrocenium hexafluorophosphate
mutant enzyme F454N, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
7.3
ferrocenium hexafluorophosphate
mutant enzyme Y456W, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
17
ferrocenium hexafluorophosphate
mutant enzyme H450Q, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
67
ferrocenium hexafluorophosphate
mutant enzyme F454P, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
74
ferrocenium hexafluorophosphate
mutant enzyme F454A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
110
ferrocenium hexafluorophosphate
mutant enzyme F454A/S455A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
210
ferrocenium hexafluorophosphate
wild type enzyme, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
400
ferrocenium hexafluorophosphate
mutant enzyme Y456W, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
420
ferrocenium hexafluorophosphate
mutant enzyme F454N, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
470
ferrocenium hexafluorophosphate
mutant enzyme H450Q, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
1.59
L-sorbose
-
pH 6.5, 30°C, recombinant enzyme
7.7
L-sorbose
at 30°C, pH 6.5
9.66
L-sorbose
-
pH 6.5, 30°C, recombinant enzyme
41.4
L-sorbose
-
at pH 6.5 and 25°C
58.8
L-sorbose
substrate L-sorbose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
74.6
L-sorbose
-
pH 7.0, 37°C
5.9
O2
-
pH 5.5, substrate D-glucose, measuring oxygen consumption (computer-interfaced Oxy-32 oxygen-monitoring system), 30°C
6.5
O2
-
pH 7.5, substrate D-glucose, measuring oxygen consumption (computer-interfaced Oxy-32 oxygen-monitoring system), 30°C
6.8
O2
-
pH 6.5, substrate D-glucose, measuring oxygen consumption (computer-interfaced Oxy-32 oxygen-monitoring system), 30°C
7.5
O2
-
pH 8.5, substrate D-glucose, measuring oxygen consumption (computer-interfaced Oxy-32 oxygen-monitoring system), 30°C
70
O2
-
soluble enzyme, 500 mM glucose used as electron acceptor, pH 5.0
109
O2
substrate O2 (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
6.61
tetrafluoro-1,4-benzoquinone
substrate tetrafluoro-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
129
tetrafluoro-1,4-benzoquinone
-
pH 6.5, 30°C, recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3.25 - 3000
1,4-benzoquinone
33.6 - 361
2,6-dichloroindophenol
0.1
2,6-dimethyl-1,4-benzoquinone
-
pH 6.5, 30°C, recombinant enzyme
34
2-chloro-1,4-benzoquinone
-
pH 6.5, 30°C, recombinant enzyme
112
2-methoxy-1,4-benzoquinone
-
pH 6.5, 30°C, recombinant enzyme
91.8
2-methyl-1,4-benzoquinone
-
pH 6.5, 30°C, recombinant enzyme
0.021
cellobiose
-
at pH 6.5 and 25°C
0.000009 - 1.7
D-galactose
0.71
D-glucono-1,5-lactone
-
at pH 6.5 and 25°C
0.017
D-mannose
-
at pH 6.5 and 25°C
0.0037 - 0.0166
D-melibiose
0.0000028 - 0.0021
D-ribose
1.5 - 235
ferricenium hexafluorophosphate
63 - 1640
ferrocenium hexafluorophosphate
213
ferrocenium ion
using D-glucose as cosubstrate, at 30°C, pH 6.5
0.000009 - 0.014
L-arabinose
0.67
maltose
-
at pH 6.5 and 25°C
0.0115
melibiose
at 30°C, pH 6.5
0.031
sucrose
-
at pH 6.5 and 25°C
13.7
tetrafluoro-1,4-benzoquinone
-
pH 6.5, 30°C, recombinant enzyme
3.25
1,4-benzoquinone
-
with D-glucose as cosubstrate, at pH 6.5 and 37°C
9.4
1,4-benzoquinone
-
pH 6.5, 30°C, recombinant enzyme
37
1,4-benzoquinone
mutant enzyme F454A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
130
1,4-benzoquinone
mutant enzyme F454A/S455A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
140
1,4-benzoquinone
wild type enzyme, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
230
1,4-benzoquinone
mutant enzyme H450Q, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
280
1,4-benzoquinone
mutant enzyme F454P, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
330
1,4-benzoquinone
mutant enzyme Y456W, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
420
1,4-benzoquinone
mutant enzyme F454P, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
520
1,4-benzoquinone
mutant enzyme F454A/S455A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
520
1,4-benzoquinone
mutant enzyme F454N, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
940
1,4-benzoquinone
mutant enzyme H450Q, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
1200
1,4-benzoquinone
wild type enzyme, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
1240
1,4-benzoquinone
-
pH 6.5, 30°C, recombinant enzyme
2100
1,4-benzoquinone
mutant enzyme F454A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
2600
1,4-benzoquinone
mutant enzyme F454N, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
2760
1,4-benzoquinone
using D-glucose as cosubstrate, at 30°C, pH 6.5
3000
1,4-benzoquinone
mutant enzyme Y456W, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
33.6
2,6-dichloroindophenol
-
pH 6.5, 30°C, recombinant enzyme
361
2,6-dichloroindophenol
using D-glucose as cosubstrate, at 30°C, pH 6.5
0.006
D-fructose
-
at pH 6.5 and 25°C
22
D-fructose
-
pH 6.5, 30°C, recombinant enzyme
0.000009
D-galactose
-
with O2 as electron acceptor, at pH 6.5 and 37°C
0.002
D-galactose
-
pH 6.5, 30°C, recombinant enzyme
0.005
D-galactose
-
mutant enzyme T169A, in 50 mM sodium phosphate (pH 7.0), at 25°C
0.0056
D-galactose
-
with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 37°C
0.011
D-galactose
mutant enzyme F454A/S455A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.024
D-galactose
mutant enzyme F454P, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.046
D-galactose
mutant enzyme F454N, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.053
D-galactose
mutant enzyme Y456W, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.059
D-galactose
mutant enzyme H450Q, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.062
D-galactose
mutant enzyme F454A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.08
D-galactose
-
wild type enzyme, in 50 mM sodium phosphate (pH 7.0), at 25°C
0.1
D-galactose
-
pH 6.5, 30°C, recombinant enzyme
0.11
D-galactose
mutant enzyme T169G, pH and temperature not specified in the publication
0.142
D-galactose
mutant enzyme V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C
0.142
D-galactose
mutant enzyme V546C, pH and temperature not specified in the publication
0.15
D-galactose
-
mutant enzyme T169S, in 50 mM sodium phosphate (pH 7.0), at 25°C
0.265
D-galactose
at 30°C, pH 6.5
0.27
D-galactose
wild type enzyme, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.286
D-galactose
His-tagged recombinant wild type enzyme, in 50 mM phosphate buffer (pH 6.5) at 60°C
0.286
D-galactose
wild type enzyme, pH and temperature not specified in the publication
0.3
D-galactose
-
mutant enzyme T169N, in 50 mM sodium phosphate (pH 7.0), at 25°C
0.364
D-galactose
mutant enzyme H450G/E542K/V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C
0.493
D-galactose
mutant enzyme H450G/V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C
0.493
D-galactose
mutant enzyme H450G/V546C, pH and temperature not specified in the publication
0.5
D-galactose
-
mutant enzyme T169G, in 50 mM sodium phosphate (pH 7.0), at 25°C
0.669
D-galactose
mutant enzyme E542K, in 50 mM phosphate buffer (pH 6.5) at 60°C
0.94
D-galactose
mutant enzyme T196G/V546C, pH and temperature not specified in the publication
1.43
D-galactose
mutant enzyme H450G, in 50 mM phosphate buffer (pH 6.5) at 60°C
1.43
D-galactose
mutant enzyme H450G, pH and temperature not specified in the publication
1.7
D-galactose
-
at pH 6.5 and 25°C
0.002
D-glucose
-
mutant enzyme T169A, in 50 mM sodium phosphate (pH 7.0), at 4°C
0.094
D-glucose
mutant enzyme F454A/S455A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.14
D-glucose
-
with O2 as electron acceptor, at pH 6.5 and 37°C
0.18
D-glucose
mutant enzyme N593C, with O2 as electron acceptor, at pH 6.5 and 30°C
0.229
D-glucose
-
with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 37°C
0.35
D-glucose
mutant enzyme H167A, pH and temperature not specified in the publication
0.38
D-glucose
mutant enzyme T169G, pH and temperature not specified in the publication
0.52
D-glucose
-
pH 6.5, 30°C, recombinant enzyme
0.54
D-glucose
mutant enzyme F454P, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.8
D-glucose
-
mutant enzyme T169G, in 50 mM sodium phosphate (pH 7.0), at 4°C
0.99
D-glucose
mutant enzyme T196G/V546C, pH and temperature not specified in the publication
1.2
D-glucose
-
mutant enzyme T169N, in 50 mM sodium phosphate (pH 7.0), at 4°C
1.47
D-glucose
-
mutant enzyme F454A, at pH 6.5 and 30°C
2.8
D-glucose
mutant enzyme L547R, with O2 as electron acceptor, at pH 6.5 and 30°C
4.6
D-glucose
mutant enzyme Q448H, with O2 as electron acceptor, at pH 6.5 and 30°C
4.7
D-glucose
mutant enzyme F454A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
5.08
D-glucose
wild-type, pH 6.5, 30°C
5.8
D-glucose
mutant T166A/E539K, pH 6.5, 30°C
7
D-glucose
mutant enzyme H450Q, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
8.1
D-glucose
-
mutant enzyme T169S, in 50 mM sodium phosphate (pH 7.0), at 4°C
8.2
D-glucose
mutant enzyme F454N, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
8.6
D-glucose
-
wild type enzyme, in 50 mM sodium phosphate (pH 7.0), at 4°C
8.83
D-glucose
mutant enzyme H450G/E542K/V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C
10.62
D-glucose
mutant K312E, pH 6.5, 30°C
10.86
D-glucose
mutant E359K, pH 6.5, 30°C
12.67
D-glucose
mutant K312E/E539K, pH 6.5, 30°C
12.7
D-glucose
mutant enzyme H450G, in 50 mM phosphate buffer (pH 6.5) at 60°C
12.7
D-glucose
mutant enzyme H450G, pH and temperature not specified in the publication
13.5
D-glucose
mutant enzyme H450G/V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C
13.5
D-glucose
mutant enzyme H450G/V546C, pH and temperature not specified in the publication
15
D-glucose
mutant enzyme Y456W, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
17.2
D-glucose
-
wild type enzyme F454Y, at pH 6.5 and 30°C
20.02
D-glucose
-
pH 6.5, 30°C, recombinant enzyme
22
D-glucose
mutant enzyme N593C, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C
22.1
D-glucose
at 30°C, pH 6.5
27
D-glucose
mutant enzyme N593C, with 1 ferrocenium ion as electron acceptor, at pH 6.5 and 30°C
29
D-glucose
mutant enzyme V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C
29
D-glucose
mutant enzyme V546C, pH and temperature not specified in the publication
32
D-glucose
mutant enzyme N593C, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C
34
D-glucose
mutant enzyme Q448H, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C
38
D-glucose
wild type enzyme, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C
43
D-glucose
wild type enzyme, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
45.6
D-glucose
-
at pH 6.5 and 25°C
48
D-glucose
mutant enzyme Q448H, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C
51.2
D-glucose
His-tagged recombinant wild type enzyme, in 50 mM phosphate buffer (pH 6.5) at 60°C
51.2
D-glucose
wild type enzyme, pH and temperature not specified in the publication
57.6
D-glucose
-
wild type enzyme, at pH 6.5 and 30°C
58
D-glucose
mutant enzyme L545C, with O2 as electron acceptor, at pH 6.5 and 30°C
68.9
D-glucose
mutant enzyme E542K, in 50 mM phosphate buffer (pH 6.5) at 60°C
70
D-glucose
mutant enzyme L545C, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C
79
D-glucose
mutant enzyme L547R, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C
120
D-glucose
mutant enzyme T166R, with O2 as electron acceptor, at pH 6.5 and 30°C
127
D-glucose
mutant enzyme T166R, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C
203
D-glucose
mutant enzyme Q448H, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C
281
D-glucose
mutant enzyme T166R, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C
308
D-glucose
wild type enzyme, with O2 as electron acceptor, at pH 6.5 and 30°C
584
D-glucose
mutant enzyme L547R, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C
592
D-glucose
wild type enzyme, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C
632
D-glucose
wild type enzyme, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C
1193
D-glucose
mutant enzyme L545C, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C
1213
D-glucose
mutant enzyme T166R, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C
1465
D-glucose
mutant enzyme L547R, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C
2608
D-glucose
mutant enzyme L545C, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C
0.0037
D-melibiose
mutant enzyme F454A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.005
D-melibiose
wild type enzyme, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.0058
D-melibiose
mutant enzyme F454P, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.008
D-melibiose
mutant enzyme F454A/S455A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.0084
D-melibiose
mutant enzyme H450Q, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.0113
D-melibiose
mutant enzyme F454N, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.0166
D-melibiose
mutant enzyme Y456W, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.0000028
D-ribose
-
with O2 as electron acceptor, at pH 6.5 and 37°C
0.0021
D-ribose
-
with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 37°C
0.000071
D-xylose
-
with O2 as electron acceptor, at pH 6.5 and 37°C
0.013
D-xylose
-
with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 37°C
0.015
D-xylose
-
pH 6.5, 30°C, recombinant enzyme
0.02
D-xylose
-
pH 6.5, 30°C, recombinant enzyme
0.867
D-xylose
at 30°C, pH 6.5
0.98
D-xylose
-
at pH 6.5 and 25°C
1.5
ferricenium hexafluorophosphate
-
pH 8.0, 30°C, recombinant enzyme
235
ferricenium hexafluorophosphate
-
pH 8.0, 30°C, recombinant enzyme
63
ferrocenium hexafluorophosphate
wild type enzyme, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
180
ferrocenium hexafluorophosphate
mutant enzyme F454A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
180
ferrocenium hexafluorophosphate
mutant enzyme Y456W, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
200
ferrocenium hexafluorophosphate
mutant enzyme F454P, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
290
ferrocenium hexafluorophosphate
mutant enzyme F454N, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
340
ferrocenium hexafluorophosphate
mutant enzyme H450Q, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
360
ferrocenium hexafluorophosphate
mutant enzyme F454A/S455A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
370
ferrocenium hexafluorophosphate
mutant enzyme F454A/S455A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
480
ferrocenium hexafluorophosphate
mutant enzyme F454P, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
500
ferrocenium hexafluorophosphate
mutant enzyme F454A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
510
ferrocenium hexafluorophosphate
wild type enzyme, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
1210
ferrocenium hexafluorophosphate
mutant enzyme F454N, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
1250
ferrocenium hexafluorophosphate
mutant enzyme H450Q, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
1640
ferrocenium hexafluorophosphate
mutant enzyme Y456W, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C
0.000009
L-arabinose
-
with O2 as electron acceptor, at pH 6.5 and 37°C
0.014
L-arabinose
-
with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 37°C
0.009
L-sorbose
-
pH 6.5, 30°C, recombinant enzyme
0.3
L-sorbose
-
pH 6.5, 30°C, recombinant enzyme
0.524
L-sorbose
at 30°C, pH 6.5
1.05
L-sorbose
-
at pH 6.5 and 25°C
0.07
O2
-
mutant enzyme T169A, using D-galactose as cosubstrate,in 50 mM sodium phosphate (pH 7.0), at 25°C
0.2
O2
-
mutant enzyme T169G, using D-glucose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 4°C
0.4
O2
-
mutant enzyme T169A, using D-glucose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 4°C
0.4
O2
-
mutant enzyme T169G, using D-galactose as cosubstrate,in 50 mM sodium phosphate (pH 7.0), at 25°C
0.99
O2
-
mutant enzyme T169S, using D-glucose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 4°C
3.4
O2
-
mutant enzyme T169N, using D-galactose as cosubstrate,in 50 mM sodium phosphate (pH 7.0), at 25°C
4.8
O2
-
mutant enzyme T169N, using D-glucose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 4°C
32
O2
-
mutant enzyme T169S, using D-galactose as cosubstrate,in 50 mM sodium phosphate (pH 7.0), at 25°C
44.2
O2
-
wild type enzyme, using D-galactose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 25°C
110
O2
-
wild type enzyme, using D-glucose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 4°C
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Izumi, Y.; Furuya, Y.; Yamada, H.
Purification and properties of pyranose oxidase from Basidiomycetous fungus No. 52
Agric. Biol. Chem.
54
1393-1399
1990
Basidiomycota
-
brenda
Izumi, Y.; Furuya, Y.; Yamada, H.
Isolation of a new pyranose oxidase producing Basidiomycete
Agric. Biol. Chem.
54
799-801
1990
Auricularia polytricha, Basidiomycota, Trametes versicolor, Gloeophyllum sepiarium, Irpex lacteus, Polyporus obtusus, Trametes cinnabarinus
-
brenda
Volc, J.; Eriksson, K.E.
Pyranose 2-oxidase from Phanerochaete chrysosporium
Methods Enzymol.
161
316-322
1988
Phanerodontia chrysosporium, Trametes versicolor, Polyporus obtusus
-
brenda
Eriksson, K.E.; Pettersson, B.; Volc, J.; Musilik, V.
Formation and partial characterization of glucose-2-oxidase, a H2O2 producing enzyme in Phanerochaete chrysosporium
Appl. Microbiol. Biotechnol.
23
257-262
1986
Phanerodontia chrysosporium
-
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Taguchi, T.; Ohwaki, K.; Okuda, J.
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Phanerodontia chrysosporium (Q6QWR1), Phanerodontia chrysosporium, Phanerodontia chrysosporium K-3 (Q6QWR1)
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Trametes ochracea (Q7ZA32)
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Trametes ochracea (Q7ZA32), Trametes ochracea
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Enzyme precipitate coating of pyranose oxidase on carbon nanotubes and their electrochemical applications
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Coriolus sp.
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