1.1.3.10: pyranose oxidase
This is an abbreviated version!
For detailed information about pyranose oxidase, go to the full flat file.
Word Map on EC 1.1.3.10
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1.1.3.10
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trametes
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multicolor
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1,4-benzoquinone
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chrysosporium
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phanerochaete
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white-rot
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nivale
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microdochium
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l-sorbose
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aldopyranoses
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synthesis
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1,5-anhydro-d-glucitol
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flavinylated
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ligninolytic
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ochracea
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glucose-methanol-choline
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1,5-anhydroglucitol
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peniophora
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c4a-hydroperoxyflavin
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biotechnology
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food industry
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energy production
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biofuel production
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analysis
- 1.1.3.10
- trametes
- multicolor
- 1,4-benzoquinone
- chrysosporium
- phanerochaete
-
white-rot
- nivale
-
microdochium
- l-sorbose
- aldopyranoses
- synthesis
- 1,5-anhydro-d-glucitol
-
flavinylated
-
ligninolytic
- ochracea
-
glucose-methanol-choline
- 1,5-anhydroglucitol
- peniophora
-
c4a-hydroperoxyflavin
- biotechnology
- food industry
- energy production
- biofuel production
- analysis
Reaction
Synonyms
C-2 specific pyranose-2-oxidase, carbohydrate oxidase, glucose 2-oxidase, glucose-2-oxidase, P2O, P2Ox, POX, PROD, PyOx, pyranose 2-Oxidase, pyranose oxidase, pyranose-2-oxidase, pyranose/oxygen 2-oxidoreductase, pyranose: oxygen 2-oxidoreductase, pyranose:oxygen 2-oxidoreductase, pyranose:oxygen-2-oxidoreductase, TmP2Ox
ECTree
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Specific Activity
Specific Activity on EC 1.1.3.10 - pyranose oxidase
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0.27
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V546C/T169G/L537W mutant, substrate D-glucose (constant O2 concentration), activity determined spectrophotometrically at 420nm 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
0.34
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V546C/T169G/L537W mutant, substrate D-galactose (constant O2 concentration), activity determined spectrophotometrically at 420nm 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
0.38
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V546C/T169G mutant, substrate D-galactose (constant O2 concentration), activity determined spectrophotometrically at 420nm 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
0.43
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V546C/T169G mutant, substrate D-glucose (constant O2 concentration), activity determined spectrophotometrically at 420nm 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
103
-
V546C/T169G/L537W mutant, substrate 1,4-benzoquinone (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420nm 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
189
-
V546C/T169G mutant, substrate 1,4-benzoquinone (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420nm 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
221
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V546C/T169G mutant, substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420nm 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
24.1
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V546C/T169G/L537W mutant, substrate 1,4-benzoquinone (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420nm 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
246
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V546C/E542K mutant, substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420nm 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
261
-
V546C/T169G mutant, substrate ferricenium hexafluorophosphate (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420nm 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
42.1
-
V546C/T169G mutant, substrate 1,4-benzoquinone (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420nm 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
5.54
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V546C/E542K mutant, substrate ferricenium hexafluorophosphate (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420nm 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
51.9
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V546C/T169G/L537W mutant, substrate ferricenium hexafluorophosphate (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420nm 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
56.4
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V546C/T169G/L537W mutant, substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420nm 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
6.13
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V546C/E542K mutant, substrate D-galactose (constant O2 concentration), activity determined spectrophotometrically at 420nm 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
664
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V546C/E542K mutant, substrate 1,4-benzoquinone (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420nm 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
82.2
additional information
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V546C/E542K mutant, substrate 1,4-benzoquinone (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420nm 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
82.2
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V546C/E542K mutant, substrate D-glucose (constant O2 concentration), activity determined spectrophotometrically at 420nm 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
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heterologously expressed enzyme yields 15 U enzyme activity per ml culture, 15 U substrate glucose, 2,2-azinobis(3-ethylbenzthiazolinesulfonic acid) assay, pH 6.5, 25°C
additional information
comparative characterization of pyranose 2-oxidase from Trametes ochracea and Trametes pubescens, enzyme activity determined by the formation of H2O2 in a peroxidase-coupled assay, inclusion body formation and specific activity of pyranose 2-oxidases in Escherichia coli harbouring chimeric plasmid constructs, site-directed recombination
additional information
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comparative characterization of pyranose 2-oxidase from Trametes ochracea and Trametes pubescens, enzyme activity determined by the formation of H2O2 in a peroxidase-coupled assay, inclusion body formation and specific activity of pyranose 2-oxidases in Escherichia coli harbouring chimeric plasmid constructs, site-directed recombination
additional information
pyranose 2-oxidase-based biosensor system, electrical wiring of different types of pyranose oxidase with an osmium redox polymer on graphite electrodes, optimization studies using glucose as substrate, biosensors with best characteristics in terms of linear range, detection limit and sensitivity used for analyzing selectivity for different sugar substrates
additional information
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report on immobilization of pyranose 2-oxidase on agarose or acrylic resins using different coupling methods, enzyme activity determined by a peroxidase-coupled assay or by measuring initial rate of oxygen consumption, molecular properties of immobilized enzymes and binding capacities summarized
additional information
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complete oxidation of D-glucose using pyranose oxidase as the synthesizing biocatalyst and laccase for redox mediator regeneration is described quantitatively to increase both stability and productivity
additional information
kinetic parameters measured at batch conversion experiments of wild-type pyranose oxidase and mutant T169G/E542K/V546C
additional information
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kinetic parameters measured at batch conversion experiments of wild-type pyranose oxidase and mutant T169G/E542K/V546C
additional information
comparative characterization of pyranose 2-oxidase from Trametes ochracea and Trametes pubescens, 93.4% identity of amino acid sequences observed, specific activity of pyranose 2-oxidase from Trametes pubescens eight times higher than that from Trametes ochracea, pyranose 2-oxidase ctivity determined in a peroxidase-coupled assay, site-directed recombination performed, pyranose 2-oxidases of Trametes pubescens shown to exhibit a unique trait regarding protein folding at growth temperature of 28°C
additional information
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comparative characterization of pyranose 2-oxidase from Trametes ochracea and Trametes pubescens, 93.4% identity of amino acid sequences observed, specific activity of pyranose 2-oxidase from Trametes pubescens eight times higher than that from Trametes ochracea, pyranose 2-oxidase ctivity determined in a peroxidase-coupled assay, site-directed recombination performed, pyranose 2-oxidases of Trametes pubescens shown to exhibit a unique trait regarding protein folding at growth temperature of 28°C