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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pH Range
pH Range on EC 1.1.3.10 - pyranose oxidase
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5 - 9
5.5 - 11
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pH 5.5: about 40% of maximal activity, pH 11: about 40% of maximal activity
5.5 - 8.5
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substrate D-glucose, measuring oxygen consumption (computer-interfaced Oxy-32 oxygen-monitoring system), 30°C, varying concentrations of both D-glucose and oxygen. Ping-pong kinetic mechanism at pH values below 7.0 and an ordered mechanism at pH above 7.0
6.5 - 8
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at pH 8.0, the enzyme still retains 45% of its maximal activity observed at pH 6.5
8 - 11
optimal buffer combination for the pyranose 2-oxidase systems determined
additional information
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flavin oxidation occurs via different pathways depending on the pH of the environment. At pH values lower than 8.0, the reduced enzyme reacts with O2 to form a C4a-hydroperoxyflavin intermediate, leading to elimination of H2O2. At pH 8.0 and higher, the majority of the reduced enzyme reacts with O2 via a pathway that does not allow detection of the C4a-hydroperoxyflavin, and flavin oxidation occurs with decreased rate constants upon the rise in pH. The switching between the two modes of enzyme oxidation is controlled by protonation of a group which has a pKa of 7.6, stopped-flow spectrophotometry, overview. The protonation of the group which controls the mode of flavin oxidation cannot be rapidly equilibrated with outside solvent. Using a double-mixing stopped-flow experiment, a rate constant for proton dissociation from the reaction site is determined to be 21.0 s-1
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at pH 5.0 in citrate buffer and pH 9.0 in glycine-NaOH buffer, the enzyme displays about 60% of its maximum activity. The activity begins to decline dramatically below pH 5.0 and above pH 9.0