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
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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
1.1.3.10 pyranose oxidaseAdvanced search results
results (
results (Temperature Stability
Temperature Stability on EC 1.1.3.10 - pyranose oxidase
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TEMPERATURE STABILITY 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4
under dry and wet storage conditions stable at 4°C, under dry storage conditions retainment of 100% of original activity after 2 days and of about 90% after one week, storage in working buffer solutions decreases activity by about 10% after one day and by more than 50% after one week
40
pH 7.0, 30 min, wild-type enzyme, mutant enzyme K312E with a C-terminal His6-tag and mutant enzyme E540K are stable
40 - 43
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the enzyme shows a melting temperature of 43°C and a half-life at 40°C of 25 min
40 - 55
the melting temperature is 54.9°C, half-life time of activity is 0.12 min at 50°C and pH 6.5, half-life time of activity is 60 h at 40°C and pH 6.5/8.0 and 43 min at 40°C and pH 4.0
50
55
60
60 - 70
60 - 80
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the enzyme remains stable up to 60°C. At 70°C, more than half of its initial activity is retained after 30 min of incubation in phosphate buffer, pH 6.5. At 80°C, it is totally inactivated within 30 min
69
melting temperature of mutant L547W, increased half-life compared to wild-type
70
71.1
melting temperature of mutant L547G, increased half-life compared to wild-type
74.2
melting temperature of mutant E542K, increased half-life compared to wild-type
74.3
melting temperature of mutant E542R, increased half-life compared to wild-type
additional information
50
pH 7.0, 30 min, wild-type enzyme loses about 40% of its activity, mutant enzyme K312E with a C-terminal His6-tag and mutant enzyme E540K are stable
55
pH 7.0, 30 min, wild-type enzyme loses 95% of its activity, mutant enzyme K312E with a C-treminal His6-tag and mutant enzyme E540K lose about 10% of its activity
60
pH 7.0, 30 min, wild-type enzyme completely loses its activity, mutant enzyme K312E with a C-terminal His6-tag loses about 40% of its activity and mutant enzyme E540K loses about 10% of its activity
60
T169G/E542K/V546C mutant, half life is increased 76fold compared to wild-type
60 - 70
the half life of the wild type enzyme at 60°C and 70°C is 12 min and 0.07 min, respectively. The melting temperature of the wild type enzyme is at 63.5°C
60 - 70
the wild type enzyme shows a half life of 10 min at 60°C and of less than 1 min at 70°C
70
T169G/E542K/V546C mutant, half life is increased 350fold compared to wild-type
additional information
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thermal inactivation of free and immobilized enzyme activity investigated at 40, 50, 60 and 70°C in 50 mM phosphate buffer at pH 6.0 over 7 days, stability of immobilized enzyme shown to be significantly higher at 60°C, no stabilizing effect observed at 70°C
additional information
mutant L537G/E542K, L537G/E542R, L537W/E542K and L537W/E542R show more complex melting curves, increased half-life compared to wild-type
additional information
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mutant L537G/E542K, L537G/E542R, L537W/E542K and L537W/E542R show more complex melting curves, increased half-life compared to wild-type
