1.10.3.3: L-ascorbate oxidase
This is an abbreviated version!
For detailed information about L-ascorbate oxidase, go to the full flat file.
Word Map on EC 1.10.3.3
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1.10.3.3
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copper
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dehydroascorbic
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electrode
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laccase
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oxidases
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ceruloplasmin
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zucchini
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cucurbita
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cucumber
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amperometric
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trinuclear
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apoplastic
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monodehydroascorbate
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squash
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multi-copper
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ascorbate-dependent
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copper-containing
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plastocyanin
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pumpkin
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azurins
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ascorbyl
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ascorbate-glutathione
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myrothecium
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vernicifera
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ferroxidase
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agriculture
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medicine
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analysis
- 1.10.3.3
- copper
-
dehydroascorbic
-
electrode
- laccase
- oxidases
- ceruloplasmin
- zucchini
- cucurbita
- cucumber
-
amperometric
-
trinuclear
- apoplastic
- monodehydroascorbate
- squash
-
multi-copper
-
ascorbate-dependent
-
copper-containing
- plastocyanin
- pumpkin
- azurins
-
ascorbyl
-
ascorbate-glutathione
- myrothecium
- vernicifera
- ferroxidase
- agriculture
- medicine
- analysis
Reaction
4 L-ascorbate + = 4 monodehydroascorbate + 2 H2O
Synonyms
AA oxidase, AA-ox, AAO, AAO1, AAO2, AAO3, Aao4, Af_AO1, AO1, AO4, AOase, ASC oxidase, ascorbase, ascorbate dehydrogenase, ascorbate oxidase, ascorbic acid oxidase, ascorbic oxidase, ASOM, L-ascorbate:O2 oxidoreductase, L-ascorbic acid oxidase, oxidase, ascorbate
ECTree
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General Stability
General Stability on EC 1.10.3.3 - L-ascorbate oxidase
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20-25% retention of activity after immobilization, at 12°C, stable for at least 30 days
Cucurbita pepo medullosa
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a long acting enzyme derivative is synthesized by covalently linking poly(ethylene glycol) to the enzyme
Cucurbita sp.
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ascorbate oxidase is alternately deposited with Au nanoparticles and forms a layer-by-layer membrane on a Pt electrode. The enzyme activities remain even after the deposition. The oxidation current of ascorbic acid (0.1 mM) decreases to 36% for the (ascorbate oxidase/Au)1 modified electrode, and to 19% for the (ascorbate oxidase/Au)10 modified electrode
Cucumis sp.
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gelatin, catalase, peroxidase and methemoglobin protect against inactivation
Cucurbita pepo condensa
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no change in total activity in the presence of 5 M urea, conversion of tetrameric form into monomer with 75% activity in 8 M urea
Cucurbita pepo medullosa
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partially unfolding of the enzyme by 1.4 M guanidinium hydrochloride or 2.8 M urea