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
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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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Metals Ions
Metals Ions on EC 1.10.3.3 - L-ascorbate oxidase
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copper
Cu2+
additional information
copper
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enzyme contains type I, type II and type III copper atoms in the ratio 1/2/2, 4 copper atoms/enzyme
copper
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the oxidative activity of ascorbate oxidase is dominated by the highly selective substrate-binding affinity based on electrostatic interaction beyond the one-electron redox potential difference between type 1 copper site of ascorbate oxidase and substrate
copper
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4 copper atoms per subunit, mononuclear blue copper in domain 3 and trinuclear copper between domain 1 and 3
copper
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principal active site comprised of one type I, one type II and a pair of type III coppers
copper
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enzyme contains a set of 1 type I, 1 type II and a pair of type III copper ions at its active site
copper
Cucurbita pepo medullosa
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each subunit has 4 copper atoms bound as mononuclear and trinuclear species, mononuclear copper representing the type I copper is located in the 3 domain
copper
Cucurbita pepo medullosa
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evidence that the coordination environment and electronic structure of the type 1 copper is similar to those of plastocyanin and azurin
copper
Cucurbita pepo medullosa
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native enzyme contains two type 1, two type 2 and four type 3 copper ions
copper
Cucurbita pepo medullosa
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measurement of intramolecular electron transfer between type I and type III copper centers in the multi-copper enzyme
copper
Cucurbita pepo medullosa
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4 copper atoms per subunit, mononuclear blue copper in domain 3 and trinuclear copper between domain 1 and 3
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a multicopper oxidase, contains type 1 Cu2+, binding residues are His445, Cys507, His512, and Met517
Cu2+
essential for activity, a tri-nuclear copper center structure, a partial loss of tertiary structure has strong effects on copper
Cu2+
9 copper atoms per enzyme molecule. Each subunit has four copper atoms bound as mononuclear and trinuclear species. The mononuclear copper has two histidine, a cysteine and a methionine ligand and represents the type-l copper. It is located in domain 3. Binding structure analysis, copper site structures, detailed overview
additional information
Cucurbita pepo medullosa
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selective removal of copper with chelating agents, e.g. EDTA or N,N-diethyldithiocarbamate produces an inactive enzyme, CN- treatment gives fully copper-depleted apoform, indication that copper affects the enzyme stability but not the enzyme conformation