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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Subunits
Subunits on EC 1.10.3.3 - L-ascorbate oxidase
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dimer
dodecamer
Cucurbita pepo condensa
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12 * 35000, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE
monomer
octamer
Cucurbita pepo condensa
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8 * 35000, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE
polymer
Cucurbita pepo condensa
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x * 35000, between 670000 Da and 2000000 Da, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE
tetramer
additional information
dimer
unfolding studies, pressure-induced and denaturing agents-induced dissociation and unfolding, and the role of dimerization in the folding strategy of a large protein, crystal structure analysis, physico-chemical properties of a molten dimer enzyme, three distinct domains per subunit, sharing a common beta-barrel topology, overview
dimer
Cucurbita pepo medullosa
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2 * 70000, 70000 Da subunit consists of 2 polypeptide chains of 30000 and 40000 Da respectively
dimer
Cucurbita pepo medullosa
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2 * 65000, treatment with 2-mercaptoethanol results in 2 new bands, an A chain of 38000 Da and an B chain of 28000 Da, SDS-PAGE
monomer
Acremonium HI-25
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1 * 80000
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monomer
Cucurbita pepo condensa
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1 * 35000, enzyme also exists as tetramer, octamer, dodecamer and polymer, SDS-PAGE
tetramer
4 * 70000, tetramer with D2 symmetry, crystal structure and SDS-PAGE, present as dimer in solution. Each subunit is built up by three domains arranged sequentially on the polypeptide chain and tightly associated in space. The folding of all three domains is of a similar beta-barrel type, analysis of intra- and intertetramer hydrogen bond and van der Waals interactions, domains structures, detailed overview
tetramer
Cucurbita pepo condensa
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4 * 35000, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE
tetramer
Cucurbita pepo medullosa
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4 * 35000, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE
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structure analysis: the monomers keep their secondary structure, whereas subtle conformational changes in the tertiary structure become apparent, salt bridges and electrostatic interactions occurring at the dimeric interface play a crucial role in the stabilization of the monomer's tertiary structure., folding/unfolding pathway, overview. Each subunit is formed by three distinct domains and contains four copper ions, three of which are located at the interface between domains, forming a so-called trinuclear centre