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Literature summary for 1.10.3.3 extracted from

  • Di Venere, A.; Nicolai, E.; Rosato, N.; Rossi, A.; Finazzi Agro, A.; Mei, G.
    Characterization of monomeric substrates of ascorbate oxidase (2011), FEBS J., 278, 1585-1593.
    View publication on PubMed
Search for more literature for 1.10.3.3

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4 L-ascorbate + O2 Cucurbita pepo
-
 4 monodehydroascorbate + 2 H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Cucurbita pepo
-
 subsp. pepo convar. giromontiina
-

Source Tissue

Source Tissue Comment Organism Textmining
fruit
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 Cucurbita pepo
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4 L-ascorbate + O2
-
 Cucurbita pepo 4 monodehydroascorbate + 2 H2O
-
 ?

Subunits

Subunits Comment Organism
homodimer ascorbate oxidase is a large, multidomain, dimeric protein Cucurbita pepo
More 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 Cucurbita pepo

Synonyms

Synonyms Comment Organism
AAO
-
 Cucurbita pepo
ascorbate oxidase
-
 Cucurbita pepo

General Information

General Information Comment Organism
additional information partially folded monomeric species might populate the energy landscape of the enzyme. The overall AAO stability is crucially controlled by a few quaternary interactions at the subunits' interface Cucurbita pepo