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Literature summary for 1.10.3.3 extracted from

  • Messerschmidt, A.; Ladenstein, R.; Huber, R.; Bolognesi, M.; Avigliano, L.; Petruzzelli, R.; Rossi, A.; Finazzi-Agro, A.
    Refined crystal structure of ascorbate oxidase at 1.9 A resolution (1992), J. Mol. Biol., 224, 179-205.
    View publication on PubMed
Search for more literature for 1.10.3.3

Crystallization (Commentary)

Crystallization (Comment) Organism
fully oxidized form of ascorbate oxidase, X-ray diffraction structure determination and analysis at 1.90 A resolution Cucurbita pepo

Metals/Ions

Metals/Ions Comment Organism Structure
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 Cucurbita pepo

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
70000
-
 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 Cucurbita pepo

Organism

Organism UniProt Comment Textmining
Cucurbita pepo P37064 medullosa
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Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein Asn92 is the attachment site for one of the two N-linked sugar moieties, which has defined electron density for the N-linked N-acetylglucosamine ring. Three putative attachment sites for N-glycosidiclinked carbohydrate moieties are present in the amino acid sequence of AOase from Zucchini, i.e. Asn92-Phe93-Thr94, Asn325-Phe326-Thr327, and Asn440-Leu441 -Ser442, but only Asn92 shows density for an N-acetyl-glucosamine group Cucurbita pepo

Subunits

Subunits Comment Organism
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 Cucurbita pepo

Synonyms

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

General Information

General Information Comment Organism
evolution AOase occurs only in higher plants Cucurbita pepo
additional information proposed catalytic model, structure-function relationship, overview. Intramolecular electron transfer from the type-l copper centre to the trinuclear copper centre Cucurbita pepo
physiological function ascorbate oxidase is a blue multicopper oxidase that catalyses the four-electron reduction of dioxygen to water with concomitant one-electron oxidation of the reducing organic substrate Cucurbita pepo