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Literature summary for 1.17.1.4 extracted from

  • Corpas, F.J.; Palma, J.M.; Sandalio, L.M.; Valderrama, R.; Barroso, J.B.; Del Rio, L.A.
    Peroxisomal xanthine oxidoreductase: Characterization of the enzyme from pea (Pisum sativum L.) leaves (2008), J. Plant Physiol., 165, 1319-1330.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
peroxisome in leaf peroxisomes, the superoxide-generating form, xanthine oxidase XOD is predominant over the xanthine dehydrogenase form XDH, with a XDH/XOD ratio of 0.5. Enzyme is localized to the matrix of peroxisome Pisum sativum 5777
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Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
59000
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x * 59000, SDS-PAGE Pisum sativum
290000
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PAGE Pisum sativum

Organism

Organism UniProt Comment Textmining
Pisum sativum B3FYT9
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Source Tissue

Source Tissue Comment Organism Textmining
leaf in leaf peroxisomes, the superoxide-generating form, xanthine oxidase XOD is predominant over the xanthine dehydrogenase form XDH, with a XDH/XOD ratio of 0.5. In crude extracts of pea leaves, the XDH form is more abundant, with a XDH/XOD ratio of 1.6 Pisum sativum
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Subunits

Subunits Comment Organism
oligomer x * 59000, SDS-PAGE Pisum sativum