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Literature summary extracted from

  • Radi, R.; Rubbo, H.; Bush, K.; Freeman, B.A.
    Xanthine oxidase binding to glycosaminoglycans: kinetics and superoxide dismutase interactions of immobilized xanthine oxidase-heparin complexes (1997), Arch. Biochem. Biophys., 339, 125-135.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.17.3.2 heparin-Sepharose 6B-bound enzyme, half-life: 120 h and 67 h at 4°C and 20°C respectively, free enzyme, 61 h and 45 h at 4°C and 67°C respectively Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.17.3.2 0.003
-
 xanthine
-
 Homo sapiens
1.17.3.2 0.015
-
 xanthine heparin-Sepharose 6B-bound enzyme Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.17.3.2 additional information enzyme binds to endothelial cells in a partially heparin-reversible manner Homo sapiens
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.17.3.2 Iron iron-molybdenum protein Homo sapiens
1.17.3.2 Molybdenum an iron-molybdenum protein Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.17.3.2 Homo sapiens
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.17.3.2 additional information
-
 Homo sapiens
1.17.3.2 proteolytic modification
-
 Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.3.2 hypoxanthine + 2 H2O + 2 O2
-
 Homo sapiens urate + 2 H2O2
-
 ?
1.17.3.2 xanthine + H2O + O2 electron acceptor O2 Homo sapiens uric acid + H2O2 enzyme contributes to the oxidant stress component of ischemia-reperfusion injury to intestine and liver, O2- production decreases with increasing substrate concentrations ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.3.2 FAD flavoprotein Homo sapiens