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Literature summary extracted from

  • Houston, M.; Esteveze, A.; Chumley, P.; Aslan, M.; Marklund, S.; Parks, D.A.; Freeman, B.A.
    Binding of xanthine oxidase to vascular endothelium (1999), J. Biol. Chem., 274, 4985-4994.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.17.3.2 allopurinol
-
 Bos taurus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.17.3.2 0.0015
-
 pterin cell-associated enzyme, determined in intact cell monolayers Bos taurus
1.17.3.2 0.0016
-
 pterin
-
 Bos taurus
1.17.3.2 0.0034
-
 xanthine cell-associated enzyme, determined in intact cell monolayers Bos taurus
1.17.3.2 0.0036
-
 xanthine
-
 Bos taurus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.17.3.2 additional information enzyme binds specifically and with high affinity to bovine aortic endothelial cells, increasing cell xanthine oxidase activity up to 10fold, circulating xanthine oxidase may therefore bind to vascular cells, impairing cell function via oxidative mechanisms Bos taurus
-
-

Metals/Ions

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

Organism

EC Number Organism UniProt Comment Textmining
1.17.3.2 Bos taurus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.17.3.2 additional information
-
 Bos taurus
1.17.3.2 proteolytic modification
-
 Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.3.2 hypoxanthine + 2 H2O + 2 O2
-
 Bos taurus urate + 2 H2O2
-
 ?
1.17.3.2 pterin + H2O + O2
-
 Bos taurus isoxanthopterin + H2O2
-
 ?
1.17.3.2 xanthine + H2O + O2 electron acceptor O2 Bos taurus uric acid + H2O2
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.3.2 FAD flavoprotein Bos taurus