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Literature summary extracted from

  • Berglund, L.; Rasmussen, J.T.; Andersen, M.D.; Rasmussen, M.S.; Petersen, T.E.
    Purification of the bovine xanthine oxidoreductase from milk fat globule membranes and cloning of complementary deoxyribonucleic acid (1996), J. Dairy Sci., 79, 198-204.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.17.3.2 expression in Escherichia coli Bos taurus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining

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 xanthine + H2O + O2 electron acceptor O2 Bos taurus uric acid + H2O2
-
?

Subunits

EC Number Subunits Comment Organism
1.17.3.2 dimer
-
Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.3.2 FAD flavoprotein Bos taurus