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Literature summary extracted from

  • Tramper, J.
    Preparation of immobilized milk xanthine oxidase and application in organic synthesis (1987), Methods Enzymol., 136, 254-262.
No PubMed abstract available

General Stability

EC Number General Stability Organism
1.17.3.2 low operational stability by immobilization 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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.17.3.2 milk
-
 Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.3.2 7-alkylpteridin-4-one + H2O + O2
-
 Bos taurus 7-alkyllumazine + H2O2
-
 ?
1.17.3.2 7-phenylpteridin-4-one + H2O + O2
-
 Bos taurus 7-phenyllumazine + H2O2
-
 ?
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
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.3.2 FAD flavoprotein Bos taurus