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Literature summary extracted from

  • Coughlan, M.P.; Johnson, D.B.
    The inactivation of xanthine-oxidizing enzymes, native and deflavo forms, in the presence of oxygen (1979), Biochem. Soc. Trans., 7, 18-21.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.17.1.4 xanthine + O2 + H2O Meleagris gallopavo
-
 urate + O2- + 2 H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.17.1.4 Meleagris gallopavo
-
 turkey
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.17.1.4 to homogeneity, immobilized preparation Meleagris gallopavo

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.17.1.4 liver
-
 Meleagris gallopavo
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.1.4 xanthine + methylene blue + H2O
-
 Meleagris gallopavo urate + reduced methylene blue
-
 ?
1.17.1.4 xanthine + O2 + H2O
-
 Meleagris gallopavo urate + O2- + 2 H+
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.17.1.4 30
-
 enhanced stability of immobilized enzyme preparation if N2 and hemoglobin is included, reaction of oxygen products causes instability of the working enzyme, half-life: 250-560 min, compared to immobilized enzyme without additions of about 145 min Meleagris gallopavo

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.1.4 FAD
-
 Meleagris gallopavo