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Literature summary for 1.17.3.2 extracted from

  • McManaman, J.L.; Neville, M.C.; Wright, R.M.
    Mouse mammary gland xanthine oxidoreductase: Purification, characterization, and regulation (1999), Arch. Biochem. Biophys., 371, 308-316.
    View publication on PubMed
Search for more literature for 1.17.3.2

Localization

Localization Comment Organism GeneOntology No. Textmining
lipid droplet milk lipid globule membrane possesses enzyme activity capable of catalyzing the conversion of xanthine dehydrogenase to xanthine oxidase, kinetic of this process is consistent with the rapid appearence of xanthine oxidase in milk Mus musculus 5811
-

Metals/Ions

Metals/Ions Comment Organism Structure
Iron iron-molybdenum protein Mus musculus
Molybdenum an iron-molybdenum protein Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information
-
 Mus musculus
proteolytic modification
-
 Mus musculus

Purification (Commentary)

Purification (Comment) Organism
60% ammonium sulfate, benzamidine-Sepharose Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
mammary gland
-
 Mus musculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.2
-
-
 Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hypoxanthine + 2 H2O + 2 O2
-
 Mus musculus urate + 2 H2O2
-
 ?
xanthine + H2O + O2 electron acceptor O2 Mus musculus uric acid + H2O2
-
 ?

Cofactor

Cofactor Comment Organism Structure
FAD flavoprotein Mus musculus