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Literature summary for 1.17.3.2 extracted from

  • Batelli, M.G.; Lorenzoni, E.; Stirpe, F.
    Milk xanthine oxidase type D (dehydrogenase) and type O (oxidase). Purification, interconversion and some properties (1973), Biochem. J., 131, 191-198.
    View publication on PubMedView publication on EuropePMC
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0065
-
 xanthine
-
 Bos taurus

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information bovine milk enzyme: conversion from oxidase into dehydrogenase by treatment with dithioerythritol or dihydrolipoic acid Bos taurus
additional information oxidase is converted into an irreversible oxidase form by pretreatment with chymotrypsin, papain or subtilisin, but only partially with trypsin Bos taurus
proteolytic modification
-
 Bos taurus

Purification (Commentary)

Purification (Comment) Organism
-
 Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
milk
-
 Bos taurus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.67
-
-
 Bos taurus

Substrates and Products (Substrate)

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

Cofactor

Cofactor Comment Organism Structure
FAD flavoprotein Bos taurus