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Literature summary 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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.17.3.2 0.0065
-
xanthine
-
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 bovine milk enzyme: conversion from oxidase into dehydrogenase by treatment with dithioerythritol or dihydrolipoic acid Bos taurus
1.17.3.2 additional information oxidase is converted into an irreversible oxidase form by pretreatment with chymotrypsin, papain or subtilisin, but only partially with trypsin Bos taurus
1.17.3.2 proteolytic modification
-
Bos taurus

Purification (Commentary)

EC Number Purification (Comment) Organism
1.17.3.2
-
Bos taurus

Source Tissue

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.17.3.2 1.67
-
-
Bos taurus

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
-
?

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.3.2 FAD flavoprotein Bos taurus