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Literature summary extracted from

  • Taneja, R.; Taneja, V.
    Xanthine oxidase in lentil (Lens esculenta) seedlings (1977), Biochim. Biophys. Acta, 485, 489-491.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.17.3.2 xanthine substrate inhibition at high concentration Lens culinaris

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.17.3.2 additional information
-
 additional information
-
 Lens culinaris

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.17.3.2 Iron iron-molybdenum protein Lens culinaris
1.17.3.2 Molybdenum an iron-molybdenum protein Lens culinaris

Organism

EC Number Organism UniProt Comment Textmining
1.17.3.2 Lens culinaris
-
 lentil
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.17.3.2 additional information
-
 Lens culinaris
1.17.3.2 proteolytic modification
-
 Lens culinaris

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.17.3.2 seedling
-
 Lens culinaris
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.3.2 hypoxanthine + 2 H2O + 2 O2
-
 Lens culinaris urate + 2 H2O2
-
 ?
1.17.3.2 xanthine + H2O + O2 electron acceptor O2 Lens culinaris uric acid + H2O2
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.17.3.2 8
-
-
 Lens culinaris

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.17.3.2 6 9 pH 6.0: about 25% of activity maximum, pH 9.0: about 20% of activity maximum Lens culinaris

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.3.2 FAD flavoprotein Lens culinaris