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Literature summary for 1.17.3.2 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

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

KM Value [mM]

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Lens culinaris
-
lentil
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information
-
Lens culinaris
proteolytic modification
-
Lens culinaris

Source Tissue

Source Tissue Comment Organism Textmining
seedling
-
Lens culinaris
-

Substrates and Products (Substrate)

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Lens culinaris

pH Range

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

Cofactor

Cofactor Comment Organism Structure
FAD flavoprotein Lens culinaris