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Literature summary for 1.17.3.2 extracted from

  • Li, H.; Samouilov, A.; Liu, X.; Zweier, J.L.
    characterization of the magnitude and kinetics of xanthine oxidase-catalyzed nitrite reduction (2001), J. Biol. Chem., 276, 24482-24489.
    View publication on PubMed
Search for more literature for 1.17.3.2

Inhibitors

Inhibitors Comment Organism Structure
allopurinol inhibits substrate binding at the molybdenum site Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00146
-
 xanthine
-
 Bos taurus
0.035
-
 2,3-Dihydroxybenzaldehyde
-
 Bos taurus
0.878
-
 NADH
-
 Bos taurus
2.25
-
 NO2-
-
 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
-
 Bos taurus
proteolytic modification
-
 Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,3-dihydroxybenzaldehyde + H2O + O2
-
 Bos taurus 2,3-dihydroxybenzoate + H2O2
-
 ?
hypoxanthine + 2 H2O + 2 O2
-
 Bos taurus urate + 2 H2O2
-
 ?
xanthine + H2O + O2 electron acceptor O2 Bos taurus uric acid + H2O2
-
 ?
xanthine + NO2- oxidation of the enzyme by NO2- or reduction by xanthine take place at the molybdenum site Bos taurus uric acid + NO
-
 ?

Cofactor

Cofactor Comment Organism Structure
FAD flavoprotein Bos taurus