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Literature summary extracted from

  • Metz, S.; Thiel, W.
    QM/MM studies of xanthine oxidase: variations of cofactor, substrate, and active-site Glu802 (2010), J. Phys. Chem. B, 114, 1506-1517.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.17.3.2 E1261X mutation of Glu1261 leads to a complete loss of activity Bos taurus
1.17.3.2 E802Q site-directed mutagenesis, altered kinetics of the mutant enzyme compared to the wild-type enzyme Bos taurus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.17.3.2 0.0552
-
 xanthine pH not specified in the publication, temperature not specified in the publication, mutant E802Q Bos taurus
1.17.3.2 0.0644
-
 xanthine pH not specified in the publication, temperature not specified in the publication, wild-type enzyme Bos taurus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.17.3.2 Fe2+ Fe2S2 cluster Bos taurus
1.17.3.2 Molybdenum molybdopterin cofactor Bos taurus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.17.3.2 xanthine + H2O + O2 Bos taurus
-
 urate + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.17.3.2 Bos taurus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.17.3.2 xanthine + H2O + O2 = urate + H2O2 favored mechanism for the reaction with xanthine, overview Bos taurus
a

Source Tissue

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.3.2 2-oxo-6-methylpurine + H2O + O2 low activity Bos taurus ? + H2O2
-
 ?
1.17.3.2 additional information quantum mechanical/molecular mechanical study of the reductive half-reaction of wild-type xanthine oxidase, overview Bos taurus ?
-
 ?
1.17.3.2 xanthine + H2O + O2
-
 Bos taurus urate + H2O2
-
 ?
1.17.3.2 xanthine + H2O + O2 effects of variations in the cofactor, the substrate, and the active site residue Glu802 on the reaction mechanism, overview Bos taurus urate + H2O2
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.17.3.2 1.16
-
 xanthine pH not specified in the publication, temperature not specified in the publication, mutant E802Q Bos taurus
1.17.3.2 108
-
 xanthine pH not specified in the publication, temperature not specified in the publication, wild-type enzyme Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.3.2 molybdenum cofactor [Mo(S2C2H2)(dO) (ORunfixed)(sSH)]2- moiety Bos taurus