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Literature summary extracted from

  • Pauff, J.M.; Hille, R.
    Inhibition studies of bovine xanthine oxidase by luteolin, silibinin, quercetin, and curcumin (2009), J. Nat. Prod., 72, 725-731.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.17.3.2 allopurinol a time-dependent inhibitor Bos taurus
1.17.3.2 luteolin competitive inhibition Bos taurus
1.17.3.2 additional information no inhibition by curcumin in vitro Bos taurus
1.17.3.2 quercetin competitive inhibition Bos taurus
1.17.3.2 silibinin a mixed-type, not-time-dependent inhibitor Bos taurus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.17.3.2 additional information
-
 additional information in vitro steady-state kinetic studies, kinetics with cofactor cytochrome C, overview Bos taurus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.17.3.2 extracellular secreted to milk Bos taurus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.17.3.2 Molybdenum a molybdenum-containing enzyme Bos taurus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.17.3.2 290000
-
-
 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 + O2 + H2O Bos taurus xanthine oxidoreductase exists in two forms. The protein normally exists as xanthine dehydrogenase, XDH, EC 1.17.1.4, and utilizes NAD+ as its final electron acceptor in catalysis. Under certain conditions, most notably schemia and/or hypoxia, XDH can be converted to an oxidase form, XO, which can no longer reduce NAD+ and instead utilizes O2 exclusively as the terminal electron acceptor in the course of turnover. This conversion may occur either by oxidation of sulfhydryl groups and/or by limited proteolysis 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 catalytic mechanism of xanthine oxidoreductase, 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 xanthine + cytochrome c + H2O
-
 Bos taurus urate + reduced cytochrome c
-
 ?
1.17.3.2 xanthine + O2 + H2O xanthine oxidoreductase exists in two forms. The protein normally exists as xanthine dehydrogenase, XDH, EC 1.17.1.4, and utilizes NAD+ as its final electron acceptor in catalysis. Under certain conditions, most notably schemia and/or hypoxia, XDH can be converted to an oxidase form, XO, which can no longer reduce NAD+ and instead utilizes O2 exclusively as the terminal electron acceptor in the course of turnover. This conversion may occur either by oxidation of sulfhydryl groups and/or by limited proteolysis Bos taurus urate + H2O2
-
 ?
1.17.3.2 xanthine + O2 + H2O conversion of xanthine to uric acid at the molybdenum-containing active site Bos taurus urate + H2O2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.17.3.2 XOR
-
 Bos taurus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.17.3.2 25
-
 assay at Bos taurus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.17.3.2 7.4
-
 assay at Bos taurus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.17.3.2 0.0012
-
 quercetin pH 7.4, 25°C Bos taurus
1.17.3.2 0.0019
-
 luteolin pH 7.4, 25°C Bos taurus