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Literature summary for 1.17.3.2 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
Search for more literature for 1.17.3.2

Inhibitors

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

KM Value [mM]

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

Localization

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

Metals/Ions

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
290000
-
-
 Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
xanthine + H2O + O2 = urate + H2O2 catalytic mechanism of xanthine oxidoreductase, overview Bos taurus
a

Source Tissue

Source Tissue Comment Organism Textmining
milk
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
xanthine + cytochrome c + H2O
-
 Bos taurus urate + reduced cytochrome c
-
 ?
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
-
 ?
xanthine + O2 + H2O conversion of xanthine to uric acid at the molybdenum-containing active site Bos taurus urate + H2O2
-
 ?

Synonyms

Synonyms Comment Organism
XOR
-
 Bos taurus

Temperature Optimum [°C]

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

pH Optimum

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

Ki Value [mM]

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