Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Tai, L.A.; Hwang, K.C.
    Regulation of xanthine oxidase activity by substrates at active sites via cooperative interactions between catalytic subunits: implication to drug pharmacokinetics (2011), Curr. Med. Chem., 18, 69-78.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.17.3.2 additional information
-
 additional information kinetic analysis, Michaelis-Menten model, detailed overview. Binding of a 6-formylpterin at one of the two xanthine oxidase active sites slows down the turnover rate of xanthine at the adjacent active site and converts the V-[S] plot from substrate inhibition kinetic pattern to a classical Michaelis-Menten hyperbolic saturation pattern. In contrast, binding of xanthine at an active site accelerates the turnover rate of 6-formylpterin at the neighboring active site Bos taurus

Localization

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.17.3.2 Fe2+ two 2Fe-2S clusters. The Mo(VI) ion at the active site is reduced to Mo(IV), which then transfers two electrons, via the 2Fe-2S clusters, to the FAD cofactor Bos taurus
1.17.3.2 Mo4+ the Mo(VI) ion at the active site is reduced to Mo(IV), which then transfers two electrons, via the 2Fe-2S clusters, to the FAD cofactor 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 + H2O + O2 Bos taurus
-
 urate + H2O2
-
 ?

Organism

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.17.3.2 commercial preparation
-
 Bos taurus
-
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-amino-4-hydroxypterin + H2O + O2 substrate inhibition kinetic pattern Bos taurus ? + H2O2
-
 ?
1.17.3.2 6-formylpterin + H2O + O2
-
 Bos taurus ? + H2O2
-
 ?
1.17.3.2 adenine + H2O + O2 substrate inhibition kinetic pattern Bos taurus ? + H2O2
-
 ?
1.17.3.2 lumazine + H2O + O2 classical Michaelis-Menten hyperbolic saturation kinetic pattern Bos taurus ? + H2O2
-
 ?
1.17.3.2 xanthine + H2O + O2
-
 Bos taurus urate + H2O2
-
 ?
1.17.3.2 xanthine + H2O + O2 substrate inhibition kinetic pattern Bos taurus urate + H2O2
-
 ?
1.17.3.2 xanthopterin + H2O + O2 substrate activation kinetic pattern Bos taurus ? + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.17.3.2 homodimer
-
 Bos taurus

Synonyms

EC Number Synonyms Comment Organism
1.17.3.2 XOD
-
 Bos taurus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.17.3.2 22
-
 assay at Bos taurus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.17.3.2 7.5
-
 assay at Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.3.2 FAD the Mo(VI) ion at the active site is reduced to Mo(IV), which then transfers two electrons, via the 2Fe-2S clusters, to the FAD cofactor Bos taurus
1.17.3.2 additional information the enzyme contains two 2Fe-2S clusters Bos taurus

General Information

EC Number General Information Comment Organism
1.17.3.2 additional information the enzyme is regulated by substrates at active sites via cooperative interactions between catalytic subunits. A substrate can regulate the activity of xanthine oxidase via binding at the active sites, or a xanthine oxidase catalytic subunit can simultaneously serve as a regulatory unit Bos taurus