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Literature summary for 1.17.3.2 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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Bos taurus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
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
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]

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 + H2O + O2 Bos taurus
-
urate + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
Bos taurus
-
milk
-
Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-amino-4-hydroxypterin + H2O + O2 substrate inhibition kinetic pattern Bos taurus ? + H2O2
-
?
6-formylpterin + H2O + O2
-
Bos taurus ? + H2O2
-
?
adenine + H2O + O2 substrate inhibition kinetic pattern Bos taurus ? + H2O2
-
?
lumazine + H2O + O2 classical Michaelis-Menten hyperbolic saturation kinetic pattern Bos taurus ? + H2O2
-
?
xanthine + H2O + O2
-
Bos taurus urate + H2O2
-
?
xanthine + H2O + O2 substrate inhibition kinetic pattern Bos taurus urate + H2O2
-
?
xanthopterin + H2O + O2 substrate activation kinetic pattern Bos taurus ? + H2O2
-
?

Subunits

Subunits Comment Organism
homodimer
-
Bos taurus

Synonyms

Synonyms Comment Organism
XOD
-
Bos taurus

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
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
additional information the enzyme contains two 2Fe-2S clusters Bos taurus

General Information

General Information Comment Organism
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