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Literature summary for 1.17.3.2 extracted from

  • Tsujii, A.; Nishino, T.
    Mechanism of transition from xanthine dehydrogenase to xanthine oxidase: Effect of guanidine-HCl or urea on the activity (2008), Nucleosides Nucleotides Nucleic Acids, 27, 881-887.
    View publication on PubMed

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ in [2Fe-2S] centers of FAD cofactor 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
milk
-
Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme also catalyzes the oxidation of hypoxanthine to xanthine as xanthine dehydrogenase, EC 1.17.1.4, using NAD+ a oxidant substrate, XDH, mechanism of transition between XOR and XDH, after conversion reversibly via disulfide formation or irreversibly via proteolytic cleavage involving residues R335, R427, W336, and F549, overview Bos taurus ?
-
?
xanthine + H2O + O2
-
Bos taurus urate + H2O2
-
?

Subunits

Subunits Comment Organism
More comparison of structural alterations of xanthine oxidase leading to xanthine dehydrogenase, EC 1.17.14, activity involving residues R335, R427, W336, and F549, mechanism of transition, overview Bos taurus

Synonyms

Synonyms Comment Organism
xanthine oxidoreductase
-
Bos taurus
XOR
-
Bos taurus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
assay at Bos taurus

Cofactor

Cofactor Comment Organism Structure
FAD required for reoxidation of the enzyme, contains two non-identical [2Fe-2S] centers Bos taurus