MetaCyc Enzyme: xanthine oxidase

Gene: Xdh Accession Number: G-10707 (MetaCyc)

Synonyms: xanthine oxidoreductase, xanthine dehydrogenase/oxidase

Species: Mus musculus

Subunit composition of xanthine oxidase = [Xdh]2
         xanthine oxidase monomer = Xdh

Xanthine oxidase has been purified to homogeneity from mouse liver after induction with bacterial lipopolysaccharide. The enzyme was a homodimer of 300 kDa, composed of two identical subunits of Mr 150 kDa each [Carpani90]. The enzyme can also catalyze the reaction of xanthine dehydrogenase. It is converted from the dehydrogenase form (D) to the oxidase form (O) reversibly through the oxidation of sulfhydryl groups [Corte72].

The gene encoding the enzyme has been cloned and characterized [Terao92, Cazzaniga94].

Molecular Weight of Polypeptide: 146.52 kD (from nucleotide sequence), 150.0 kD (experimental) [Carpani90 ]

Molecular Weight of Multimer: 300.0 kD (experimental) [Carpani90]

pI: 6.7 [Carpani90]

Unification Links: ArrayExpress:Q00519 , Mint:MINT-1866314 , PhosphoSite:Q00519 , Pride:Q00519 , Protein Model Portal:Q00519 , SMR:Q00519 , String:10090.ENSMUSP00000024866 , UniProt:Q00519

Relationship Links: InterPro:IN-FAMILY:IPR000674 , InterPro:IN-FAMILY:IPR001041 , InterPro:IN-FAMILY:IPR002346 , InterPro:IN-FAMILY:IPR002888 , InterPro:IN-FAMILY:IPR005107 , InterPro:IN-FAMILY:IPR006058 , InterPro:IN-FAMILY:IPR008274 , InterPro:IN-FAMILY:IPR012675 , InterPro:IN-FAMILY:IPR014307 , InterPro:IN-FAMILY:IPR014309 , InterPro:IN-FAMILY:IPR016166 , InterPro:IN-FAMILY:IPR016167 , InterPro:IN-FAMILY:IPR016169 , InterPro:IN-FAMILY:IPR016208 , InterPro:IN-FAMILY:IPR022407 , Pfam:IN-FAMILY:PF00111 , Pfam:IN-FAMILY:PF00941 , Pfam:IN-FAMILY:PF01315 , Pfam:IN-FAMILY:PF01799 , Pfam:IN-FAMILY:PF02738 , Pfam:IN-FAMILY:PF03450 , Prosite:IN-FAMILY:PS00197 , Prosite:IN-FAMILY:PS00559 , Prosite:IN-FAMILY:PS51085 , Prosite:IN-FAMILY:PS51387 , Smart:IN-FAMILY:SM01008 , Smart:IN-FAMILY:SM01092

In Reactions of unknown directionality:

Not in pathways:
a xanthine dehydrogenase + glutathione disulfide = a xanthine oxidase + 2 glutathione

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Created 29-May-2008 by Caspi R , SRI International

Enzymatic reaction of: xanthine dehydrogenase (xanthine oxidase)

EC Number:

xanthine + NAD+ + H2O <=> urate + NADH + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

This reaction is reversible.

In Pathways: purine nucleotides degradation II (aerobic) , guanosine nucleotides degradation III , urate biosynthesis/inosine 5'-phosphate degradation

Enzymatic reaction of: xanthine oxidase

EC Number:

xanthine + oxygen + H2O <=> urate + hydrogen peroxide

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

Cofactors or Prosthetic Groups: FAD

Kinetic Parameters:

Km (μM)


Carpani90: Carpani G, Racchi M, Ghezzi P, Terao M, Garattini E (1990). "Purification and characterization of mouse liver xanthine oxidase." Arch Biochem Biophys 279(2);237-41. PMID: 2350174

Cazzaniga94: Cazzaniga G, Terao M, Lo Schiavo P, Galbiati F, Segalla F, Seldin MF, Garattini E (1994). "Chromosomal mapping, isolation, and characterization of the mouse xanthine dehydrogenase gene." Genomics 23(2);390-402. PMID: 7835888

Corte72: Corte ED, Stirpe F (1972). "The regulation of rat liver xanthine oxidase. Involvement of thiol groups in the conversion of the enzyme activity from dehydrogenase (type D) into oxidase (type O) and purification of the enzyme." Biochem J 126(3);739-45. PMID: 4342395

Terao92: Terao M, Cazzaniga G, Ghezzi P, Bianchi M, Falciani F, Perani P, Garattini E (1992). "Molecular cloning of a cDNA coding for mouse liver xanthine dehydrogenase. Regulation of its transcript by interferons in vivo." Biochem J 283 ( Pt 3);863-70. PMID: 1590774

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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