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Literature summary for 1.17.3.2 extracted from

  • Nishino, T.; Okamoto, K.; Eger, B.T.; Pai, E.F.; Nishino, T.
    Mammalian xanthine oxidoreductase - mechanism of transition from xanthine dehydrogenase to xanthine oxidase (2008), FEBS J., 275, 3278-3289.
    View publication on PubMed
Search for more literature for 1.17.3.2

Crystallization (Commentary)

Crystallization (Comment) Organism
W335A/F336L double mutant enzyme crystal structure analysis Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
W335A/F336L xanthine oxidase locked mutant Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Rattus norvegicus 5829
-
extracellular secreted to milk Bos taurus
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
xanthine + O2 + H2O Rattus norvegicus
-
 urate + H2O2
-
 ?
xanthine + O2 + H2O Bos taurus
-
 urate + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Rattus norvegicus
-
 male Wistar rats
-

Purification (Commentary)

Purification (Comment) Organism
from liver Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Rattus norvegicus
-
milk
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
FYX-051 + O2 + H2O the structure of bovine XOR exposed to the slow-reacting substrate FYX-051 shows a covalent intermediate of the hydroxylation reaction, in which the hydroxyl oxygen bridged the molybdenumatom and the acceptor carbon atom of the aromatic ring of the substrate Bos taurus ?
-
 ?
additional information the oxidation of xanthine takes place at the molybdenum center, and the electrons thus introduced are rapidly transferred to FAD via the Fe-SI and Fe-SII centers. Glu1261, located near the Mo-OH in the salicylate bound-form of XOR, initiates catalysis by deprotonating the Mo-OH group Bos taurus ?
-
 ?
additional information the oxidation of xanthine takes place at the molybdenum cofactor, and the electrons thus introduced are rapidly transferred to FAD via the Fe-SI and Fe-SII centers. Glu1261, located near the Mo-OH in the salicylate bound-form of XOR, initiates catalysis by deprotonating the Mo-OH group Rattus norvegicus ?
-
 ?
xanthine + O2 + H2O
-
 Rattus norvegicus urate + H2O2
-
 ?
xanthine + O2 + H2O
-
 Bos taurus urate + H2O2
-
 ?
xanthine + O2 + H2O binding modes of the substrate xanthine and mechanism of its hydroxylation, overview Rattus norvegicus urate + H2O2
-
 ?
xanthine + O2 + H2O binding modes of the substrate xanthine and mechanism of its hydroxylation, overview Bos taurus urate + H2O2
-
 ?

Subunits

Subunits Comment Organism
More structural comparison of xanthine dehydrogenase, EC 1.17.1.4, and xanthine oxidase, overview Rattus norvegicus

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
FAD the FAD cofactor is open to solvent in XO, but much less accessible in XDH, binding site structure, overview Rattus norvegicus
FAD the FAD cofactor is open to solvent in XO, but much less accessible in XDH, binding site structure, overview Bos taurus
molybdenum cofactor structure-function analysis, mechanism, overview Rattus norvegicus
molybdenum cofactor structure-function analysis, mechanism, overview Bos taurus

General Information

General Information Comment Organism
physiological function xanthine oxidoreductase catalyzes the oxidation of hypoxanthine to xanthine or xanthine to uric acid in the metabolic pathway of purine degradation Rattus norvegicus
physiological function xanthine oxidoreductase catalyzes the oxidation of hypoxanthine to xanthine or xanthine to uric acid in the metabolic pathway of purine degradation Bos taurus