Cloned (Comment) | Organism |
---|---|
expression of enzyme mutant D428A in Spodoptera frugiperda Sf9 cells via the baculovirus transfection system in mostly the demolybdo-form | Rattus norvegicus |
Crystallization (Comment) | Organism |
---|---|
urate complexes of the reduced form of native milk enzyme reaction intermediate, X-ray diffraction structure determination and analysis at 2.1 A resolution | Bos taurus |
XOR complexed with the artificial substrate 4-[5-pyridine-4-yl-1H-[1,2,4]triazol-3-yl]pyridine-2-carbonitril, FYX-051, crystal structure analysis. Urate complexes of the purified recombinant demolybdo-form of mutant D428A, X-ray diffraction structure determination and analysis at 1.7 A resolution | Rattus norvegicus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Bos taurus | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Iron | two [2Fe-2S] centers | Bos taurus | |
Iron | two [2Fe-2S] centers | Rattus norvegicus | |
Molybdenum | XOR is a molybdenum-containing enzyme. In the oxidized form of XORs, the Mo(VI) ion is in the center of a square-pyramidal geometry, coordinated by an oxo-ligand at the apical position and one hydroxo and one sulfido ligand at equatorial positions, in addition to the two vicinal sulfur ligands contributed by the pterin group, cofactor geometry, overview | Rattus norvegicus | |
Molybdenum | XOR is a molybdenum-containing enzyme. In the oxidized form of XORs, the Mo(VI) ion is in the center of a square-pyramidal geometry, coordinated by an oxo-ligand at the apical position and one hydroxo and one sulfido ligand at equatorial positions,3a in addition to the two vicinal sulfur ligands contributed by the pterin group, cofactor geometry, overview | Bos taurus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
hypoxanthine + 2 H2O + 2 O2 | Bos taurus | - |
urate + 2 H2O2 | - |
? | |
hypoxanthine + 2 H2O + 2 O2 | Rattus norvegicus | - |
urate + 2 H2O2 | - |
? | |
xanthine + H2O + O2 | Bos taurus | catalytically relevant binding mode of the substrate xanthine, overview | urate + H2O2 | - |
? | |
xanthine + H2O + O2 | Rattus norvegicus | catalytically relevant binding mode of the substrate xanthine, overview | urate + H2O2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bos taurus | - |
- |
- |
Rattus norvegicus | P22985 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
xanthine + H2O + O2 = urate + H2O2 | reaction mechanism of XOR and binding modes of the substrate xanthine, overview. The oxidative hydroxylation of purine substrates takes place at the molybdenum center. Reducing equivalents introduced there are then transferred via two [2Fe-2S] centers to the FAD cofactor where reduction of the physiological electron acceptors occurs, NAD+ in the case of the dehydrogenase form, XDH, or O2 in the oxidase form, XO, of the enzyme occur | Bos taurus | |
xanthine + H2O + O2 = urate + H2O2 | reaction mechanism of XOR and binding modes of the substrate xanthine, overview. The oxidative hydroxylation of purine substrates takes place at the molybdenum center. Reducing equivalents introduced there are then transferred via two [2Fe-2S] centers to the FAD cofactor where reduction of the physiological electron acceptors occurs, NAD+ in the case of the dehydrogenase form, XDH, or O2 in the oxidase form, XO, of the enzyme occur | Rattus norvegicus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
milk | - |
Bos taurus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
hypoxanthine + 2 H2O + 2 O2 | - |
Bos taurus | urate + 2 H2O2 | - |
? | |
hypoxanthine + 2 H2O + 2 O2 | - |
Rattus norvegicus | urate + 2 H2O2 | - |
? | |
xanthine + H2O + O2 | catalytically relevant binding mode of the substrate xanthine, overview | Bos taurus | urate + H2O2 | - |
? | |
xanthine + H2O + O2 | catalytically relevant binding mode of the substrate xanthine, overview | Rattus norvegicus | urate + H2O2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
More | XOR can adopt its XOR xanthine oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4 | Rattus norvegicus |
More | XOR can adopt its XOR xanthone oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4 | Bos taurus |
xanthine oxidoreductase | - |
Bos taurus |
xanthine oxidoreductase | - |
Rattus norvegicus |
XOR | - |
Bos taurus |
XOR | - |
Rattus norvegicus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Bos taurus | |
FAD | role of Asp428 in the FAD reactivity, overview | Rattus norvegicus | |
molybdenum cofactor | cofactor geometry, overview | Bos taurus | |
molybdenum cofactor | cofactor geometry, overview | Rattus norvegicus | |
additional information | cofactor conformation, binding structure analysis and mechanism, overview | Bos taurus | |
additional information | cofactor conformation, binding structure analysis and mechanism, overview | Rattus norvegicus |
General Information | Comment | Organism |
---|---|---|
additional information | XOR can adopt its XOR xanthine oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4 | Rattus norvegicus |
additional information | XOR can adopt its XOR xanthone oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4 | Bos taurus |