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Literature summary extracted from
- 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.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.17.1.4 | C535A/C992R/C1316S | mutation in residues involved in conversion of xanthin dehydrogenase to xanthine oxidase by formation of disulfide bonds. Using guanidine-HCl, the mutant can be converted into the oxidase form | Rattus norvegicus |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 1.17.1.4 | conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant | Rattus norvegicus |
| 1.17.1.4 | conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant | Bos taurus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.17.1.4 | Guanidine-HCl | conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant. Above 3 M gunandine-HCl, even xanthine oxidase activity decreases drastically, but the xanthine oxidase form treated with 1.5 M can be completely reconverted into xanthine dehydrogenase by dialysis | Bos taurus |  |
| 1.17.1.4 | Guanidine-HCl | conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant | Rattus norvegicus | |
| 1.17.1.4 | Urea | conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant | Bos taurus | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.17.3.2 | extracellular | - |
Bos taurus | - |
- |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.17.3.2 | Fe2+ | in [2Fe-2S] centers of FAD cofactor | Bos taurus | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.17.3.2 | xanthine + H2O + O2 | Bos taurus | - |
urate + H2O2 | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.17.1.4 | Bos taurus | - |
- |
- |
| 1.17.1.4 | Rattus norvegicus | - |
- |
- |
| 1.17.3.2 | Bos taurus | - |
- |
- |
Renatured (Commentary)
| EC Number | Renatured (Comment) | Organism |
|---|---|---|
| 1.17.1.4 | conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant | Rattus norvegicus |
| 1.17.1.4 | conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant. Above 3 M guandine-HCl, even xanthine oxidase activity decreases drastically, but the xanthine oxidase form treated with 1.5 M can be completely reconverted into xanthine dehydrogenase by dialysis | Bos taurus |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.17.1.4 | liver | - |
Rattus norvegicus | - |
| 1.17.1.4 | milk | - |
Bos taurus | - |
| 1.17.3.2 | milk | - |
Bos taurus | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.17.1.4 | additional information | conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant | Rattus norvegicus | ? | - |
? | |
| 1.17.1.4 | additional information | conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant | Bos taurus | ? | - |
? | |
| 1.17.3.2 | 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 | ? | - |
? | |
| 1.17.3.2 | xanthine + H2O + O2 | - |
Bos taurus | urate + H2O2 | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.17.3.2 | 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
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.17.3.2 | xanthine oxidoreductase | - |
Bos taurus |
| 1.17.3.2 | XOR | - |
Bos taurus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.17.3.2 | 7.8 | - |
assay at | Bos taurus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.17.3.2 | FAD | required for reoxidation of the enzyme, contains two non-identical [2Fe-2S] centers | Bos taurus | |
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