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Literature summary for 1.17.1.4 extracted from
- Crystal structures of mammalian xanthine oxidoreductase bound with various inhibitors: allopurinol, febuxostat, and FYX-051 (2008), J. Nippon Med. Sch., 75, 2-3.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| in complex with inhibotrs allopurinol, febuxostat, and FYX-051 | Bos taurus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| allopurinol | mechanism-based inhibitor. Allopurinol is oxidized by xanthine oxidoreductase itself to oxypurinol which forms a covalent bond with the reduced molybdenium atom | Bos taurus |  |
| febuxostat | structure-based inhibitor, forms numerous hydrogen bonds, slat bridges, and hydrophobic interactions with amino acids in the active site and nearly completely fills the narrow channel leading to the molydbenum center of the enzyme | Bos taurus | |
| FYX-051 | inhibitor has features of both a mechanism-based and a structure-based inhibitor. It is a slow substrate and forms a stable reaction intermediate with the molybdenum atom in the enzyme | Bos taurus | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Molybdenum | - |
Bos taurus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
- |
- |
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