| xanthine oxidase/dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Crystallographic structure (monomer) of bovine xanthine oxidase.[1] The bounded FAD (red), FeS-cluster (orange), the molybdopterin cofactor with molybdenum (yellow) and salicylate (blue) are indicated. | |||||||||
| Identifiers | |||||||||
| EC no. | 1.17.3.2 | ||||||||
| CAS no. | 9002-17-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
| xanthine oxidase/dehydrogenase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | XDH | ||||||
| NCBI gene | 7498 | ||||||
| HGNC | 12805 | ||||||
| OMIM | 607633 | ||||||
| PDB | 1FIQ | ||||||
| RefSeq | NM_000379 | ||||||
| UniProt | P47989 | ||||||
| Other data | |||||||
| EC number | 1.17.3.2 | ||||||
| Locus | Chr. 2 p23.1 | ||||||
| |||||||
Xanthine oxidase (XO or XAO) is a form of xanthine oxidoreductase, a type of enzyme that generates reactive oxygen species.[2] These enzymes catalyze the oxidation of hypoxanthine to xanthine and can further catalyze the oxidation of xanthine to uric acid. These enzymes play an important role in the catabolism of purines in some species, including humans.[3]
Xanthine oxidase is defined as an enzyme activity (EC 1.17.3.2).[4] The same protein, which in humans has the HGNC approved gene symbol XDH, can also have xanthine dehydrogenase activity (EC 1.17.1.4).[5] Most of the protein in the liver exists in a form with xanthine dehydrogenase activity, but it can be converted to xanthine oxidase by reversible sulfhydryl oxidation or by irreversible proteolytic modification.[6][7]
- ^ PDB: 1FIQ; Enroth C, Eger BT, Okamoto K, Nishino T, Nishino T, Pai EF (September 2000). "Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion". Proceedings of the National Academy of Sciences of the United States of America. 97 (20): 10723–8. Bibcode:2000PNAS...9710723E. doi:10.1073/pnas.97.20.10723. PMC 27090. PMID 11005854.
- ^ Ardan T, Kovaceva J, Cejková J (February 2004). "Comparative histochemical and immunohistochemical study on xanthine oxidoreductase/xanthine oxidase in mammalian corneal epithelium". Acta Histochemica. 106 (1): 69–75. doi:10.1016/j.acthis.2003.08.001. PMID 15032331.
- ^ Hille R, Hall J, Basu P (April 2014). "The Mononuclear Molybdenum Enzymes". Chemical Reviews. 114 (7): 3963–4038. doi:10.1021/cr400443z. PMC 4080432. PMID 24467397.
- ^ "KEGG record for EC 1.17.3.2". Genome.jp. Retrieved 23 December 2017.
- ^ "KEGG record for EC 1.17.1.4". Genome.jp. Retrieved 23 December 2017.
- ^ EntrezGene 7498 "XDH xanthine dehydrogenase"
- ^ Online Mendelian Inheritance in Man (OMIM): Xanthine dehydrogenase; XDH - 607633