Urate oxidase
| UOX | |||||||
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| Aliases | UOX, UOXP, URICASE, Urate oxidase, urate oxidase (pseudogene) | ||||||
| External IDs | GeneCards: UOX | ||||||
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| Species | Human | Mouse | |||||
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| Location (UCSC) | n/a | n/a | |||||
| PubMed search | n/a | ||||||
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| factor-independent urate hydroxylase | |||||||||
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| EC number | 1.7.3.3 | ||||||||
| CAS number | 9002-12-4 | ||||||||
| 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 | ||||||||
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| PMC | articles |
| PubMed | articles |
| NCBI | proteins |
| Uricase | |||||||||
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| Symbol | Uricase | ||||||||
| Pfam | PF01014 | ||||||||
| InterPro | IPR002042 | ||||||||
| PROSITE | PDOC00315 | ||||||||
| SCOP | 1uox | ||||||||
| SUPERFAMILY | 1uox | ||||||||
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| Available protein structures: | |
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| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
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The enzyme urate oxidase (UO), or uricase or factor-independent urate hydroxylase, absent in humans, catalyzes the oxidation of uric acid to 5-hydroxyisourate:
Urate oxidase is mainly localised in the liver, where it forms a large electron-dense paracrystalline core in many peroxisomes. The enzyme exists as a tetramer of identical subunits, each containing a possible type 2 copper-binding site.
Urate oxidase is a homotetrameric enzyme containing four identical active sites situated at the interfaces between its four subunits. UO from A. flavus is made up of 301 residues and has a molecular weight of 33438 daltons. It is unique among the oxidases in that it does not require a metal atom or an organic co-factor for catalysis. Sequence analysis of several organisms has determined that there are 24 amino acids which are conserved, and of these, 15 are involved with the active site.
Of all animals that include meat in their diet, humans are the only animal that is unable to break down uric acid to allantoin. This is because humans do not have the necessary enzyme uricase. This leads to an increased possibility of an accumulation of uric acid in the body when animal products are eaten.
Humans do have a gene for urate oxidase, but it is nonfunctional. Thus uric acid is the end product of catabolism of purines in humans. Excessive concentration of uric acid in the blood stream leads to gout.
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Wikipedia