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urate oxidase
The enzyme urate oxidase (UO), or uricase or factor-independent urate hydroxylase, absent in humans, catalyzes the oxidation of uric acid to 5-hydroxyisourate:
:Uric acid + O2 + H2O → 5-hydroxyisourate + H2O2 → allantoin + CO2
==Structure==
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 dalton. 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.
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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