| Literature DB >> 9360612 |
N Colloc'h1, M el Hajji, B Bachet, G L'Hermite, M Schiltz, T Prangé, B Castro, J P Mornon.
Abstract
The gene coding for urate oxidase, an enzyme that catalyzes the oxidation of uric acid to allantoin, is inactivated in humans. Consequently, urate oxidase is used as a protein drug to overcome severe disorders induced by uric acid accumulation. The structure of the active homotetrameric enzyme reveals the existence of a small architectural domain that we call T-fold (for tunnelling-fold) domain. It assembles to form a perfect unusual dimeric alpha 8 beta 16 barrel. Urate oxidase may be the archetype of an expanding new family of tunnel-shaped proteins that now has three members; tetrahydropterin synthase, GTP cyclohydrolase I and urate oxidase. The structure of the active site of urate oxidase around the 8-azaxanthine inhibitor reveals an original mechanism of oxidation that does not require any ions or prosthetic groups.Entities:
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Year: 1997 PMID： 9360612 DOI： 10.1038/nsb1197-947
Source DB: PubMed Journal: Nat Struct Biol ISSN： 1072-8368