1. Recapture of [S]-allantoin, the product of the two-step degradation of uric acid, by urate oxidase.
- Author
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Gabison L, Chiadmi M, Colloc'h N, Castro B, El Hajji M, and Prangé T
- Subjects
- Aspergillus flavus enzymology, Binding Sites, Crystallography, X-Ray, Models, Molecular, Molecular Conformation, Recombinant Proteins metabolism, Uric Acid chemistry, Allantoin metabolism, Urate Oxidase metabolism, Uric Acid metabolism
- Abstract
Urate oxidase from Aspergillus flavus catalyzes the degradation of uric acid to [S]-allantoin through 5-hydroxyisourate as a metastable intermediate. The second degradation step is thought either catalyzed by another specific enzyme, or spontaneous. The structure of the enzyme was known at high resolution by X-ray diffraction of I222 crystals complexed with a purine-type inhibitor (8-azaxanthin). Analyzing the X-ray structure of urate oxidase treated with an excess of urate, the natural substrate, shows unexpectedly that the active site recaptures [S]-allantoin from the racemic end product of a second degradation step.
- Published
- 2006
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