Structural highlights
Function
[URIC_ASPFL] Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Recapture of [S]-allantoin, the product of the two-step degradation of uric acid, by urate oxidase.,Gabison L, Chiadmi M, Colloc'h N, Castro B, El Hajji M, Prange T FEBS Lett. 2006 Apr 3;580(8):2087-91. Epub 2006 Mar 10. PMID:16545381[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gabison L, Chiadmi M, Colloc'h N, Castro B, El Hajji M, Prange T. Recapture of [S]-allantoin, the product of the two-step degradation of uric acid, by urate oxidase. FEBS Lett. 2006 Apr 3;580(8):2087-91. Epub 2006 Mar 10. PMID:16545381 doi:10.1016/j.febslet.2006.03.007
