2FXL

Urate oxidase from aspergillus flavus complexed with allantoin

Summary for 2FXL

• Entry DOI: 10.2210/pdb2fxl/pdb
• Related: 1R4S 1R4U 1R51 1R56
• Descriptor: Uricase, 1-(2,5-DIOXO-2,5-DIHYDRO-1H-IMIDAZOL-4-YL)UREA (3 entities in total)
• Functional Keywords: oxidoreductase, uric acid degradation, dimeric barrel, tunnel-shaped protein, allantoin
• Biological source: Aspergillus flavus
• Cellular location: Peroxisome: Q00511
• Total number of polymer chains: 1
• Total formula weight: 34355.69

Authors

Gabison, L.,Chiadmi, M.,Colloc'h, N.,Prange, T. (deposition date: 2006-02-06, release date: 2006-05-23, Last modification date: 2023-08-30)

Primary citation

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., 580:2087-2091, 2006

PubMed 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.

PubMed: 16545381
DOI: 10.1016/j.febslet.2006.03.007

Experimental method

X-RAY DIFFRACTION (1.76 Å)