2FXL
Urate oxidase from aspergillus flavus complexed with allantoin
2FXL の概要
| エントリーDOI | 10.2210/pdb2fxl/pdb |
| 関連するPDBエントリー | 1R4S 1R4U 1R51 1R56 |
| 分子名称 | Uricase, 1-(2,5-DIOXO-2,5-DIHYDRO-1H-IMIDAZOL-4-YL)UREA (3 entities in total) |
| 機能のキーワード | oxidoreductase, uric acid degradation, dimeric barrel, tunnel-shaped protein, allantoin |
| 由来する生物種 | Aspergillus flavus |
| 細胞内の位置 | Peroxisome: Q00511 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 34355.69 |
| 構造登録者 | Gabison, L.,Chiadmi, M.,Colloc'h, N.,Prange, T. (登録日: 2006-02-06, 公開日: 2006-05-23, 最終更新日: 2023-08-30) |
| 主引用文献 | 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 Cited by 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: 16545381DOI: 10.1016/j.febslet.2006.03.007 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.76 Å) |
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