3OBP

Anaerobic complex of urate oxidase with uric acid

3OBP の概要

• エントリーDOI: 10.2210/pdb3obp/pdb
• 関連するPDBエントリー: 1R4S 3BJP
• 分子名称: Uricase, URIC ACID, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: uric acid, inhibition, degradation mechanism, oxidoreductase, peroxisome, purine metabolism
• 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: 34374.69

構造登録者

Gabison, L.,Chopard, C.,Colloc'h, N.,El Hajji, M.,Castro, B.,Chiadmi, M.,Prange, T. (登録日: 2010-08-08, 公開日: 2011-06-22, 最終更新日: 2024-10-16)

主引用文献

Gabison, L.,Chopard, C.,Colloc'h, N.,Peyrot, F.,Castro, B.,Hajji, M.E.,Altarsha, M.,Monard, G.,Chiadmi, M.,Prange, T.
X-ray, ESR, and quantum mechanics studies unravel a spin well in the cofactor-less urate oxidase.
Proteins, 79:1964-1976, 2011

PubMed Abstract: Urate oxidase (EC 1.7.3.3 or UOX) catalyzes the conversion of uric acid using gaseous molecular oxygen to 5-hydroxyisourate and hydrogen peroxide in absence of any cofactor or transition metal. The catalytic mechanism was investigated using X-ray diffraction, electron spin resonance spectroscopy (ESR), and quantum mechanics calculations. The X-ray structure of the anaerobic enzyme-substrate complex gives credit to substrate activation before the dioxygen fixation in the peroxo hole, where incoming and outgoing reagents (dioxygen, water, and hydrogen peroxide molecules) are handled. ESR spectroscopy establishes the initial monoelectron activation of the substrate without the participation of dioxygen. In addition, both X-ray structure and quantum mechanic calculations promote a conserved base oxidative system as the main structural features in UOX that protonates/deprotonates and activate the substrate into the doublet state now able to satisfy the Wigner's spin selection rule for reaction with molecular oxygen in its triplet ground state.

PubMed: 21491497
DOI: 10.1002/prot.23022

実験手法

X-RAY DIFFRACTION (1.5 Å)