Crystal Structures of Urate Bound Form of Xanthine Oxidoreductase: Substrate Orientation and Structure of the Key Reaction Intermediate
Crystal Structures of Urate Bound Form of Xanthine Oxidoreductase: Substrate Orientation and Structure of the Key Reaction Intermediate
复制标题
DOI：
10.1021/ja1077574
复制
发表时间：
2010-12-08
影响因子：
15
通讯作者：
Nishino, Takeshi
中科院分区：
文献类型：
--
作者：
Okamoto, Ken;Kawaguchi, Yuko;Nishino, Takeshi
对于黄嘌呤氧化还原酶与底物黄嘌呤的结合方式及其活化机制，提出了两种相互矛盾的模型。为了区分这两种模型，我们确定了大鼠黄嘌呤氧化还原酶D428A突变体在1.7埃和还原牛乳酶在2.1埃的demolybdo形式的尿酸盐复合物的晶体结构，后者代表反应中间体。结果清楚地表明底物黄嘌呤的催化相关结合模式。
Two contradictory models have been proposed for the binding mode of the substrate xanthine to and its activation mechanism by xanthine oxidoreductase. In an effort to distinguish between the two models, we determined the crystal structures of the urate complexes of the demolybdo-form of the D428A mutant of rat xanthine oxidoreductase at 1.7 angstrom and of the reduced bovine milk enzyme at 2.1 angstrom, the latter representing a reaction intermediate. The results clearly indicate the catalytically relevant binding mode of the substrate xanthine.