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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structures of Arthrobacter globiformis urate oxidase-ligand complexes.
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Structures of Arthrobacter globiformis urate oxidase-ligand complexes.

机译：结构节细菌属globiformis尿酸盐oxidase-ligand复合物。

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摘要

The enzyme urate oxidase catalyzes the conversion of uric acid to 5-hydroxyisourate, one of the steps in the ureide pathway. Arthrobacter globiformis urate oxidase (AgUOX) was crystallized and structures of crystals soaked in the substrate uric acid, the inhibitor 8-azaxanthin and allantoin have been determined at 1.9-2.2 A resolution. The biological unit is a homotetramer and two homotetramers comprise the asymmetric crystallographic unit. Each subunit contains two T-fold domains of betabetaalphaalphabetabeta topology, which are usually found in purine- and pterin-binding enzymes. The uric acid substrate is bound tightly to the enzyme by interactions with Arg180, Leu222 and Gln223 from one subunit and with Thr67 and Asp68 of the neighbouring subunit in the tetramer. In the other crystal structures, lithium borate, 8-azaxanthin and allantoate are bound to the enzyme in a similar manner as uric acid. Based on these AgUOX structures, the enzymatic reaction mechanism of UOX has been proposed.
机译：尿酸盐氧化酶催化转换尿酸5-hydroxyisourate,其中的一个酰脲通路中的步骤。globiformis尿酸氧化酶(AgUOX)结晶和结构的晶体浸泡在衬底尿酸,抑制剂8-azaxanthin和尿囊素已经确定在1.9 - -2.2的决议。homotetramer和两个homotetramers组成不对称晶体单元。包含两个T-fold域betabetaalphaalphabetabeta拓扑,通常在嘌呤和pterin-binding发现酶。酶的相互作用Arg180 Leu222从一个单元和Gln223 Thr67和Asp68邻近单元的四聚物。硼酸锂,8-azaxanthin allantoate绑定到尿酸酶以类似的方式酸。UOX的酶促反应机制建议。

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