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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structures of the hydrolase domain of human 10-formyltetrahydrofolate dehydrogenase and its complex with a substrate analogue
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Structures of the hydrolase domain of human 10-formyltetrahydrofolate dehydrogenase and its complex with a substrate analogue

机译：水解酶的结构域的人类10-formyltetrahydrofolate脱氢酶及其复杂的底物类似物

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摘要

10-Formyltetrahydrofolate dehydrogenase is a ubiquitously expressed enzyme in the human body. It catalyses the formation of tetrahydrofolate and carbon dioxide from 10-formyltetrahydrofolate, thereby playing an important role in the human metabolism of one-carbon units. It is a two-domain protein in which the N-terminal domain hydrolyses 10-formyltetrahydrofolate into formate and tetrahydrofolate. The high-resolution crystal structure of the hydrolase domain from human 10-formyltetrahydrofolate dehydrogenase has been determined in the presence and absence of a substrate analogue. The structures reveal conformational changes of two loops upon ligand binding, while key active-site residues appear to be pre-organized for catalysis prior to substrate binding. Two water molecules in the structures mark the positions of key oxygen moieties in the catalytic reaction and reaction geometries are proposed based on the structural data.
机译：10-Formyltetrahydrofolate脱氢酶是一种无所不在地表达了对人体的酶。它催化作用tetrahydrofolate的形成和二氧化碳10-formyltetrahydrofolate,从而发挥人体新陈代谢的重要作用一个碳单位。n端结构域的水解10-formyltetrahydrofolate甲酸,tetrahydrofolate。从人类的水解酶结构域10-formyltetrahydrofolate脱氢酶已被确定的存在和缺乏底物类似物。构象变化对配体的两个循环绑定,而关键活性位点残基出现之前被pre-organized催化底物绑定。马克关键氧根的位置催化反应和反应的几何图形提出了基于结构的数据。

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