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首页> 外文期刊>Biochimica et Biophysica Acta. Protein Structure and Molecular Enzymology >The pyruvate dehydrogenase multi-enzyme complex from Gram-negative bacteria
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The pyruvate dehydrogenase multi-enzyme complex from Gram-negative bacteria

机译：革兰氏阴性细菌的丙酮酸脱氢酶多酶复合物

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摘要

Pyruvate dehydrogenase multi-enzyme complexes from Gram-negative bacteria consists of three enzymes, pyruvate dehydrogenase/decarboxylase (E1p), dihydrolipoyl acetyltransferase (E2p) and dihydrolipoyl dehydrogenase (E3). The acetyltransferase harbors all properties required for multi-enzyme catalysis: it forms a large core of 24 subunits, it contains multiple binding sites for the E1p and E3 components, the acetyltransferase catalytic site and mobile substrate carrying lipoyl domains that visit the active sites. Today, the Azotobacter vinelandii complex is the best understood oxo acid dehydrogenase complex with respect to structural details. A description of multi-enzyme catalysis starts with the structural and catalytic properties of the individual components of the complex. Integration of the individual properties is obtained by a description of how the many copies of the individual enzymes are arranged in the complex and how the lipoyl domains couple the activities of the respective active sites by way of flexible linkers. These latter aspects are the most difficult to study and future research need to be aimed at these properties.
机译：革兰氏阴性细菌的丙酮酸脱氢酶多酶复合物由三种酶组成，即丙酮酸脱氢酶/脱羧酶（E1p），二氢脂酰乙酰基转移酶（E2p）和二氢脂酰脱氢酶（E3）。乙酰基转移酶具有多酶催化所需的所有特性：它形成24个亚基的大核心，它包含E1p和E3组分的多个结合位点，乙酰基转移酶催化位点和携带带脂酰结构域的可移动底物，这些活性位点访问活性位点。今天，就结构细节而言，葡萄固氮菌（Azotobacter vinelandii）复合物是最广为人知的含氧酸脱氢酶复合物。对多酶催化的描述始于配合物各个组分的结构和催化性能。通过描述单个酶的多个拷贝在复合物中的排列方式以及脂酰结构域如何通过柔性接头连接各个活性位点的活性，来获得单个特性的整合。后面这些方面最难研究，将来需要针对这些特性进行研究。

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