The knowledge of sequence and structural properties of residues in the catalytic sites of enzymes is important for understanding the physiochemical basis of enzymatic catalysis. We reveal new features of the catalytic sites by analyzing the coevolutionary behavior of amino acid sequences. By performing direct coupling analysis of the sequences of homologous proteins, we construct the coevolution networks at the residue level. Based on the analysis of the topological features of the coevolution networks for a dataset including 20 enzymes, we show that there is significant correlation between the catalytic sites and topological features of protein coevolution networks. Residues at the catalytic center often correspond to the nodes with high values of centralities in the networks as characterized by the degree, betweenness, closeness, and Laplacian centrality. The results of this work provide a possible way to extract key coevolutionary information from the sequences of enzymes...

中文翻译：

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蛋白质进化网络中催化位点的拓扑特征的表征

酶催化位点中残基的序列和结构特性的知识对于理解酶催化的物理化学基础很重要。我们通过分析氨基酸序列的协同进化行为揭示了催化位点的新特征。通过对同源蛋白序列进行直接偶联分析，我们在残基水平上构建了协同进化网络。基于对包含20种酶的数据集的协同进化网络的拓扑特征的分析，我们表明蛋白质协同进化网络的催化位点与拓扑特征之间存在显着相关性。催化中心的残基通常对应于网络中中心度较高的节点，其特征是程度，中间性，亲密性，和拉普拉斯的中心地位。这项工作的结果提供了一种从酶序列中提取关键协同进化信息的可能方法。