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首页> 外文期刊>The FEBS journal >In silico analysis of the adenylation domains of the freestanding enzymes belonging to the eucaryotic nonribosomal peptide synthetase-like family
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In silico analysis of the adenylation domains of the freestanding enzymes belonging to the eucaryotic nonribosomal peptide synthetase-like family

机译：计算机分析真核生物非核糖体肽合成酶样家族的独立酶的腺苷酸化域

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摘要

This work presents a computational analysis of the molecular characteristics shared by the adenylation domains from traditional nonribosomal peptide synthetases (NRPSs) and the group of the freestanding homologous enzymes: alpha-aminoadipate semialdehyde dehydrogenase, alpha-aminoadipate reductase and the protein Ebony. The results of systematic sequence comparisons allow us to conclude that a specificity-conferring code, similar to that described for the NRPSs, can be recognized in such enzymes. The structural and functional roles of the residues involved in the substrate selection and binding are proposed through the analysis of the predicted interactions of the model active sites and their respective substrates. The indications deriving from this study can be useful for the programming of experiments aimed at a better characterization and at the engineering of this emerging group of single NRPS modules that are responsible for amino acid selection, activation and modification in the absence of other NRPS assembly line components.
机译：这项工作提出了对来自传统的非核糖体肽合成酶（NRPS）和独立的同源酶类的腺苷酸化域所共有的分子特性的计算分析。系统性序列比较的结果使我们得出结论，在此类酶中可以识别出类似于针对NRPS所述的赋予特异性的密码。通过分析模型活性位点及其各自底物的预测相互作用，提出了参与底物选择和结合的残基的结构和功能作用。这项研究得出的适应症可用于旨在更好地表征的实验程序，以及该新兴的单个NRPS模块组的工程设计，这些模块负责在没有其他NRPS生产线的情况下进行氨基酸的选择，激活和修饰。组件。

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