To create better enzyme for enhanced yield of industrial products is a challenging task in protein engineering. It requires lots of resources to manipulate or mutate enzymes experimentally. Computational biology helps in studying the mutational effects on enzymes’ structure and stability. The enzyme selected for our study is a Resveratrol-cleaving Dioxygenase that convert resveratrol to vanillin. Using comprehensive computational investigation, we studied the catalytic activity of Resveratrol-cleaving Dioxygenase at the molecular level. We introduced site directed mutations to create mutants of the Resveratrol-cleaving Dioxygenase and studied its interactions with resveratrol by Molecular docking and Molecular dynamics simulations. Here, by investigating the interactions between the mutant Resveratrol-cleaving Dioxygenase and the substrate allow us to highlight the improved performance of mutants over the wild type Resveratrol-cleaving Dioxygenase. It was observed that mutant1 is as stable as wild type of enzyme and has a better affinity toward substrate as the formation of hydrogen bond has increased as compared to wild type. Hence we propose that mutant1 if created in lab could provide better yield.

中文翻译：

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白藜芦醇裂解双加氧酶促进香兰素合成的突变分析

为提高工业产品的产量创造更好的酶是蛋白质工程中的一项具有挑战性的任务。它需要大量资源来通过实验来操纵或变异酶。计算生物学有助于研究突变对酶结构和稳定性的影响。为我们的研究选择的酶是一种白藜芦醇裂解双加氧酶，可将白藜芦醇转化为香草醛。通过综合计算研究，我们在分子水平上研究了白藜芦醇裂解双加氧酶的催化活性。我们引入定点突变以创建白藜芦醇裂解双加氧酶的突变体，并通过分子对接和分子动力学模拟研究其与白藜芦醇的相互作用。这里，通过研究突变体白藜芦醇裂解双加氧酶与底物之间的相互作用，我们可以突出突变体相对于野生型白藜芦醇裂解双加氧酶的性能改进。观察到突变体1与野生型酶一样稳定，并且由于与野生型相比氢键的形成增加，因此对底物具有更好的亲和力。因此，我们建议在实验室中创建的突变体 1 可以提供更好的产量。