Kohen Amnon
Department of Chemistry, University of Iowa, Iowa City, IA, USA.
F1000Res. 2015 Dec 17;4. doi: 10.12688/f1000research.6968.1. eCollection 2015.
Dihydrofolate reductase from Escherichia coli (ecDHFR) serves as a model system for investigating the role of protein dynamics in enzyme catalysis. We discuss calculations predicting a network of dynamic motions that is coupled to the chemical step catalyzed by this enzyme. Kinetic studies testing these predictions are presented, and their potential use in better understanding the role of these dynamics in enzyme catalysis is considered. The cumulative results implicate motions across the entire protein in catalysis.
来自大肠杆菌的二氢叶酸还原酶(ecDHFR)作为一个模型系统,用于研究蛋白质动力学在酶催化中的作用。我们讨论了预测与该酶催化的化学步骤相关的动态运动网络的计算。展示了验证这些预测的动力学研究,并考虑了它们在更好地理解这些动力学在酶催化中的作用方面的潜在用途。累积结果表明整个蛋白质的运动参与了催化过程。