Computational Design and Study of Artificial Selenoenzyme with Controllable Activity Based on an Allosteric Protein Scaffold |
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Authors: | Siyuan Li Wanjia Xu Shengnan Chu Ningning Ma Shengda Liu Xiumei Li Tingting Wang Xiaojia Jiang Fei Li Yijia Li Dongmei Zhang Prof Quan Luo Prof Junqiu Liu |
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Institution: | State Key Laboratory of Supramolecular Structure and Materials, Institute of Theoretical Chemistry, Jilin University, 2699 Qianjin Road, Changchun, 130012 China |
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Abstract: | The establishment of new enzymatic function in an existing scaffold is a great challenge for protein engineers. In previous work, a highly efficient artificial selenoenzyme with controllable activity was constructed, based on a Ca2+-responsive recoverin (Rn) protein. In this study, a design strategy combining docking, molecular dynamics, and MM-PBSA is presented, to predict the catalytically active site of glutathione peroxidase (GPx) on the allosteric domain of Rn. The energy contributions of the binding hot spot residues are evaluated further by energy decomposition analysis to determine the detailed substrate recognition mechanism of Rn, which provides clear guidance for artificial enzyme design for improved substrate binding (Michaelis–Menten constant, Km). |
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Keywords: | artificial enzymes enzyme design enzymes GPx mimics molecular modeling substrate recognition |
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