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QM/MM MD and Free Energy Simulation Study of Methyl Transfer Processes Catalyzed by PKMTs and PRMTs

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Abstract

Methyl transfer processes catalyzed by protein lysine methyltransferases (PKMTs) and protein arginine methyltransferases (PRMTs) control important biological events including transcriptional regulation and cell signaling. One important property of these enzymes is that different PKMTs and PRMTs catalyze the formation of different methylated product (product specificity). These different methylation states lead to different biological outcomes. Here, we review the results of quantum mechanics/molecular mechanics molecular dynamics and free energy simulations that have been performed to study the reaction mechanism of PKMTs and PRMTs and the mechanism underlying the product specificity of the methyl transfer processes.

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Authors and Affiliations

  1. School of Life Science and Biotechnology, Dalian University of Technology, Dalian, 116024, China

    Yuzhuo Chu

  2. Department of Biochemistry and Cellular and Molecular Biology, University of Tennessee, Knoxville, TN, 37996, USA

    Hong Guo

  3. UT/ORNL Center for Molecular Biophysics, Oak Ridge National Laboratory, Oak Ridge, TN, 37831-6164, USA

    Hong Guo

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  1. Yuzhuo Chu
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  2. Hong Guo
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Correspondence to Yuzhuo Chu.

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Chu, Y., Guo, H. QM/MM MD and Free Energy Simulation Study of Methyl Transfer Processes Catalyzed by PKMTs and PRMTs. Interdiscip Sci Comput Life Sci 7, 309–318 (2015). https://doi.org/10.1007/s12539-015-0280-y

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  • DOI: https://doi.org/10.1007/s12539-015-0280-y

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