QM/MM MD and Free Energy Simulation Study of Methyl Transfer Processes Catalyzed by PKMTs and PRMTs
| Autor: | Hong Guo, Yuzhuo Chu |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
Protein-Arginine N-Methyltransferases
Methyltransferase Stereochemistry Chemistry Lysine Health Informatics Histone-Lysine N-Methyltransferase Methylation Molecular Dynamics Simulation Molecular mechanics General Biochemistry Genetics and Molecular Biology Substrate Specificity Computer Science Applications QM/MM Molecular dynamics Catalytic Domain Biocatalysis Quantum Theory Thermodynamics Mutant Proteins |
| Zdroj: | Interdisciplinary Sciences: Computational Life Sciences. 7:309-318 |
| ISSN: | 1867-1462 1913-2751 |
| DOI: | 10.1007/s12539-015-0280-y |
| Popis: | 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 (QM/MM) molecular dynamics (MD) 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. |
| Databáze: | OpenAIRE |
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