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题名: QM/MM MD and free energy simulations of the methylation reactions catalyzed by protein arginine methyltransferase PRMT3
作者: Chu, Yuzhuo1, 2;  Li, Guohui3;  Guo, Hong1, 4
关键词: protein arginine methyltransferases ;  product specificity ;  QM/MM ;  MD and free energy simulations ;  reaction mechanism
刊名: CANADIAN JOURNAL OF CHEMISTRY-REVUE CANADIENNE DE CHIMIE
发表日期: 2013-07-01
DOI: 10.1139/cjc-2012-0483
卷: 91, 期:7, 页:605-612
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology ;  Physical Sciences
类目[WOS]: Chemistry, Multidisciplinary
研究领域[WOS]: Chemistry
英文摘要: Protein arginine N-methyltransferases (PRMTs) catalyze the transfer of methyl group(s) from S-adenosyl-L-methionine (AdoMet) to the guanidine group of arginine residue in abundant eukaryotic proteins. Two major types of PRMTs have been identified in mammalian cells. Type I PRMTs catalyze the formation of asymmetric omega-N-G, N-G-dimethylarginine (ADMA), while Type II PRMTs catalyze the formation of symmetric omega-N-G, N'(G)-dimethylarginine (SDMA). The two different methylation products (ADMA or SDMA) of the substrate could lead to different biological consequences. Although PRMTs have been the subject of extensive experimental investigations, the origin of the product specificity remains unclear. In this study, quantum mechanical/molecular mechanical (QM/MM) molecular dynamics (MD) and free energy simulations are performed to study the reaction mechanism for one of Type I PRMTs, PRMT3, and to gain insights into the energetic origin of its product specificity (ADMA). Our simulations have identified some important interactions and proton transfers involving the active site residues. These interactions and proton transfers seem to be responsible, at least in part, in making the N-eta 2 atom of the substrate arginine the target of the both 1st and 2nd methylations, leading to the asymmetric dimethylation product. The simulations also suggest that the methyl transfer and proton transfer appear to be somehow concerted processes and that Glu326 is likely to function as the general base during the catalysis.
关键词[WOS]: SERINE-CARBOXYL PEPTIDASE ;  PRODUCT SPECIFICITY ;  MOLECULAR-DYNAMICS ;  ENZYME CATALYSIS ;  TIGHT-BINDING ;  MECHANISM ;  RESIDUES ;  STABILIZATION ;  INSIGHTS ;  ORIGINS
语种: 英语
WOS记录号: WOS:000321436200016
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/137584
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

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作者单位: 1.Univ Tennessee, Dept Biochem Cellular & Mol Biol, Knoxville, TN 37996 USA
2.Univ Tennessee, Natl Inst Math & Biol Synth, Knoxville, TN 37996 USA
3.Chinese Acad Sci, Dalian Inst Chem Phys, State Key Lab Mol React Dynam, Lab Mol Modeling & Design, Dalian 116023, Peoples R China
4.Oak Ridge Natl Lab, UT ORNL Ctr Mol Biophys, Oak Ridge, TN 37830 USA

Recommended Citation:
Chu, Yuzhuo,Li, Guohui,Guo, Hong. QM/MM MD and free energy simulations of the methylation reactions catalyzed by protein arginine methyltransferase PRMT3[J]. CANADIAN JOURNAL OF CHEMISTRY-REVUE CANADIENNE DE CHIMIE,2013,91(7):605-612.
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