QM/MM MD and free energy simulations of the methylation reactions catalyzed by protein arginine methyltransferase PRMT3
文献类型：期刊论文
| 作者 | Chu, Yuzhuo1,2; Li, Guohui3; Guo, Hong1,4 |
| 刊名 | canadian journal of chemistry-revue canadienne de chimie
 |
| 出版日期 | 2013-07-01 |
| 卷号 | 91期号:7页码:605-612 |
| 关键词 | protein arginine methyltransferases product specificity QM/MM MD and free energy simulations reaction mechanism |
| 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. |
| WOS标题词 | science & technology ; physical sciences |
| 类目[WOS] | chemistry, multidisciplinary |
| 研究领域[WOS] | chemistry |
| 关键词[WOS] | serine-carboxyl peptidase ; product specificity ; molecular-dynamics ; enzyme catalysis ; tight-binding ; mechanism ; residues ; stabilization ; insights ; origins |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000321436200016 |
| 公开日期 | 2015-11-10 |
| 源URL | [http://159.226.238.44/handle/321008/137535]  |
| 专题 | 大连化学物理研究所_中国科学院大连化学物理研究所 |
| 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 |
| 推荐引用方式 GB/T 7714 | 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. |
| APA | Chu, Yuzhuo,Li, Guohui,&Guo, Hong.(2013).QM/MM MD and free energy simulations of the methylation reactions catalyzed by protein arginine methyltransferase PRMT3.canadian journal of chemistry-revue canadienne de chimie,91(7),605-612. |
| MLA | Chu, Yuzhuo,et al."QM/MM MD and free energy simulations of the methylation reactions catalyzed by protein arginine methyltransferase PRMT3".canadian journal of chemistry-revue canadienne de chimie 91.7(2013):605-612. |
入库方式： OAI收割
来源：大连化学物理研究所
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