S. P. Singh, C. R. Deb, N. Lakhmi, an Kakati, B. K. Konwar
{"title":"MD Simulation Studies of Fumarase Reveal Thermo Dynamical Stability","authors":"S. P. Singh, C. R. Deb, N. Lakhmi, an Kakati, B. K. Konwar","doi":"10.4172/2161-0398.1000206","DOIUrl":null,"url":null,"abstract":"Fumarase enzyme is known to catalyse the stereo specific inter conversion of fumarate to L-malate which is a part of the Krebs cycle. Despite the biological significance and importance of this enzyme, the reaction mechanism of fumarase is not completely understood or known. In this context an experiment on molecular dynamics simulation was carried out for at least 10 nanoseconds molecular dynamics simulation run using Nano Scale Molecular Dynamics program implemented in Discovery Studio 4.0. The trajectory analysis of various energy parameters revealed the thermo dynamical stability of the enzyme. The present findings may aid in understanding the biological significance of this enzyme.","PeriodicalId":94103,"journal":{"name":"Journal of physical chemistry & biophysics","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2016-02-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of physical chemistry & biophysics","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.4172/2161-0398.1000206","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 1
Abstract
Fumarase enzyme is known to catalyse the stereo specific inter conversion of fumarate to L-malate which is a part of the Krebs cycle. Despite the biological significance and importance of this enzyme, the reaction mechanism of fumarase is not completely understood or known. In this context an experiment on molecular dynamics simulation was carried out for at least 10 nanoseconds molecular dynamics simulation run using Nano Scale Molecular Dynamics program implemented in Discovery Studio 4.0. The trajectory analysis of various energy parameters revealed the thermo dynamical stability of the enzyme. The present findings may aid in understanding the biological significance of this enzyme.
已知富马酸酶催化富马酸酯到l -苹果酸酯的立体特异性相互转化，这是克雷布斯循环的一部分。尽管这种酶具有生物学意义和重要性，但其反应机制尚不完全清楚。在此背景下，利用Discovery Studio 4.0中实现的纳米尺度分子动力学程序进行了至少10纳秒的分子动力学模拟实验。各种能量参数的轨迹分析揭示了酶的热力学稳定性。目前的发现可能有助于理解这种酶的生物学意义。
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