Structure prediction and functional analyses of a thermostable lipase obtained from Shewanella putrefaciens
Structure prediction and functional analyses of a thermostable lipase obtained from Shewanella putrefaciens
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DOI：
10.1080/07391102.2016.1206837
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发表时间：
2017-01-01
影响因子：
4.4
通讯作者：
Wei, Dong-Qing
中科院分区：
文献类型：
--
作者：
Khan, Faez Iqbal;Nizami, Bilal;Wei, Dong-Qing
Previous experimental studies on thermostable lipase from Shewanella putrefaciens suggested the maximum activity at higher temperatures, but with little information on its conformational profile. In this study, the three-dimensional structure of lipase was predicted and a 60ns molecular dynamics (MD) simulation was carried out at temperatures ranging from 300 to 400K to better understand its thermostable nature at the molecular level. MD simulations were performed in order to predict the optimal activity of thermostable lipase. The results suggested strong conformational temperature dependence. The thermostable lipase maintained its bio-active conformation at 350K during the 60ns MD simulations.
