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• W1817490889 endingPage "2130" @default.
• W1817490889 startingPage "2122" @default.
• W1817490889 abstract "Abstract In most lipases, a mobile lid covers the substrate binding site. In this closed structure, the lipase is assumed to be inactive. Upon activation of the lipase by contact with a hydrophobic solvent or at a hydrophobic interface, the lid opens. In its open structure, the substrate binding site is accessible and the lipase is active. The molecular mechanism of this interfacial activation was studied for three lipases (from Candida rugosa , Rhizomucor miehei , and Thermomyces lanuginosa ) by multiple molecular dynamics simulations for 25 ns without applying restraints or external forces. As initial structures of the simulations, the closed and open structures of the lipases were used. Both the closed and the open structure were simulated in water and in an organic solvent, toluene. In simulations of the closed lipases in water, no conformational transition was observed. However, in three independent simulations of the closed lipases in toluene the lid gradually opened. Thus, pathways of the conformational transitions were investigated and possible kinetic bottlenecks were suggested. The open structures in toluene were stable, but in water the lid of all three lipases moved towards the closed structure and partially unfolded. Thus, in all three lipases opening and closing was driven by the solvent and independent of a bound substrate molecule." @default.
• W1817490889 created "2016-06-24" @default.
• W1817490889 creator A5033762637 @default.
• W1817490889 creator A5062182560 @default.
• W1817490889 creator A5067406221 @default.
• W1817490889 date "2010-09-24" @default.
• W1817490889 modified "2023-10-16" @default.
• W1817490889 title "Solvent-induced lid opening in lipases: A molecular dynamics study" @default.
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• W1817490889 doi "https://doi.org/10.1002/pro.493" @default.
• W1817490889 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3005783" @default.
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