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• W2080909101 endingPage "637" @default.
• W2080909101 startingPage "630" @default.
• W2080909101 abstract "Enzymes from thermophiles are poorly active at temperatures at which their mesophilic homologs exhibit high activity and attain corresponding active states at high temperatures. In this study, comparative molecular dynamics (MD) simulations, supplemented by normal mode analysis, have been performed on an enzyme Adenylosuccinate synthetase (AdSS) from E. coli (mesophilic) and P. horikoshii (thermophilic) systems to understand the effects of loop dynamics on thermal stability of AdSS. In mesophilic AdSS, both ligand binding and catalysis are facilitated through the coordinated movement of five loops on the protein. The simulation results suggest that thermophilic P. horikoshii preserves structure and catalytic function at high temperatures by using the movement of only a subset of loops (two out of five) for ligand binding and catalysis unlike its mesophilic counterpart in E. coli. The pre-arrangement of the catalytic residues in P. horikoshii is well-preserved and salt bridges remain stable at high temperature (363K). The simulations suggest a general mechanism (including pre-arrangement of catalytic residues, increased polar residue content, stable salt bridges, increased rigidity, and fewer loop movements) used by thermophilic enzymes to preserve structure and be catalytically active at elevated temperatures." @default.
• W2080909101 created "2016-06-24" @default.
• W2080909101 creator A5016668907 @default.
• W2080909101 creator A5024273182 @default.
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• W2080909101 date "2011-05-01" @default.
• W2080909101 modified "2023-10-12" @default.
• W2080909101 title "Role of loop dynamics in thermal stability of mesophilic and thermophilic adenylosuccinate synthetase: A molecular dynamics and normal mode analysis study" @default.
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• W2080909101 doi "https://doi.org/10.1016/j.bbapap.2011.03.012" @default.
• W2080909101 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21440684" @default.
• W2080909101 hasPublicationYear "2011" @default.
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