title: New understandings of thermostable and peizostable enzymes.
abstract: Recent large-scale studies illustrate the importance of electrostatic interactions near the surface of proteins as a major factor in enhancing thermal stability. Mutagenesis studies have also demonstrated the importance of optimized charge interactions on the surface of the protein, which can significantly augment enzyme thermal stability. Directed evolution studies show that increased stability may be obtained by different routes, which may not mimic those used by nature. Despite observations that some of the most thermotolerant organisms grow under conditions of high pressure, little effort has been made to understand the correlation between pressure and temperature stability. One recent study demonstrates that the active-site volume may be important in increasing pressure stability.
authors.affiliation: The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
authors.forename: Jason K
authors.initials: JK
authors.lastname: Yano
authors.forename: Thomas L
authors.initials: TL
authors.lastname: Poulos
mesh_terms: D018360:Crystallography, X-Ray; D030562:Databases, Protein; D019020:Directed Molecular Evolution / Q000639:trends; D004795:Enzyme Stability / Q000235:genetics*; D004798:Enzymes / Q000737:chemistry* / Q000235:genetics; D015698:Genomic Library; D006358:Hot Temperature; D008958:Models, Molecular; D016296:Mutagenesis / Q000235:genetics; D016297:Mutagenesis, Site-Directed / Q000235:genetics; D011312:Pressure; D011487:Protein Conformation; D015202:Protein Engineering
chemical_list: D004798:Enzymes