title: Approaches for deciphering the structural basis of low temperature enzyme activity.
abstract: An increasing number of enzymes active at low temperature are being studied to help determine the structural features important for cold-activity. This review examines the diversity of prokaryotic cold-active enzymes and the features proposed to account for low temperature activity. We then consider the difficulty of identifying the key structural features needed for cold-activity and the need to compare enzymes having different temperature optima from phylogenetically related organisms to determine features responsible for low temperature activity. In addition to studying naturally occurring enzymes, directed evolution experiments are discussed as methods for examining the proposed mechanisms influencing the thermal dependence of activity.
authors.affiliation: Department of Biochemistry and Molecular Biology, Pennsylvania State University, 16802, University Park, PA, USA. pps3@psu.edu
authors.forename: P P
authors.initials: PP
authors.lastname: Sheridan
authors.forename: N
authors.initials: N
authors.lastname: Panasik
authors.forename: J M
authors.initials: JM
authors.lastname: Coombs
authors.forename: J E
authors.initials: JE
authors.lastname: Brenchley
mesh_terms: D001419:Bacteria / Q000201:enzymology; D003080:Cold Temperature; D018360:Crystallography, X-Ray; D019020:Directed Molecular Evolution; D004795:Enzyme Stability; D004798:Enzymes / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D010802:Phylogeny; D011487:Protein Conformation; D015202:Protein Engineering; D000516:alpha-Amylases / Q000737:chemistry
chemical_list: D004798:Enzymes; D000516:alpha-Amylases