PubMed · 2004 · 36 citations · 64 references
Life SciencesBiochemistryMolecular BiologyBiocatalysisEnzymologyStructural BiologyEnzyme FunctionEnzyme StabilityEnzyme StructureProtein StructureStructural EnzymologyThermostable EnzymesCold-adapted EnzymesEnzyme Adaptation To ColdEnzymesProtein Thermal AdaptationProtein Thermal StabilityTemperature Effects On Enzyme ActivityThermal StabilityThermostability Mechanisms
Studies on psychrophilic enzymes to determine the structural features important for cold-activity have attracted increased attention in the last few years. This enhanced interest is due to the attractive properties of such proteins, i.e. a high specific activity and a low thermal stability, and thus, these enzymes constitute a tremendous potential for fundamental research and biotechnological applications. This review examines the impact of low temperatures on life, the diversity of adaptation to counteract these effects and gives an overview of the features proposed to account for low thermal stability and cold-activity, following the chronological order of the catalytic cycle phases. Moreover, we present an overview of recent techniques used in the analysis of the flexibility of a protein structure which is an important concept in cold-adaptation; an overview of biotechnological potential of psychrophilic enzymes and finally, a few frequently asked questions about cold-adaptation and their possible answers.
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Directed evolution of a thermostable esterase
Lori Giver, Anne Gershenson, Per‐Ola Freskgård et al. · Proceedings of the National Academy of Sciences · 1998 · 530 citations
Activity-Stability Relationships in Extremophilic Enzymes
Salvino D’Amico, Jean‐Claude Marx, Charles Gerday et al. · Journal of Biological Chemistry · 2003 · 457 citations · Full text
Peter A. Fields, George N. Somero · Proceedings of the National Academy of Sciences · 1998 · 412 citations · Full text
Life Sciences, Biochemistry, Biology +13