Temperature adaptation of enzymes: Lessons from laboratory evolution

Abstract

This chapter outlines the evolutionary protein design methods that are used to help uncover the molecular basis for temperature adaptation in enzymes. The chapter explains how temperature affects protein stability and enzyme activity. The chapter also discusses some of the results of comparative studies of enzymes isolated from the organisms adapted to different temperatures. The chapter reveals small number of studies on natural thermophilic proteins that has identified various thermodynamic strategies for stabilization. Laboratory evolution makes it possible to ask, for example, whether proteins have adopted these different strategies by chance, or whether certain protein architectures favor specific thermodynamic mechanisms. It will also be possible to determine how other selective pressures, such as the requirement for efficient low temperature activity, influence stabilization mechanisms. Directed evolution can also be used to probe the boundaries of protein function, for example, the role of protein stability in setting the upper temperature limits for life. The combination of directed evolution with high resolution structural studies and detailed characterization of dynamics promises to provide insights into the molecular basis of stability and catalysis.

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