Psychrophilic enzymes: insights into cold adaptation and catalysis from the first high resolution crystal structures

Abstract

A number of reviews have already addressed the diversity, physiology, enzymology, ecology, and methodology for isolation, purification and characterization of extremophile proteins, including those from psychrophilic organisms.1–5 Enzymes from organisms adapted to cold environments function optimally at low temperatures, and have therefore considerable potential in biotechnological applications. Psychrophilic enzymes are characterized by a high catalytic efficiency at low temperature and an enhanced thermosensivity, these characteristics being proposed to be related to a higher flexibility of the corresponding three-dimensional (3D) structures when compared to that of their mesophilic and thermophilic counterparts.