Reference : Psychrophilic Enzymes: Molecular Basis of Cold Adaptation
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Psychrophilic Enzymes: Molecular Basis of Cold Adaptation
Feller, Georges mailto [Université de Liège - ULiège > Département des sciences de la vie > Labo de biochimie >]
Gerday, Charles mailto [Université de Liège - ULiège > Services généraux (Faculté des sciences) > Relations académiques et scientifiques (Sciences) >]
Cellular and Molecular Life Sciences
Yes (verified by ORBi)
[en] Psychrophilic organisms have successfully colonized polar and alpine regions and are able to grow efficiently at sub-zero temperatures. At the enzymatic level, such organisms have to cope with the reduction of chemical reaction rates induced by low temperatures in order to maintain adequate metabolic fluxes. Thermal compensation in cold-adapted enzymes is reached through improved turnover number and catalytic efficiency. This optimization of the catalytic parameters can originate from a highly flexible structure which provides enhanced abilities to undergo conformational changes during catalysis. Thermal instability of cold-adapted enzymes is therefore regarded as a consequence of their conformational flexibility. A survey of the psychrophilic enzymes studied so far reveals only minor alterations of the primary structure when compared to mesophilic or thermophilic homologues. However, all known structural factors and weak interactions involved in protein stability are either reduced in number or modified in order to increase their flexibility.

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