[en] Psychrophilic microorganisms, hosts of permanently cold habitats, produce enzymes which are adapted to work at low temperatures. When compared to their mesophilic counterparts, these enzymes display a higher catalytic efficiency over a temperature range of roughly 0-30 degrees C and a high thermosensitivity. The molecular characteristics of cold enzymes originating from Antarctic bacteria have been approached through protein modelling and X-ray crystallography. The deduced three-dimensional structures of cold alpha-amylase, beta-lactamase, lipase and subtilisin have been compared to their mesophilic homologs. It appears that the molecular adaptation resides in a weakening of the intramolecular interactions, and in some cases in an increase of the interaction with the solvent, leading to more flexible molecular edifices capable of performing catalysis at a lower energy cost.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Gerday, Charles ; Université de Liège - ULiège > Services généraux (Faculté des sciences) > Relations académiques et scientifiques (Sciences)
Aittaleb, Mohamed
Arpigny, Jean Louis
Baise, Etienne ; Université de Liège - ULiège > Département des sciences de la vie > Macromolécules biologiques
Chessa, Jean-Pierre
Garsoux, Geneviève
Petrescu, Ioan
Feller, Georges ; Université de Liège - ULiège > Département des sciences de la vie > Labo de biochimie
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