Psychrophilic Enzymes: Molecular Basis of Cold Adaptation

• Published in: Cellular and molecular life sciences : CMLS Vol. 53; no. 10; pp. 830 - 41
• Main Authors: Feller, Georges, Gerday, Charles
• Format: Journal Article Web Resource
• Language: English
• Published: Switzerland Birkhauser Verlag 01.10.1997; Birkhäuser-Verlag
• Subjects: Adaptation, Biological; Animals; Bacteria - enzymology; Bacteria - growth & development; Binding Sites; Biochemistry; Biochemistry, biophysics & molecular biology; Biochimie, biophysique & biologie moléculaire; biophysics; Catalysis; Cold Climate; Cold Temperature; Enzymes - chemistry; Enzymes - metabolism; Kinetics; Life sciences; molecular biology; Protein Conformation; Psychrobacter immobilis; Review; Sciences du vivant; Temperature; Thermodynamics
• ISSN: 1420-682X; 1420-9071; 1420-9071
• DOI: 10.1007/s000180050103

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.