Fundamentals of Cold-Adapted Enzymes

Catalysis by Dihydrofolate Reductase from the Psychropiezophile Moritella profunda

“…In general, the overall folded structures of psychrophilic, mesophilic and thermophilic homologues are similar, and residues involved in catalysis are generally conserved. [20,21] However, in cold-adapted enzymes, there are often fewer stabilising intramolecular bonds and weaker binding of stabilising ligands. [22][23][24] The reduction in the number of intermolecular interactions is also thought to increase the number of ground-state conformational substates in cold-adapted enzymes.…”

Biotechnological Applications of Cold‐Adapted Bacteria

“…Until now, more than 100 enzymes have been purified from prokaryotic organisms inhabiting permanently low-temperature environments: for example, cellulases, amylases, xylanases, DNA-ligases, proteases, pectinases, keratinases, lipases, esterases, catalases, peroxidases, alkaline phosphatases, lactamases, and phytases. Most of them can be consulted at http://www.ulg.ac.be/biochlab (Collins et al, 2008).…”

Backbone and side chain 1H, 15N and 13C assignments for a thiol-disulphide oxidoreductase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125

“…Their strategy of adaptation must include maintenance of membrane fluidity, efficient transcription and translation rates, as well as effective nutrient transport and cryoprotection. A further essential component of this adaptation is the maintenance of an efficient enzyme activity (Collins et al 2008;Feller and Gerday 2003). Indeed, enzymes produced by these organisms have been found to have successfully adapted to their environment and typically display high catalytic activity at low to moderate temperatures (Collins et al 2008;Feller and Gerday 2003).…”

“…Indeed, enzymes produced by these organisms have been found to have successfully adapted to their environment and typically display high catalytic activity at low to moderate temperatures (Collins et al 2008;Feller and Gerday 2003). As compared to their mesophilic and thermophilic homologs, their activity at low temperatures is in general much higher and their apparent optimal temperature is shifted towards lower temperatures while they are also typically characterized by a reduced thermal and chemical stability (Collins et al 2003(Collins et al , 2008. Furthermore, while being much less well studied than mesophilic and thermophilic enzymes, comparative crystal structure analyses indicate that cold adapted enzymes are characterized by subtle enzyme specific structural modifications, with, in particular, a reduction in the number and/or strength of stabilizing interactions being reported.…”

“…A further essential component of this adaptation is the maintenance of an efficient enzyme activity (Collins et al 2008;Feller and Gerday 2003). Indeed, enzymes produced by these organisms have been found to have successfully adapted to their environment and typically display high catalytic activity at low to moderate temperatures (Collins et al 2008;Feller and Gerday 2003). As compared to their mesophilic and thermophilic homologs, their activity at low temperatures is in general much higher and their apparent optimal temperature is shifted towards lower temperatures while they are also typically characterized by a reduced thermal and chemical stability (Collins et al 2003(Collins et al , 2008.…”