C. Gerday et al., PSYCHROPHILIC ENZYMES - A THERMODYNAMIC CHALLENGE, Biochimica et biophysica acta. Protein structure and molecular enzymology, 1342(2), 1997, pp. 119-131
Psychrophilic microorganisms, hosts of permanently cold habitats, prod
uce enzymes which are adapted to work at low temperatures. When compar
ed to their mesophilic counterparts, these enzymes display a higher ca
talytic efficiency over a temperature range of roughly 0-30 degrees C
and a high thermosensitivity. The molecular characteristics of cold en
zymes originating from Antarctic bacteria have been approached through
protein modelling and X-ray crystallography. The deduced three-dimens
ional structures of cold alpha-amylase, beta-lactamase, lipase and sub
tilisin have been compared to their mesophilic homologs. It appears th
at the molecular adaptation resides in a weakening of the intramolecul
ar interactions, and in some cases in an increase of the interaction w
ith the solvent, leading to more flexible molecular edifices capable o
f performing catalysis at a lower energy cost. (C) 1997 Elsevier Scien
ce B.V.