Cold-adapted enzymes

Annu Rev Biochem. 2006;75:403-33. doi: 10.1146/annurev.biochem.75.103004.142723.

Abstract

By far the largest proportion of the Earth's biosphere is comprised of organisms that thrive in cold environments (psychrophiles). Their ability to proliferate in the cold is predicated on a capacity to synthesize cold-adapted enzymes. These enzymes have evolved a range of structural features that confer a high level of flexibility compared to thermostable homologs. High flexibility, particularly around the active site, is translated into low-activation enthalpy, low-substrate affinity, and high specific activity at low temperatures. High flexibility is also accompanied by a trade-off in stability, resulting in heat lability and, in the few cases studied, cold lability. This review addresses the structure, function, and stability of cold-adapted enzymes, highlighting the challenges for immediate and future consideration. Because of the unique properties of cold-adapted enzymes, they are not only an important focus in extremophile biology, but also represent a valuable model for fundamental research into protein folding and catalysis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adaptation, Biological*
  • Animals
  • Cold Temperature*
  • Enzyme Stability
  • Enzymes / chemistry
  • Enzymes / metabolism*
  • Mathematics
  • Protein Conformation
  • Protein Folding
  • Static Electricity
  • Structure-Activity Relationship
  • Surface Properties
  • Thermodynamics

Substances

  • Enzymes