Extremophiles

, Volume 4, Issue 2, pp 91–98

Halophilic adaptation of enzymes

  • D. Madern
  • C. Ebel
  • G. Zaccai
MINI-REVIEW
  • 1.5k Downloads

Abstract

It is now clear that the understanding of halophilic adaptation at a molecular level requires a strategy of complementary experiments, combining molecular biology, biochemistry, and cellular approaches with physical chemistry and thermodynamics. In this review, after a discussion of the definition and composition of halophilic enzymes, the effects of salt on their activity, solubility, and stability are reviewed. We then describe how thermodynamic observations, such as parameters pertaining to solvent–protein interactions or enzyme-unfolding kinetics, depend strongly on solvent composition and reveal the important role played by water and ion binding to halophilic proteins. The three high-resolution crystal structures now available for halophilic proteins are analyzed in terms of haloadaptation, and finally cellular response to salt stress is discussed briefly.

Key words Halophilic Archaea Halobacteria Stabilization Solubility Protein–solvent interactions Malate dehydrogenase 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

Copyright information

© Springer-Verlag Tokyo 2000

Authors and Affiliations

  • D. Madern
    • 1
  • C. Ebel
    • 1
  • G. Zaccai
    • 1
  1. 1.Institut de Biologie Structurale CEA-CNRS, 41 rue Jules Horowitz, 38027 Grenoble Cedex 1, France Tel. +33.4.76.88.95.73; Fax +33.4.76.88.54.94, e-mail: zaccai@ibs.frFR

Personalised recommendations