Extremophiles

, Volume 4, Issue 2, pp 91–98

Halophilic adaptation of enzymes

  • D. Madern
  • C. Ebel
  • G. Zaccai
MINI-REVIEW

DOI: 10.1007/s007920050142

Cite this article as:
Madern, D., Ebel, C. & Zaccai, G. Extremophiles (2000) 4: 91. doi:10.1007/s007920050142

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 ArchaeaHalobacteriaStabilizationSolubilityProtein–solvent interactionsMalate dehydrogenase

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