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Salt-dependent studies of NADP-dependent isocitrate dehydrogenase from the halophilic archaeon Haloferax volcanii

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Abstract

The salt-dependent stability of recombinant dimeric isocitrate dehydrogenase [ICDH; isocitrate: NADP oxidoreductase (decarboxylating), EC 1.1.1.42] from the halophilic archaeon Haloferax volcanii (Hv) was investigated in various conditions. Hv ICDH dissociation/deactivation was measured to probe the respective effect of anions and cations on stability. Surprisingly, enzyme stability was found to be mainly sensitive to cations and very little (or not) sensitive to anions. Divalent cations induced a strong shift of the active/inactive transition towards low salt concentration. A high resistance of Hv ICDH to chemical denaturation was also found. The data were analysed and are discussed in the framework of the solvation stability model for halophilic proteins.

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Acknowledgements

Part of this work was financially supported by CICYT (Spain; project number PB98-0969) and by the Programme Interdepartemental GEOMEX du CNRS.

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Authors and Affiliations

  1. Laboratoire de Biophysique Moléculaire, Institut de Biologie Structurale CEA-CNRS-UJF, 41 Rue Jules Horowitz, 38042, Grenoble, France

    Dominique Madern & Giuseppe Zaccai

  2. División de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad de Alicante, Spain

    Mónica Camacho, Adoración Rodríguez-Arnedo & María-José Bonete

Authors
  1. Dominique Madern
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  2. Mónica Camacho
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  3. Adoración Rodríguez-Arnedo
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  4. María-José Bonete
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  5. Giuseppe Zaccai
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Corresponding author

Correspondence to Dominique Madern.

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Communicated by W.D. Grant

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Madern, D., Camacho, M., Rodríguez-Arnedo, A. et al. Salt-dependent studies of NADP-dependent isocitrate dehydrogenase from the halophilic archaeon Haloferax volcanii . Extremophiles 8, 377–384 (2004). https://doi.org/10.1007/s00792-004-0398-z

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  • DOI: https://doi.org/10.1007/s00792-004-0398-z

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