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Originally published In Press as doi:10.1074/jbc.M212508200 on January 2, 2003

J. Biol. Chem., Vol. 278, Issue 10, 7891-7896, March 7, 2003
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Activity-Stability Relationships in Extremophilic Enzymes*

Salvino D'Amico, Jean-Claude Marx, Charles Gerday, and Georges FellerDagger

From the Laboratory of Biochemistry, University of Liège, Institute of Chemistry B6, B-4000 Liège-Sart Tilman, Belgium

Psychrophilic, mesophilic, and thermophilic alpha -amylases have been studied as regards their conformational stability, heat inactivation, irreversible unfolding, activation parameters of the reaction, properties of the enzyme in complex with a transition state analog, and structural permeability. These data allowed us to propose an energy landscape for a family of extremophilic enzymes based on the folding funnel model, integrating the main differences in conformational energy, cooperativity of protein unfolding, and temperature dependence of the activity. In particular, the shape of the funnel bottom, which depicts the stability of the native state ensemble, also accounts for the thermodynamic parameters of activation that characterize these extremophilic enzymes, therefore providing a rational basis for stability-activity relationships in protein adaptation to extreme temperatures.

* This work was supported by the European Union (Grant CT970131), the Région Wallonne (Grants Bioval 981/3860, Bioval 981/3848, Initiative 114705), the FNRS Belgium (Grant 2.4515.00), and the Institut Polaire Français.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 32-4-366-33-43; Fax: 32-4-366-33-64; E-mail: gfeller@ulg.ac.be.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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