Reference : Activity-stability relationships in extremophilic enzymes
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Activity-stability relationships in extremophilic enzymes
D'Amico, Salvino [Université de Liège - ULiège > > GIGA-Research >]
Marx, J. C. [> > > >]
Gerday, Charles mailto [Université de Liège - ULiège > Services généraux (Faculté des sciences) > Relations académiques et scientifiques (Sciences) >]
Feller, Georges mailto [Université de Liège - ULiège > Département des sciences de la vie > Labo de biochimie >]
Journal of Biological Chemistry
Amer Soc Biochemistry Molecular Biology Inc
Yes (verified by ORBi)
[en] 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.

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