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Author(s): D'Amico S; Marx JC; Gerday C; Feller G
Title: Activity-stability relationships in extremophilic enzymes
Source: JOURNAL OF BIOLOGICAL CHEMISTRY 278 (10): 7891-7896
Date: 2003 MAR 7
Document Type: Journal : Article
DOI:
Language: English
Comment:
Address: Univ Liege, Biochem Lab, Inst Chem B6, B-4000 Liege, Belgium.
Reprint: Feller, G, Univ Liege, Biochem Lab, Inst Chem B6, B-4000 Liege,
Belgium. E-mail:
Abstract: 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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