Activity-stability relationships in extremophilic enzymes
摘要：
Psychrophilic, mesophilic, and thermophilic α-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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关键词：
Pseudoalteromonas Escherichia coli Recombinant Proteins Calorimetry, Differential Scanning Spectrometry, Fluorescence Protein Conformation Protein Denaturation alpha-Amylases Hot Temperature Structure-Activity Relationship
DOI：
10.1074/jbc.M212508200
被引量：
年份：
2003
Elsevier
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