Eurythermalism and the temperature dependence of enzyme activity Charles K. Lee * , Roy M. Daniel * ,1 , Charis Shepherd † , David Saul † , S. Craig Cary * ,‡ , Michael J. Danson § , Robert Eisenthal || and Michelle E. Peterson * * Department of Biological Sciences, University of Waikato, Hamilton, New Zealand; † School of Biological Sciences, University of Auckland, Auckland, New Zealand; ‡ College of Marine and Earth Studies, University of Delaware, Lewis, Delaware, USA; § Centre for Extremophile Research, Department of Biology and Biochemistry, and || Department of Biology and Biochemistry, University of Bath, Bath, UK 1 Correspondence: Department of Biological Sciences, University of Waikato, Private Bag 3105, Hamilton 3240, New Zealand. E-mail: r.daniel@waikato.ac.nz The "Equilibrium Model" has provided new tools for describing and investigating enzyme thermal adaptation. It has been shown that the effect of temperature on enzyme activity is not only governed by Δ G ‡ cat and Δ G ‡ inact but also by two new intrinsic parameters, Δ H eq and T eq , which describe the enthalpy and midpoint, respectively, of a reversible equilibrium between active and inactive (but not denatured) forms of enzyme. Twenty-one enzymes from organisms with a wide range of growth temperatures were characterized using the Equilibrium Model. Statistical analysis indicates that T eq is a better predictor of growth temperature than enzyme stability (Δ G ‡ inact ). As expected from the Equilibrium Model, Δ H eq correlates with catalytic temperature tolerance of enzymes and thus can be declared the first intrinsic and quantitative measure of enzyme eurythermalism. Other findings shed light on the evolution of psychrophilic and thermophilic enzymes. The findings suggest that the description of the Equilibrium Model of the effect of temperature on enzyme activity applies to all enzymes regardless of their temperature origins and that its associated parameters, Δ H eq and T eq , are intrinsic and necessary parameters for characterizing the thermal properties of enzymes and their temperature adaptation and evolution.—Lee, C. K., Daniel, R. M., Shepherd, C., Saul, D., Cary, S. C., Danson, M. J., Eisenthal, R., Peterson, M. E. Eurythermalism and the temperature dependence of enzyme activity Key Words: enzyme temperature optimum • Equilibrium Model • growth temperature • protein stability • temperature adaptation
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Eurythermalism and the temperature dependence of enzyme activity
Lee, Charles K.; Daniel, Roy M.; Shepherd, Charis; Saul, David; Cary, S. Craig; Danson, Michael J.; Eisenthal, Robert; Peterson, Michelle E.
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, Volume 21 (8): 1934
Fed of American Socs for Experimental Biology – Jun 1, 2007
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