Research Commons
      • Browse 
        • Communities & Collections
        • Titles
        • Authors
        • By Issue Date
        • Subjects
        • Types
        • Series
      • Help 
        • About
        • Collection Policy
        • OA Mandate Guidelines
        • Guidelines FAQ
        • Contact Us
      • My Account 
        • Sign In
        • Register
      View Item 
      •   Research Commons
      • University of Waikato Research
      • Science and Engineering
      • Science and Engineering Papers
      • View Item
      •   Research Commons
      • University of Waikato Research
      • Science and Engineering
      • Science and Engineering Papers
      • View Item
      JavaScript is disabled for your browser. Some features of this site may not work without it.

      Eurythermalism and the temperature dependence of enzyme activity

      Lee, Charles Kai-Wu; Daniel, Roy M.; Shepherd, Charis; Saul, David; Cary, S. Craig; Danson, Michael J.; Eisenthal, Robert; Peterson, Michelle E.
      DOI
       10.1096/fj.06-7265com
      Find in your library  
      Citation
      Export citation
      Lee, C.K., Daniel, R.M., Shepherd, C., Saul, D., Cary, S.C., Danson, M.J., Eisenthal, R. & Peterson, M.E. (2007). Eurythermalism and the temperature dependence of enzyme activity. The FASEB Journal, 21, 1934-1941.
      Permanent Research Commons link: https://hdl.handle.net/10289/4368
      Abstract
      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 ΔG‡cat and ΔG‡inact but also by two new intrinsic parameters, ΔHeq and Teq, 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 Teq is a better predictor of growth temperature than enzyme stability (ΔG‡inact). As expected from the Equilibrium Model, ΔHeq 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, ΔHeq and Teq, are intrinsic and necessary parameters for characterizing the thermal properties of enzymes and their temperature adaptation and evolution.
      Date
      2007
      Type
      Journal Article
      Publisher
      Federation of American Societies for Experimental Biology
      Collections
      • Science and Engineering Papers [3143]
      Show full item record  

      Usage

       
       
       

      Usage Statistics

      For this itemFor all of Research Commons

      The University of Waikato - Te Whare Wānanga o WaikatoFeedback and RequestsCopyright and Legal Statement