Eurythermalism and the temperature dependence of enzyme activity

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dc.contributor.authorLee, Charles Kai-Wu
dc.contributor.authorDaniel, Roy M.
dc.contributor.authorShepherd, Charis
dc.contributor.authorSaul, David
dc.contributor.authorCary, S. Craig
dc.contributor.authorDanson, Michael J.
dc.contributor.authorEisenthal, Robert
dc.contributor.authorPeterson, Michelle E.
dc.coverage.spatialUnited Statesen_NZ
dc.date.accessioned2010-08-19T00:50:18Z
dc.date.available2010-08-19T00:50:18Z
dc.date.issued2007
dc.description.abstractThe "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.en_NZ
dc.identifier.citationLee, 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.en_NZ
dc.identifier.doi10.1096/fj.06-7265comen_NZ
dc.identifier.urihttps://hdl.handle.net/10289/4368
dc.language.isoen
dc.publisherFederation of American Societies for Experimental Biologyen_NZ
dc.relation.isPartOfThe FASEB Journalen_NZ
dc.subjectenzyme temperature optimumen_NZ
dc.subjectEquilibrium Modelen_NZ
dc.subjectgrowth temperatureen_NZ
dc.subjectprotein stabilityen_NZ
dc.subjecttemperature adaptationen_NZ
dc.titleEurythermalism and the temperature dependence of enzyme activityen_NZ
dc.typeJournal Articleen_NZ
pubs.begin-page1934en_NZ
pubs.elements-id33137
pubs.end-page1941en_NZ
pubs.issue8en_NZ
pubs.volume21en_NZ
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