Show simple item record  

dc.contributor.authorDaniel, Roy M.
dc.contributor.authorPeterson, Michelle E.
dc.contributor.authorDanson, Michael J.
dc.contributor.authorPrice, Nicholas C.
dc.contributor.authorKelly, Sharon M.
dc.contributor.authorMonk, Colin R.
dc.contributor.authorWeinberg, Cristina S.
dc.contributor.authorOudshoorn, Matthew Leslie
dc.contributor.authorLee, Charles Kai-Wu
dc.date.accessioned2010-02-08T20:00:44Z
dc.date.available2010-02-08T20:00:44Z
dc.date.issued2010
dc.identifier.citationDaniel, Roy M., Peterson, M. E., Danson, M. J., Price, N. C., Kelly, S. M., Monk, C. R., Weinberg, C. S., Oudshoorn, M., Lee, C. K. (2010). The molecular basis of the effect of temperature on enzyme activity. Biochemical Journal, 425(2), 353-360.en
dc.identifier.urihttps://hdl.handle.net/10289/3552
dc.description.abstractExperimental data show that the effect of temperature on enzymes cannot be adequately explained in terms of a two-state model based on increases in activity and denaturation. The Equilibrium Model provides a quantitative explanation of enzyme thermal behaviour under reaction conditions by introducing an inactive (but not denatured) intermediate in rapid equilibrium with the active form. The temperature midpoint (Teq) of the rapid equilibration between the two forms is related to the growth temperature of the organism, and the enthalpy of the equilibrium (ΔHeq) to its ability to function over various temperature ranges. In the present study, we show that the difference between the active and inactive forms is at the enzyme active site. The results reveal an apparently universal mechanism, independent of enzyme reaction or structure, based at or near the active site, by which enzymes lose activity as temperature rises, as opposed to denaturation which is global. Results show that activity losses below Teq may lead to significant errors in the determination of ΔG*cat made on the basis of the twostate (‘Classical’) model, and the measured kcat will then not be a true indication of an enzyme’s catalytic power. Overall, the results provide a molecular rationale for observations that the active site tends to be more flexible than the enzyme as a whole, and that activity losses precede denaturation, and provide a general explanation in molecular terms for the effect of temperature on enzyme activity.en
dc.format.mimetypeapplication/pdf
dc.language.isoen
dc.publisherPortland Press Ltden_NZ
dc.relation.urihttp://www.biochemj.org/bj/default.htm
dc.rightsThis is an author's accepted version of an article published in Biochemical Journal. The final version of record is available at http://www.biochemj.org/bj/default.htm.
dc.subjectadaptationen
dc.subjectenzymeen
dc.subjectEquilibrium Modelen
dc.subjectevolutionen
dc.subjectkineticsen
dc.subjecttemperatureen
dc.titleThe molecular basis of the effect of temperature on enzyme activityen
dc.typeJournal Articleen
dc.identifier.doi10.1042/BJ20091254en
dc.relation.isPartOfBiochemical Journalen_NZ
pubs.begin-page353en_NZ
pubs.elements-id34691
pubs.end-page360en_NZ
pubs.issue2en_NZ
pubs.volume425en_NZ


Files in this item

This item appears in the following Collection(s)

Show simple item record