The molecular basis of the effect of temperature on enzyme activity

R M Daniel, M E Peterson, Michael J Danson, N C Price, S M Kelly, C R Monk, C S Weinberg, M L Oudshoorn, C K Lee

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Abstract

Experimental 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 (T-eq) of the rapid equilibration between the two forms is related to the growth temperature of the organism, and the enthalpy of the equilibrium (Delta H-eq) 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 T-eq may lead to significant errors in the determination of Delta G(cat)* made on the basis of the two-state ('Classical') model, and the measured k(cat) 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.
Original languageEnglish
Pages (from-to)353-360
Number of pages8
JournalBiochemical Journal
Volume425
Issue number2
DOIs
Publication statusPublished - 15 Jan 2010

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Enzyme activity
Denaturation
Temperature
Enzymes
Catalytic Domain
Growth temperature
Aptitude
Enthalpy
Cats
Hot Temperature
Growth

Cite this

Daniel, R. M., Peterson, M. E., Danson, M. J., Price, N. C., Kelly, S. M., Monk, C. R., ... Lee, C. K. (2010). The molecular basis of the effect of temperature on enzyme activity. Biochemical Journal, 425(2), 353-360. https://doi.org/10.1042/bj20091254

The molecular basis of the effect of temperature on enzyme activity. / Daniel, R M; Peterson, M E; Danson, Michael J; Price, N C; Kelly, S M; Monk, C R; Weinberg, C S; Oudshoorn, M L; Lee, C K.

In: Biochemical Journal, Vol. 425, No. 2, 15.01.2010, p. 353-360.

Research output: Contribution to journalArticle

Daniel, RM, Peterson, ME, Danson, MJ, Price, NC, Kelly, SM, Monk, CR, Weinberg, CS, Oudshoorn, ML & Lee, CK 2010, 'The molecular basis of the effect of temperature on enzyme activity', Biochemical Journal, vol. 425, no. 2, pp. 353-360. https://doi.org/10.1042/bj20091254
Daniel RM, Peterson ME, Danson MJ, Price NC, Kelly SM, Monk CR et al. The molecular basis of the effect of temperature on enzyme activity. Biochemical Journal. 2010 Jan 15;425(2):353-360. https://doi.org/10.1042/bj20091254
Daniel, R M ; Peterson, M E ; Danson, Michael J ; Price, N C ; Kelly, S M ; Monk, C R ; Weinberg, C S ; Oudshoorn, M L ; Lee, C K. / The molecular basis of the effect of temperature on enzyme activity. In: Biochemical Journal. 2010 ; Vol. 425, No. 2. pp. 353-360.
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