A new intrinsic thermal parameter for enzymes reveals true temperature optima

M E Peterson, R Eisenthal, M J Danson, A Spence, R M Daniel

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Abstract

Two established thermal properties of enzymes are the Arrhenius activation energy and thermal stability. Arising from anomalies found in the variation of enzyme activity with temperature, a comparison has been made of experimental data for the activity and stability properties of five different enzymes with theoretical models. The results provide evidence for a new and fundamental third thermal parameter of enzymes, T-eq, arising from a subsecond timescale-reversible temperature-dependent equilibrium between the active enzyme and an inactive (or less active) form. Thus, at temperatures above its optimum, the decrease in enzyme activity arising from the temperature-dependent shift in this equilibrium is up to two orders of magnitude greater than what occurs through thermal denaturation. This parameter has important implications for our understanding of the connection between catalytic activity and thermostability and of the effect of temperature on enzyme reactions within the cell. Unlike the Arrhenius activation energy, which is unaffected by the source ("evolved") temperature of the enzyme, and enzyme stability, which is not necessarily related to activity, T-eq is central to the physiological adaptation of an enzyme to its environmental temperature and links the molecular, physiological, and environmental aspects of the adaptation of life to temperature in a way that has not been described previously. We may therefore expect the effect of evolution on T-eq with respect to enzyme temperature/activity effects to be more important than on thermal stability. T-eq is also an important parameter to consider when engineering enzymes to modify their thermal properties by both rational design and by directed enzyme evolution.
Original languageEnglish
Pages (from-to)20717-20722
Number of pages6
JournalJournal of Biological Chemistry
Volume279
Issue number20
DOIs
Publication statusPublished - May 2004

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Hot Temperature
Temperature
Enzymes
Thermodynamic properties
Enzyme activity
Thermodynamic stability
Activation energy
Physiological Adaptation
Enzyme Stability
Denaturation
Enzyme Activation
Catalyst activity
Theoretical Models

Cite this

A new intrinsic thermal parameter for enzymes reveals true temperature optima. / Peterson, M E; Eisenthal, R; Danson, M J; Spence, A; Daniel, R M.

In: Journal of Biological Chemistry, Vol. 279, No. 20, 05.2004, p. 20717-20722.

Research output: Contribution to journalArticle

Peterson, M E ; Eisenthal, R ; Danson, M J ; Spence, A ; Daniel, R M. / A new intrinsic thermal parameter for enzymes reveals true temperature optima. In: Journal of Biological Chemistry. 2004 ; Vol. 279, No. 20. pp. 20717-20722.
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