New parameters controlling the effect of temperature on enzyme activity

Arising from careful measurements of the thermal behaviour of enzymes, a new model, the Equilibrium Model, has been developed to explain more fully the effects of temperature on enzymes. The model describes the effect of temperature on enzyme activity in terms of a rapidly reversible active-inactive...

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Bibliographic Details
Published inBiochemical Society transactions Vol. 35; no. Pt 6; p. 1543
Main Authors Daniel, R M, Danson, M J, Eisenthal, R, Lee, C K, Peterson, M E
Format Journal Article
LanguageEnglish
Published England 01.12.2007
Subjects
Enzyme Activation
Enzymes - chemistry
Enzymes - metabolism
Models, Chemical
Protein Engineering
Temperature
Thermodynamics
Time Factors
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Summary:Arising from careful measurements of the thermal behaviour of enzymes, a new model, the Equilibrium Model, has been developed to explain more fully the effects of temperature on enzymes. The model describes the effect of temperature on enzyme activity in terms of a rapidly reversible active-inactive (but not denatured) transition, revealing an additional and reversible mechanism for enzyme activity loss in addition to irreversible thermal inactivation at high temperatures. Two new thermal parameters, T(eq) and DeltaH(eq), describe the active-inactive transition, and enable a complete description of the effect of temperature on enzyme activity. We describe here the Model and its fit to experimental data, methods for the determination of the Equilibrium Model parameters, and the implications of the Model for the environmental adaptation and evolution of enzymes, and for biotechnology.
ISSN:0300-5127
DOI:10.1042/BST0351543