A new understanding of how temperature affects the catalytic activity of enzymes

R M Daniel, Michael J Danson

Research output: Contribution to journalArticle

63 Citations (Scopus)

Abstract

The two established thermal properties of enzymes are their activation energy and their thermal stability, but experimental data do not match the expectations of these two properties. The recently proposed Equilibrium Model (EM) 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. It was formulated as a mathematical model, and fits the known experimental data. Importantly, the EM gives rise to a number of new insights into the molecular basis of the temperature control of enzymes and their environmental adaptation and evolution, it is consistent with active site properties, and it has fundamental implications for enzyme engineering and other areas of biotechnology.
Original languageEnglish
Pages (from-to)584-591
Number of pages8
JournalTrends in Biochemical Sciences
Volume35
Issue number10
DOIs
Publication statusPublished - Oct 2010

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Catalyst activity
Hot Temperature
Temperature
Enzymes
Enzyme Activation
Biotechnology
Catalytic Domain
Theoretical Models
Temperature control
Thermodynamic stability
Thermodynamic properties
Activation energy
Mathematical models

Cite this

A new understanding of how temperature affects the catalytic activity of enzymes. / Daniel, R M; Danson, Michael J.

In: Trends in Biochemical Sciences, Vol. 35, No. 10, 10.2010, p. 584-591.

Research output: Contribution to journalArticle

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