Temperature and the catalytic activity of enzymes

a fresh understanding

R.M. Daniel, M.J. Danson

Research output: Contribution to journalArticle

38 Citations (Scopus)

Abstract

The discovery of an additional step in the progression of an enzyme from the active to inactive state under the influence of temperature has led to a better match with experimental data for all enzymes that follow Michaelis-Menten kinetics, and to an increased understanding of the process. The new model of the process, the Equilibrium Model, describes an additional mechanism by which temperature affects the activity of enzymes, with implications for ecological, metabolic, structural, and applied studies of enzymes.
Original languageEnglish
Pages (from-to)2738-2743
JournalFEBS Letters
Volume17
Issue number2
Early online date17 Jun 2013
DOIs
Publication statusPublished - 2013

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Catalyst activity
Temperature
Enzymes
Kinetics

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Temperature and the catalytic activity of enzymes : a fresh understanding. / Daniel, R.M.; Danson, M.J.

In: FEBS Letters, Vol. 17, No. 2, 2013, p. 2738-2743.

Research output: Contribution to journalArticle

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