Journal
FEBS LETTERS
Volume 587, Issue 17, Pages 2738-2743Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2013.06.027
Keywords
Enzyme; Temperature; Catalytic activity; Equilibrium Model
Funding
- Royal Society of New Zealand Marsden Fund [UOW0501]
- UK Biotechnology and Biological Sciences Research Council
- Royal Society
- US Air Force Office of Scientific Research. Professor Robert Eisenthal
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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. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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