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Temperature and the catalytic activity of enzymes: A fresh understanding
Author(s) -
Daniel Roy M.,
Danson Michael J.
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.06.027
Subject(s) - enzyme , chemistry , kinetics , mechanism (biology) , enzyme kinetics , biochemistry , michaelis–menten kinetics , process (computing) , enzyme assay , thermodynamics , biophysics , biology , active site , computer science , philosophy , physics , operating system , quantum mechanics , epistemology
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.