TY - JOUR
T1 - Temperature and the catalytic activity of enzymes
T2 - a fresh understanding
AU - Daniel, R.M.
AU - Danson, M.J.
PY - 2013
Y1 - 2013
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84879825865&partnerID=8YFLogxK
UR - http://dx.doi.org/10.1016/j.febslet.2013.06.027
U2 - 10.1016/j.febslet.2013.06.027
DO - 10.1016/j.febslet.2013.06.027
M3 - Article
SN - 0014-5793
VL - 17
SP - 2738
EP - 2743
JO - FEBS Letters
JF - FEBS Letters
IS - 2
ER -