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dc.contributor.authorDaniel, Roy M.
dc.contributor.authorDanson, Michael J.
dc.date.accessioned2013-07-09T23:18:47Z
dc.date.available2013-07-09T23:18:47Z
dc.date.copyright2013-06
dc.date.issued2013
dc.identifier.citationDaniel, R. M., Danson, M. J. (2013). Temperature and the catalytic activity of enzymes: a fresh understanding. FEBS Letters, published online 27 June 2013.en_NZ
dc.identifier.urihttps://hdl.handle.net/10289/7764
dc.description.abstractThe 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.en_NZ
dc.language.isoenen_NZ
dc.publisherElsevieren_NZ
dc.relation.ispartofFEBS Letters
dc.relation.urihttp://www.sciencedirect.com/science/article/pii/S0014579313004857en_NZ
dc.subjectenzymesen_NZ
dc.subjecttemperatureen_NZ
dc.subjectcatalytic activityen_NZ
dc.subjectequilibrium modelen_NZ
dc.titleTemperature and the catalytic activity of enzymes: A fresh understandingen_NZ
dc.typeJournal Articleen_NZ
dc.identifier.doi10.1016/j.febslet.2013.06.027en_NZ
dc.relation.isPartOfFEBS Lettersen_NZ
pubs.begin-page2738en_NZ
pubs.elements-id38910
pubs.end-page2743en_NZ
pubs.issue17en_NZ
pubs.volume587en_NZ


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