dc.contributor.author | Daniel, Roy M. | |
dc.contributor.author | Danson, Michael J. | |
dc.date.accessioned | 2013-07-09T23:18:47Z | |
dc.date.available | 2013-07-09T23:18:47Z | |
dc.date.copyright | 2013-06 | |
dc.date.issued | 2013 | |
dc.identifier.citation | Daniel, 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.uri | https://hdl.handle.net/10289/7764 | |
dc.description.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. | en_NZ |
dc.language.iso | en | en_NZ |
dc.publisher | Elsevier | en_NZ |
dc.relation.ispartof | FEBS Letters | |
dc.relation.uri | http://www.sciencedirect.com/science/article/pii/S0014579313004857 | en_NZ |
dc.subject | enzymes | en_NZ |
dc.subject | temperature | en_NZ |
dc.subject | catalytic activity | en_NZ |
dc.subject | equilibrium model | en_NZ |
dc.title | Temperature and the catalytic activity of enzymes: A fresh understanding | en_NZ |
dc.type | Journal Article | en_NZ |
dc.identifier.doi | 10.1016/j.febslet.2013.06.027 | en_NZ |
dc.relation.isPartOf | FEBS Letters | en_NZ |
pubs.begin-page | 2738 | en_NZ |
pubs.elements-id | 38910 | |
pubs.end-page | 2743 | en_NZ |
pubs.issue | 17 | en_NZ |
pubs.volume | 587 | en_NZ |