Show simple item record  

dc.contributor.authorPeterson, Michelle E.
dc.contributor.authorEisenthal, Robert
dc.contributor.authorDanson, Michael J.
dc.contributor.authorSpence, Alastair
dc.contributor.authorDaniel, Roy M.
dc.date.accessioned2010-08-27T01:35:05Z
dc.date.available2010-08-27T01:35:05Z
dc.date.issued2004
dc.identifier.citationPeterson, M.E., Eisenthal, R., Danson, M.J., Spence, A. & Daniel, R.M. (2004). A new intrinsic thermal parameter for enzymes reveals true temperature optima. The Journal of Biological Chemistry, 279(20), 20717-20722.en_NZ
dc.identifier.urihttps://hdl.handle.net/10289/4446
dc.description.abstractTwo established thermal properties of enzymes are the Arrhenius activation energy and thermal stability. Arising from anomalies found in the variation of enzyme activity with temperature, a comparison has been made of experimental data for the activity and stability properties of five different enzymes with theoretical models. The results provide evidence for a new and fundamental third thermal parameter of enzymes, Teq, arising from a subsecond timescale-reversible temperature-dependent equilibrium between the active enzyme and an inactive (or less active) form. Thus, at temperatures above its optimum, the decrease in enzyme activity arising from the temperature-dependent shift in this equilibrium is up to two orders of magnitude greater than what occurs through thermal denaturation. This parameter has important implications for our understanding of the connection between catalytic activity and thermostability and of the effect of temperature on enzyme reactions within the cell. Unlike the Arrhenius activation energy, which is unaffected by the source (“evolved”) temperature of the enzyme, and enzyme stability, which is not necessarily related to activity, Teq is central to the physiological adaptation of an enzyme to its environmental temperature and links the molecular, physiological, and environmental aspects of the adaptation of life to temperature in a way that has not been described previously. We may therefore expect the effect of evolution on Teq with respect to enzyme temperature/activity effects to be more important than on thermal stability. Teq is also an important parameter to consider when engineering enzymes to modify their thermal properties by both rational design and by directed enzyme evolution.en_NZ
dc.format.mimetypeapplication/pdf
dc.language.isoen
dc.publisherThe American Society for Biochemistry and Molecular Biology, Inc.en_NZ
dc.relation.urihttp://www.jbc.org/content/279/20/20717.abstracten_NZ
dc.rightsThis is an author's accepted version. This research was originally published in The Journal of Biological Chemistry. © the American Society for Biochemistry and Molecular Biology.
dc.subjectenzymeen_NZ
dc.subjectthermalen_NZ
dc.titleA new intrinsic thermal parameter for enzymes reveals true temperature optimaen_NZ
dc.typeJournal Articleen_NZ
dc.identifier.doi10.1074/jbc.M309143200en_NZ
dc.relation.isPartOfThe Journal of Biological Chemistryen_NZ
pubs.begin-page20717en_NZ
pubs.editionMayen_NZ
pubs.elements-id29981
pubs.end-page20722en_NZ
pubs.issue20en_NZ
pubs.volume279en_NZ


Files in this item

This item appears in the following Collection(s)

Show simple item record