Data from: An appraisal of the enzyme stability-activity trade-off

Miller SR

Date Published: May 11, 2017

DOI: http://dx.doi.org/10.5061/dryad.5k30c

 

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Title Data used for analyses of the enzyme stability-activity relationship
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Description Data were obtained from a literature search. Web of Science searches from 1968 through 2016 were performed under the topic terms (1) “enzyme stability” and “temperature” and (2) “temperature adaptation” and “protein”, respectively.To be included, data were required for three or more purified orthologous enzymes for some measure of both (1) enzyme stability and (2) enzyme kinetics assayed at a common garden temperature. For the former, this included enzyme denaturation temperature (Tm), enzyme optimal temperature (Topt), time to 50% enzyme inactivation (T50) or other estimate of residual activity, and the free energy of unfolding (GU). For the latter, this included enzyme catalytic turnover number (kcat), maximal rate of catalysis (Vmax), enzyme specific activity, and the Michaelis constant (Km), a measure of an enzyme’s substrate affinity (1/Km is related but not identical to enzyme binding affinity).
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When using this data, please cite the original publication:

Miller SR (2017) An appraisal of the enzyme stability-activity trade-off. Evolution 71(7): 1876-1887. http://dx.doi.org/10.1111/evo.13275

Additionally, please cite the Dryad data package:

Miller SR (2017) Data from: An appraisal of the enzyme stability-activity trade-off. Dryad Digital Repository. http://dx.doi.org/10.5061/dryad.5k30c
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