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dc.contributor.authorPrentice, Erica Jeanen_NZ
dc.contributor.authorHicks, Joannaen_NZ
dc.contributor.authorBallerstedt, Hendriken_NZ
dc.contributor.authorBlank, Lars M.en_NZ
dc.contributor.authorLiang, Liyin L.en_NZ
dc.contributor.authorSchipper, Louis A.en_NZ
dc.contributor.authorArcus, Vickery L.en_NZ
dc.coverage.spatialUnited Statesen_NZ
dc.date.accessioned2020-10-15T02:29:16Z
dc.date.available2020-10-15T02:29:16Z
dc.date.issued2020en_NZ
dc.identifier.citationPrentice, E. J., Hicks, J., Ballerstedt, H., Blank, L. M., Liang, L. L., Schipper, L. A., & Arcus, V. L. (2020). The inflection point hypothesis: The relationship between the temperature dependence of enzyme-catalyzed reaction rates and microbial growth rates. Biochemistry, 59(38), 3562–3569. https://doi.org/10.1021/acs.biochem.0c00530en
dc.identifier.urihttps://hdl.handle.net/10289/13901
dc.description.abstractThe temperature dependence of biological rates at different scales (from individual enzymes to isolated organisms to ecosystem processes such as soil respiration and photosynthesis) is the subject of much historical and contemporary research. The precise relationship between the temperature dependence of enzyme rates and those at larger scales is not well understood. We have developed macromolecular rate theory (MMRT) to describe the temperature dependence of biological processes at all scales. Here we formalize the scaling relationship by investigating MMRT both at the molecular scale (constituent enzymes) and for growth of the parent organism. We demonstrate that the inflection point (𝘛ᵢₙ𝒻) for the temperature dependence of individual metabolic enzymes coincides with the optimal growth temperature for the parent organism, and we rationalize this concordance in terms of the necessity for linearly correlated rates for metabolic enzymes over fluctuating environmental temperatures to maintain homeostasis. Indeed, 𝘛ᵢₙ𝒻 is likely to be under strong selection pressure to maintain coordinated rates across environmental temperature ranges. At temperatures at which rates become uncorrelated, we postulate a regulatory catastrophe and organism growth rates precipitously decline at temperatures where this occurs. We show that the curvature in the plots of the natural log of the rate versus temperature for individual enzymes determines the curvature for the metabolic process overall and the curvature for the temperature dependence of the growth of the organism. We have called this "the inflection point hypothesis", and this hypothesis suggests many avenues for future investigation, including avenues for engineering the thermal tolerance of organisms.en_NZ
dc.language.isoengen_NZ
dc.rightsThis is an author's accepted version of an article published in Biochemistry. © 2020 American Chemical Society.
dc.subjectPeptides and proteins
dc.subjectHeat capacity
dc.subjectCarbohydrates
dc.subjectChemical reactions
dc.subjectTemperature dependence
dc.titleThe inflection point hypothesis: The relationship between the temperature dependence of enzyme-catalyzed reaction rates and microbial growth rates.en_NZ
dc.typeJournal Article
dc.identifier.doi10.1021/acs.biochem.0c00530en_NZ
dc.relation.isPartOfBiochemistryen_NZ
pubs.begin-page3562
pubs.elements-id257479
pubs.end-page3569
pubs.issue38en_NZ
pubs.publication-statusPublisheden_NZ
pubs.volume59en_NZ
dc.identifier.eissn1520-4995en_NZ


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