Activation parameters, enthalpy-entropy compensation and the temperature-dependent activity of enzymes.

ABSTRACT: The increase in enzyme-catalyzed reaction rates with temperature is typically modeled using Arrhenius or Eyring relations. Interpretation of extracted parameters is subject to multiple caveats. Here we analyze the impact of expected small temperature variations of underlying activation/Eyring parameters on this modeling. Linear Arrhenius/Eyring behavior can still be observed when the underlying activation energy Ea or enthalpy ΔH and entropy ΔS vary with temperature. Modest variations - of the order of an H-bond energy over 60 °C - lead to large fractional deviations of Ea,ΔH and ΔS values derived from linear fits from their underlying values and to deviations of Arrhenius prefactors A by orders of magnitude. In a family of related enzymes with similar activation free energies ΔG , small d

SUBMITTER: McLeod MJ 

PROVIDER: S-EPMC12642627 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature