Cooperative Conformational Transitions Underpin the Activation Heat Capacity in the Temperature Dependence of Enzyme Catalysis.

ABSTRACT: Many enzymes display non-Arrhenius behavior with curved Arrhenius plots in the absence of denaturation. There has been significant debate about the origin of this behavior and recently the role of the activation heat capacity (ΔC_P^⧧) has been widely discussed. If enzyme-catalyzed reactions occur with appreciable negative values of ΔC_P^⧧ (arising from narrowing of the conformational space along the reaction coordinate), then curved Arrhenius plots are a consequence. To investigate these phenomena in detail, we have collected high precision temperature-rate data over a wide temperature interval for a model glycosidase enzyme MalL, and a series of mutants that change the temperature-dependence of the enzyme-catalyzed rate. We use these d

SUBMITTER: Walker EJ 

PROVIDER: S-EPMC11020164 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature