Biophysical characterization and analysis of a mesophilic chorismate mutase from B. pumilus
Chorismate mutases have extensively been used as computational benchmarking systems for enzyme catalysis, yet the roles entropy and enthalpy play in catalysis are still not fully understood. Thus, it is important to better understand these enzymes for potential research or industrial applications. Here, we report the first crystal structure and kinetic characterization of a chorismate mutase from Bacillus pumilus. This enzyme exhibits a high degree of similarity to a known mesophilic chorismate mutase from Bacillus subtilis. Using this crystal structure, we further employ EVB/MD simulations to construct Arrhenius plots, allowing us to extract thermodynamic activation parameters. Overall, this study provides new insights into the structural and functional features of the B. pumilus chorismate mutase and highlights its potential as a valuable enzyme for biocatalytic and biotechnological applications.