The Energetic Origin of Different Catalytic Activities in Temperature-Adapted Trypsins.

ABSTRACT: Psychrophilic enzymes were always observed to have higher catalytic activity (k _cat) than their mesophilic homologs at room temperature, while the origin of this phenomenon remains obscure. Here, we used two different temperature-adapted trypsins, the psychrophilic Atlantic cod trypsin (ACT) and the mesophilic bovine trypsin (BT), as a model system to explore the energetic origin of their different catalytic activities using computational methods. The results reproduce the characteristic changing trends in the activation free energy, activation enthalpy, and activation entropy between the psychrophilic and mesophilic enzymes, where, in particular, the slightly decreased activation free energy of ACT is determined by its considerably reduced activation enthalpy rather than

SUBMITTER: Xia YL 

PROVIDER: S-EPMC7542600 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature