Insights into the low-temperature adaptation of an enzyme as studied through ancestral sequence reconstruction.

ABSTRACT: For billions of years, enzymes have evolved in response to the changing environments in which their host organisms lived. Various lines of evidence suggest the earliest primitive organisms inhabited high-temperature environments and possessed enzymes adapted to such conditions. Consequently, extant mesophilic and psychrophilic enzymes are believed to have adapted to lower temperatures during the evolutionary process. Herein, we analyzed this low-temperature adaptation using ancestral sequence reconstruction. Previously, we generated the phylogenetic tree of 3-isopropylmalate dehydrogenases (IPMDHs) and reconstructed the sequence of the last bacterial common ancestor. The corresponding ancestral enzyme displayed high thermostability and catalytic activity at elevated temperatures but modera

SUBMITTER: Cui S 

PROVIDER: S-EPMC11836894 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature