Temperature adaptation in structure and function in lactate dehydrogenase-A reflects convergent evolution in a few key protein regions.

ABSTRACT: Adaptive differences in the thermal stabilities of enzyme structure and function play critical roles in establishing the thermal optima and limits of all organisms. Thus, understanding the mechanisms underlying these adaptations can yield insights into protein structure-function relationships, protein evolution, and the consequences of temperature shifts on species distributions. Past studies have suggested that only a small number of amino acid substitutions are needed for adaptive change, but whether similar sites in the sequence, which we term thermal adaptation-related sequence sites (TRSS), and similar changes in amino acid content at these TRSS occur across widely different taxa remains to be elucidated. For detecting TRSS among orthologs of species adapted to a wide range of tempera

SUBMITTER: Zhu XL 

PROVIDER: S-EPMC12557798 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature