Dynamic allostery can drive cold adaptation in enzymes.

ABSTRACT: Adaptation of organisms to environmental niches is a hallmark of evolution. One prevalent example is that of thermal adaptation, in which two descendants evolve at different temperature extremes^1,2. Underlying the physiological differences between such organisms are changes in enzymes that catalyse essential reactions ³ , with orthologues from each organism undergoing adaptive mutations that preserve similar catalytic rates at their respective physiological temperatures^4,5. The sequence changes responsible for these adaptive differences, however, are often at surface-exposed sites distant from the substrate-binding site, leaving the active site of the enzyme structurally unperturbed^6,7. How such changes are allosterically propagated to the active

SUBMITTER: Saavedra HG 

PROVIDER: S-EPMC6033628 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature