Complex Loop Dynamics Underpin Activity, Specificity, and Evolvability in the (βα)₈ Barrel Enzymes of Histidine and Tryptophan Biosynthesis.

ABSTRACT: Enzymes are conformationally dynamic, and their dynamical properties play an important role in regulating their specificity and evolvability. In this context, substantial attention has been paid to the role of ligand-gated conformational changes in enzyme catalysis; however, such studies have focused on tremendously proficient enzymes such as triosephosphate isomerase and orotidine 5'-monophosphate decarboxylase, where the rapid (μs timescale) motion of a single loop dominates the transition between catalytically inactive and active conformations. In contrast, the (βα)₈-barrels of tryptophan and histidine biosynthesis, such as the specialist isomerase enzymes HisA and TrpF, and the bifunctional isomerase PriA, are decorated by multiple long loops that undergo conformational tran

SUBMITTER: Romero-Rivera A 

PROVIDER: S-EPMC9088769 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature