Assessment of enzyme active site positioning and tests of catalytic mechanisms through X-ray-derived conformational ensembles.

ABSTRACT: How enzymes achieve their enormous rate enhancements remains a central question in biology, and our understanding to date has impacted drug development, influenced enzyme design, and deepened our appreciation of evolutionary processes. While enzymes position catalytic and reactant groups in active sites, physics requires that atoms undergo constant motion. Numerous proposals have invoked positioning or motions as central for enzyme function, but a scarcity of experimental data has limited our understanding of positioning and motion, their relative importance, and their changes through the enzyme's reaction cycle. To examine positioning and motions and test catalytic proposals, we collected "room temperature" X-ray crystallography data for Pseudomonas putida ketosteroid isomerase (KS

SUBMITTER: Yabukarski F 

PROVIDER: S-EPMC7776779 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature