Engineered Tryptophan Synthase Balances Equilibrium Effects and Fast Dynamic Effects.

ABSTRACT: Creating efficient and stable enzymes for catalysis in pharmaceutical and industrial laboratories is an important research goal. Arnold et al. used directed evolution to engineer a natural tryptophan synthase to create a mutant that is operable under laboratory conditions without the need for a natural allosteric effector. The use of directed evolution allows researchers to improve enzymes without understanding the structure-activity relationship. Here, we present a transition path sampling study of a key chemical transformation in the tryptophan synthase catalytic cycle. We observed that while directed evolution does mimic the natural allosteric effect from a stability perspective, fast protein dynamics associated with chemistry has been dramatically altered. This work provides further ev

SUBMITTER: Schafer JW 

PROVIDER: S-EPMC9202816 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature