On the challenge of exploring the evolutionary trajectory from phosphotriesterase to arylesterase using computer simulations.

ABSTRACT: The ability to design effective enzymes presents a fundamental challenge in biotechnology and also in biochemistry. Unfortunately, most of the progress on this field has been accomplished by bringing the reactants to a reasonable orientation relative to each other, rather than by rational optimization of the polar preorganization of the environment, which is the most important catalytic factor. True computer based enzyme design would require the ability to evaluate the catalytic power of designed active sites. This work considers the evolution from a phosphotriesterase (with the paraoxon substrate) to arylesterase (with the 2-naphthylhexanoate (2NH) substrate) catalysis. Both the original and the evolved enzymes involve two zinc ions and their ligands, making it hard to obtain a reliable q

SUBMITTER: Bora RP 

PROVIDER: S-EPMC11343073 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature