Analysis of Wild-type and Gly96Ala mutant EPSP synthase structures via in silico docking with inhibitors and molecular dynamics simulation

Abstract

The high frequency of contamination by herbicides suggests the need for more active and selective herbicides. Glyphosate is the active component of one of the top-selling herbicides, which is also a potent EPSP synthase inhibitor. That is a key enzyme in the shikimic acid pathway, which is found only in plants and some microorganisms. Thus, EPSP synthase is regarded as a prime target for herbicides. In this line, molecular modeling studies using molecular dynamics simulations and molecular docking techniques were performed to understand the interaction of glyphosate and its analogs with the wild type enzyme and Gly96Ala mutant EPSP synthase. Our findings indicate some key points for the designing new selective glyphosate derivates.