Please note these web pages are part of an assignment for a graduate course in Advanced Biochemistry and Molecular Biology BCMB8010 at the University of Georgia. Questions should be directed to Gina Pries (gpries@uga.edu).

Summary

In summary, EPSP synthase has been shown to be a unique enzyme both in its tertiary structure and its mechanism. EPSP synthase functions in transfering the enolpyruvyl moiety of PEP, rather than the phosphoryl group as in most PEP-catalyzing enzymes, to S3P to produce EPSP. Catalysis is carried out via an induced-fit mechanism with formation of a tetrahedral intermediate between S3P and PEP. Substrate binding induces closure of the two inside-out alpha/beta barrel domains to create a tight active site where catalysis can take place. It is important to understand the structure and mechanism of any enzyme in order to best design fine-tuned inhibitors which will only render a specific enzyme non-functional. The more than thirty years of study dedicated by so many groups to EPSP synthase has brought us to a near complete understanding of its structure and function.