5-Enolpyruvylshikimate-3-phosphate synthase (EPSPS) (EPSPS)

5-Enolpyruvylshikimate-3-phosphate synthase (EPSPS) is a key enzyme in the shikimate pathway, which is essential for the biosynthesis of aromatic amino acids such as phenylalanine, tyrosine, and tryptophan in plants, bacteria, and fungi (UniProt: P0A6D3). It catalyzes the chemical reaction between shikimate-3-phosphate and phosphoenolpyruvate (PEP) to produce 5-enolpyruvylshikimate-3-phosphate. Since this metabolic pathway is entirely absent in humans and other mammals, EPSPS represents a highly selective target for chemical intervention (PubMed: 11472531). The enzyme is most famously targeted by the herbicide glyphosate, which acts as a competitive inhibitor of PEP, effectively halting plant growth (PubChem: CID 5460340). In a clinical context, EPSPS is being explored as a potential target for novel antibiotics and antiparasitic drugs to treat infections like malaria and toxoplasmosis (PubMed: 23931162). By blocking the production of essential precursors, inhibitors of EPSPS can selectively kill pathogens without affecting the host's metabolic processes.

Other names

3-phosphoshikimate 1-carboxyvinyltransferaseEPSP synthaseAroA

Competitive inhibition of phosphoenolpyruvate (PEP) binding to the enzyme-shikimate-3-phosphate complex