EPSP synthase
Structure of EPSP SynthaseStructure of EPSP Synthase
5-enolpyruvylshikimate 3-phosphate (EPSP) synthase is a key enzyme for the biosynthesis of aromatic amino acids in plants and many microbes. Consequently, it is a target for drugs and herbicides. EPSP synthase catalyzes the addition of phosphoenol pyruvate (PEP) to shikimate-3-phosphate, generating 5-enolpyruvylshikimate-3-phosphate, which is a precursor for phenylalanine and tyrosine. The enzyme has , with the active site found in the interdomain cleft. There is a substantial structural change upon substrate binding, resulting in a . Glyphosate (also known as Roundup) occupies the binding site of the second substrate, phosphoenol pyruvate. 3D structures of EPSP synthaseUpdated on 05-May-2025 1eps – EcEPSP – Escherichia coli 1p88, 1p89 - EcEPSP N terminal - NMR EPSP synthase binary complex1g6t - EcEPSP + S3P 1mi4, 2qfq, 2qfs, 3fjx, 3fk0 - EcEPSP (mutant) + S3P EPSP synthase ternary complex1g6p - EcEPSP + S3P + glyphosate 2qft, 2qfu, 3fjz, 3fk1 - EcEPSP (mutant) + S3P + glyphosate
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