Interaction of the Herbicide Glyphosate with Its Target Enzyme 5-Enolpyruvylshikimate 3-Phosphate Synthase in Atomic Detail

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 98; no. 4; pp. 1376 - 1380
• Main Authors: Schönbrunn, Ernst, Eschenburg, Susanne, Shuttleworth, Wendy A., Schloss, John V., Amrhein, Nikolaus, Jeremy N. S. Evans, Kabsch, Wolfgang
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 13.02.2001; National Acad Sciences; The National Academy of Sciences
• Subjects: 3-Phosphoshikimate 1-Carboxyvinyltransferase; Alkyl and Aryl Transferases - chemistry; Amino acids; Binding Sites; Biochemistry; Biological Sciences; Drug resistance; Enzyme Inhibitors - chemistry; Enzymes; Formates - chemistry; Glycine - analogs & derivatives; Glycine - chemistry; Glyphosate; Herbicides; Herbicides - chemistry; Models, Molecular; Molecular Structure; Phosphates - chemistry; Phosphoenolpyruvate - chemistry; Protein Structure, Tertiary; X-Ray Diffraction

Biosynthesis of aromatic amino acids in plants, many bacteria, and microbes relies on the enzyme 5-enolpyruvylshikimate 3-phosphate (EPSP) synthase, a prime target for drugs and herbicides. We have identified the interaction of EPSP synthase with one of its two substrates (shikimate 3-phosphate) and...