Ontology highlight
ABSTRACT:
SUBMITTER: Schonbrunn E
PROVIDER: S-EPMC29264 | biostudies-literature | 2001 Feb
REPOSITORIES: biostudies-literature
Proceedings of the National Academy of Sciences of the United States of America 20010201 4
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 with the widely used herbicide glyphosate by x-ray crystallography. The two-domain enzyme closes on ligand binding, thereby forming the active site in the interdomain cleft. Glyphosate appears to occ ...[more]