@article{3d3303988747402c936f9d3b875c0fc5,
title = "Rotational-echo double-resonance NMR-restrained model of the ternary complex of 5-enolpyruvylshikimate-3-phosphate synthase.",
author = "McDowell, \{Lynda M.\} and Barbara Poliks and Studelska, \{Daniel R.\} and O'Connor, \{Robert D.\} and Beusen, \{Denise D.\} and Jacob Schaefer",
note = "Lynda M. McDowell Barbara Poliks Daniel R. Studelska Robert D. O'Connor Denise D. Beusen Jacob Schaefer The 46-kD enzyme 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase catalyzes the condensation of shikimate-3-phosphate (S3P) and phosphoenolpyruvate to form EPSP. The reaction is inhibited by N-(phosphonomethyl)-glycine (Glp), which, in the presence of S3P, binds to EPSP synthase to form a stable ternary complex.",
year = "2004",
month = jan,
day = "1",
doi = "10.1023/B:JNMR.0000012864.70184.48",
language = "American English",
volume = "28",
journal = "Journal of Biomolecular NMR",
}