Rotational-echo double-resonance NMR-restrained model of the ternary complex of 5-enolpyruvylshikimate-3-phosphate synthase.

TY - JOUR

T1 - Rotational-echo double-resonance NMR-restrained model of the ternary complex of 5-enolpyruvylshikimate-3-phosphate synthase.

AU - McDowell, Lynda M.

AU - Poliks, Barbara

AU - Studelska, Daniel R.

AU - O'Connor, Robert D.

AU - Beusen, Denise D.

AU - Schaefer, Jacob

N1 - 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.

PY - 2004/1/1

Y1 - 2004/1/1

UR - https://link.springer.com/article/10.1023/B:JNMR.0000012864.70184.48

U2 - 10.1023/B:JNMR.0000012864.70184.48

DO - 10.1023/B:JNMR.0000012864.70184.48

M3 - Article

VL - 28

JO - Journal of Biomolecular NMR

JF - Journal of Biomolecular NMR

ER -