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Article

Slowed enzymatic turnover allows characterization of intermediates by solid-state NMR.

Biochemistry - 16 Dec 1997

Studelska D R, McDowell L M, Espe M P, Klug C A, Schaefer J

Abstract excerpt

EPSP (5-enolpyruvylshikimate-3-phosphate) synthase catalyzes condensation of shikimate 3-phosphate (S3P) and phosphoenolpyruvate (PEP) to form EPSP, a precursor to the aromatic amino acids. S3P and [2-13C]POP were bound to mutant or wild type E. coli forms of the enzyme prior to lyophilization. CPMAS-echo and rotational-echo double-resonance (REDOR) NMR experiments, employing a slow catalytic EPSP synthase mutant...

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Identifiers

PMID: 9445553
DOI: 10.1021/bi972246v

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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