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Article

Identification of substrate contact residues important for the allosteric regulation of phosphofructokinase from Eschericia coli.

Biochemistry - 3 Jun 2003

Fenton Aron W, Paricharttanakul N Monique, Reinhart Gregory D

Abstract excerpt

The side chains of Escherichia coli phosphofructokinase (EcPFK) that interact with bound substrate, fructose 6-phosphate (Fru-6-P), are examined for their potential roles in allosteric regulation. Mutations that severely decrease Fru-6-P affinity and/or k(cat)/K(m) were created at each contact residue, with the exception of the catalytic base, D127. Even though Fru-6-P affinity was greatly decreased for R162E,...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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PMID: 12767227
DOI: 10.1021/bi034273t

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

Source receipt: pubmed, retrieved 7 Sept 2026.

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