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Article

Probing the roles of key residues in the unique regulatory NADH binding site of type II citrate synthase of Escherichia coli.

The Journal of biological chemistry - 12 Sept 2003

Stokell David J, Donald Lynda J, Maurus Robert, Nguyen Nham T, Sadler Gillian, Choudhary Kajal, Hultin Philip G, Brayer Gary D, Duckworth Harry W

Abstract excerpt

The citrate synthase of Escherichia coli is an example of a Type II citrate synthase, a hexamer that is subject to allosteric inhibition by NADH. In previous crystallographic work, we defined the NADH binding sites, identifying nine amino acids whose side chains were proposed to make hydrogen bonds with the NADH molecule. Here, we describe the functional properties of nine sequence variants, in which these have...

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PMID: 12824188
DOI: 10.1074/jbc.M302786200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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