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Article

Insights into the evolution of allosteric properties. The NADH binding site of hexameric type II citrate synthases.

Biochemistry - 20 May 2003

Maurus Robert, Nguyen Nham T, Stokell David J, Ayed Ayeda, Hultin Philip G, Duckworth Harry W, Brayer Gary D

Abstract excerpt

Study of the hexameric and allosterically regulated citrate synthases (type II CS) provides a rare opportunity to gain not only an understanding of a novel allosteric mechanism but also insight into how such properties can evolve from an unregulated structural platform (the dimeric type I CS). To address both of these issues, we have determined the structure of the complex of NADH (a negative allosteric effector)...

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Share to Allosteric Regulation
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 12741811
DOI: 10.1021/bi020622s

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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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