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Article

Electrostatic and steric contributions to regulation at the active site of isocitrate dehydrogenase.

Science (New York, N.Y.) - 31 Aug 1990

Dean A M, Koshland D E

Abstract excerpt

The isocitrate dehydrogenase of Escherichia coli is regulated by covalent modification at the active site rather than, as expected, at an allosteric site. As a means of evaluating the mechanism of regulation, the kinetics of the substrate, 2R,3S-isocitrate, and a substrate analog, 2R-malate, were compared for the native, phosphorylated, and mutant enzymes. Phosphorylation decreases activity by more than a factor...

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Identifiers

PMID: 2204110
DOI: 10.1126/science.2204110

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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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