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Escherichia coli E-39 ADPglucose synthetase has different activation kinetics from the wild-type allosteric enzyme.

Archives of biochemistry and biophysics - 1 Jul 1990

Gardiol A, Preiss J

Abstract excerpt

Kinetic and binding studies have shown that Lys39 of Escherichia coli ADPglucose synthetase is involved in binding of the allosteric activator. In order to study structure-function relationships at the activator binding site, this lysine residue was substituted by glutamic acid (Lys39----Glu) by site-directed mutagenesis. The resultant mutant enzyme (E-39) showed activation kinetics different from those of the...

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PMID: 2162151
DOI: 10.1016/0003-9861(90)90533-5

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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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