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Article

A kinetic study of site-directed mutants of Escherichia coli ADP-glucose pyrophosphorylase: the role of residue 295 in allosteric regulation.

Archives of biochemistry and biophysics - 15 Apr 1998

Meyer C R, Yirsa J, Gott B, Preiss J

Abstract excerpt

The effects of amino acid substitutions at residue 295 on the regulatory properties of Escherichia coli ADP-glucose pyrophosphorylase were studied. In previous studies, this residue, altered from proline to serine (P295S) in the gene of a mutant strain of E. coli, resulted in a high-activity form of enzyme [higher activity in absence of activator fructose 1,6-bisphosphate (FBP), higher apparent affinity for FBP...

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Identifiers

PMID: 9587413
DOI: 10.1006/abbi.1998.0593

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