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...
Topics
- Adenosine Monophosphate
- Adenosine Triphosphate
- Allosteric Regulation
- Enzyme Activation
- Enzyme Inhibitors
- Escherichia coli
- Fructosediphosphates
- Glucose-1-Phosphate Adenylyltransferase
- Kinetics
- Magnesium Chloride
- Mutagenesis, Site-Directed
- Mutation
- Nucleotidyltransferases