Article
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...
Topics
- Allosteric Regulation
- Allosteric Site
- Base Sequence
- Chromatography, Ion Exchange
- Enzyme Activation
- Escherichia coli
- Glucose-1-Phosphate Adenylyltransferase
- Kinetics
- Lysine
- Molecular Sequence Data
- Mutation
- Nucleotidyltransferases
- Oligonucleotide Probes