Site-directed mutagenesis of a regulatory site of Escherichia coli ADP-glucose pyrophosphorylase: the role of residue 336 in allosteric behavior.

@article{Meyer1998SitedirectedMO,
  title={Site-directed mutagenesis of a regulatory site of Escherichia coli ADP-glucose pyrophosphorylase: the role of residue 336 in allosteric behavior.},
  author={Craig R Meyer and Jack A Bork and S. Scott Nadler and J Yirsa and Jack Preiss},
  journal={Archives of biochemistry and biophysics},
  year={1998},
  volume={353 1},
  pages={152-9}
}
Site-directed mutagenesis was used to probe the role of glycine residue 336 in the regulatory properties of Escherichia coli ADP-glucose pyrophosphorylase. This residue was previously found to be changed from glycine to aspartate in the gene of an Escherichia coli mutant strain. The mutant enzyme had altered kinetic properties, including higher activity in the absence of the activator fructose 1,6-bisphosphate (FBP), higher apparent affinity for FBP and substrates, and lower apparent affinity… CONTINUE READING

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