Evidence for an arginine residue at the allosteric sites of spinach leaf ADPglucose pyrophosphorylase.

@article{Ball1992EvidenceFA,
  title={Evidence for an arginine residue at the allosteric sites of spinach leaf ADPglucose pyrophosphorylase.},
  author={Kathryn L. Ball and Jack Preiss},
  journal={Journal of protein chemistry},
  year={1992},
  volume={11 3},
  pages={231-8}
}
The covalent modification of spinach leaf ADPglucose pyrophosphorylase leads to inactivation of both activator-stimulated and -unstimulated activity. Inactivation can be prevented if either the activator 3PGA or the inhibitor Pi are present during the modification. Pi proved to be more effective at protecting the enzyme from inactivation as it afforded 50% protection at 51 microM compared to 50% protection by 405 microM 3PGA. Partial modification of the enzyme using [14C]-phenylglyoxal leads to… CONTINUE READING