Dissociation of the tetrameric phosphoglycerate mutase from yeast by a mutation in the subunit contact region.

@article{White1993DissociationOT,
  title={Dissociation of the tetrameric phosphoglycerate mutase from yeast by a mutation in the subunit contact region.},
  author={Malcolm F White and Linda A Fothergill-Gilmore and Sharon M Kelly and Nick C Price},
  journal={The Biochemical journal},
  year={1993},
  volume={295 ( Pt 3)},
  pages={743-8}
}
Phosphoglycerate mutases from different sources exhibit a variety of quaternary structures (tetramer, dimer and monomer). To perturb the tetrameric structure of yeast phosphoglycerate mutase we have prepared a mutant enzyme in which Lys-168 in the subunit-contact region has been replaced by proline. The K168P mutant enzyme undergoes dissociation to dimers at low concentrations; thus on lowering the concentration from 200 micrograms/ml to 5 micrograms/ml the proportion of tetramer falls from 85… CONTINUE READING