Purification and properties of phosphoglycerate phosphomutase from spores and cells of Bacillus megaterium.

@article{Singh1979PurificationAP,
  title={Purification and properties of phosphoglycerate phosphomutase from spores and cells of Bacillus megaterium.},
  author={Rana P Singh and Peter Setlow},
  journal={Journal of bacteriology},
  year={1979},
  volume={137 2},
  pages={1024-7}
}
Phosphoglycerate phosphomutase has been purified to homogeneity from vegetative cells and germinated spores of Bacillus megaterium, and the spore and cell enzymes appear identical. The enzyme is a monomer of molecular weight 61,000. The compound 2,3-diphosphoglyceric acid is not required for activity, but the enzyme has an absolute and specific requirement for Mn2+. The enzyme is inhibited by ethylenediaminetetraacetate and sulfhydryl reagents, has a pH optimum of about 8.0, and has Km values… CONTINUE READING

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