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. 1979 Feb;137(2):1024–1027. doi: 10.1128/jb.137.2.1024-1027.1979

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

R P Singh, P Setlow
PMCID: PMC218391  PMID: 33959

Abstract

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 for 3-phosphoglyceric acid and Mn2+ of 5 x 10(-4) and 4 x 10(-5) M, respectively.

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Selected References

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  1. Grisolia S., Carreras J. Phosphoglycerate mutase from yeast, chicken breast muscle, and kidney (2, 3-PGA-dependent). Methods Enzymol. 1975;42:435–450. doi: 10.1016/0076-6879(75)42149-8. [DOI] [PubMed] [Google Scholar]
  2. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  3. Oh Y. K., Freese E. Manganese requirement of phosphoglycerate phosphomutase and its consequences for growth and sporulation of Bacillus subtilis. J Bacteriol. 1976 Aug;127(2):739–746. doi: 10.1128/jb.127.2.739-746.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Setlow P., Kornberg A. Biochemical studies of bacterial sporulation and germination. XXII. Energy metabolism in early stages of germination of Bacillus megaterium spores. J Biol Chem. 1970 Jul 25;245(14):3637–3644. [PubMed] [Google Scholar]
  5. Setlow P. Purification and properties of a specific proteolytic enzyme present in spores of Bacillus magaterium. J Biol Chem. 1976 Dec 25;251(24):7853–7862. [PubMed] [Google Scholar]
  6. Singh R. P., Setlow B., Setlow P. Levels of small molecules and enzymes in the mother cell compartment and the forespore of sporulating Bacillus megaterium. J Bacteriol. 1977 Jun;130(3):1130–1138. doi: 10.1128/jb.130.3.1130-1138.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Singh R. P., Setlow P. Enolase from spores and cells of Bacillus megaterium: two-step purification of the enzyme and some of its properties. J Bacteriol. 1978 Apr;134(1):353–355. doi: 10.1128/jb.134.1.353-355.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Singh R. P., Setlow P. Phosphoglycerate mutase in developing forespores of Bacillus megaterium may be regulated by the intrasporal level of free manganous ion. Biochem Biophys Res Commun. 1978 May 15;82(1):1–5. doi: 10.1016/0006-291x(78)90567-3. [DOI] [PubMed] [Google Scholar]
  9. Watabe K., Freese E. Purification and properties of the manganese-dependent phosphoglycerate mutase of Bacillus subtilis. J Bacteriol. 1979 Feb;137(2):773–778. doi: 10.1128/jb.137.2.773-778.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]

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