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. 1979 Feb;137(2):1024-7.
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

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

R P Singh et al. J Bacteriol. 1979 Feb.

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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References

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