Purification and properties of phosphoglycerate phosphomutase from spores and cells of Bacillus megaterium.
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.
D000596:Amino Acids / Q000032:analysis; D001410:Bacillus megaterium / Q000201:enzymology*; D005994:Glycerophosphates / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008345:Manganese / Q000378:metabolism; D008970:Molecular Weight; D010736:Phosphoglycerate Mutase / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism; D010770:Phosphotransferases / Q000302:isolation & purification; D013171:Spores, Bacterial / Q000201:enzymology
D000596:Amino Acids; D005994:Glycerophosphates; D008345:Manganese; D010770:Phosphotransferases; D010736:Phosphoglycerate Mutase