title: Purification and properties of phosphoglycerate phosphomutase from spores and cells of Bacillus megaterium.
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.
mesh_terms: 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
chemical_list: D000596:Amino Acids; D005994:Glycerophosphates; D008345:Manganese; D010770:Phosphotransferases; D010736:Phosphoglycerate Mutase