title: Purification and properties of the manganese-dependent phosphoglycerate mutase of Bacillus subtilis.
abstract: Phosphoglycerate mutase of Bacillus subtilis was purified to apparent homogeneity. It specifically required manganese ions for stability and activity, but it does not need 2,3-diphosphoglycerate as cofactor; the Km for Mn2+ is about 4.5 micrometer. Enzyme activity was inhibited by heavy-metal ions, 2,3-butanedione, and sulfhydryl agents. The mutase has a molecular weight of about 74,000 as shown by Sephadex gel filtration and by acrylamide gel electrophoresis in the presence of sodium dodecyl sulfate; it consisted of one polypeptide.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D001412:Bacillus subtilis / Q000201:enzymology*; D002474:Cell-Free System; D003931:Diacetyl / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D008345:Manganese / Q000378:metabolism; D008670:Metals / Q000494:pharmacology; D008970:Molecular Weight; D010736:Phosphoglycerate Mutase / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism*; D010770:Phosphotransferases / Q000378:metabolism*; D013439:Sulfhydryl Reagents / Q000494:pharmacology
chemical_list: D000596:Amino Acids; D008670:Metals; D013439:Sulfhydryl Reagents; D008345:Manganese; D010770:Phosphotransferases; D010736:Phosphoglycerate Mutase; D003931:Diacetyl