doi: 10.1128/jb.137.2.1024-1027.1979.
Purification and properties of phosphoglycerate phosphomutase from spores and cells of Bacillus megaterium
- PMID: 33959
- PMCID: PMC218391
- DOI: 10.1128/jb.137.2.1024-1027.1979
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Purification and properties of phosphoglycerate phosphomutase from spores and cells of Bacillus megaterium
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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