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. 1979 Feb;137(2):773–778. doi: 10.1128/jb.137.2.773-778.1979

Purification and properties of the manganese-dependent phosphoglycerate mutase of Bacillus subtilis.

K Watabe, E Freese
PMCID: PMC218356  PMID: 33963

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.

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Selected References

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