| Literature DB >> 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.Entities:
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Year: 1979 PMID: 33963 PMCID: PMC218356 DOI: 10.1128/jb.137.2.773-778.1979
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490