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. 1971 Dec;108(3):1122–1128. doi: 10.1128/jb.108.3.1122-1128.1971

Catalytic Properties and Regulatory Diversity of Inorganic Pyrophosphatases from Photosynthetic Bacteria

Jobst-Heinrich Klemme a,1, Brigitte Klemme a,1, Howard Gest a
PMCID: PMC247195  PMID: 4333319

Abstract

Soluble inorganic pyrophosphatases of five species of nonsulfur purple bacteria were investigated in respect to reaction kinetics, regulatory behavior, and other characteristics. The enzymes appear to fall into two groups with correlated properties. The pyrophosphatases of Rhodopseudomonas capsulata and R. spheroides have molecular weights of ∼60,000, are stabilized by Co2+, and exhibit simple Michaelis-Menten reaction kinetics. On the other hand, the enzymes of R. palustris, R. gelatinosa, and Rhodospirillum rubrum are larger (molecular weight ∼100,000), require Zn2+ for maintenance of catalytic activity, and show complex reaction kinetics; these pyrophosphatases are activated by free Mg2+ ions and, in the absence of the latter, are inhibited by 2-phosphoglyceric acid. The results described indicate the existence of alternative control patterns for regulation of intracellular turnover of phosphate, which is in part mediated by pyrophosphatases.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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