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. 1986 Oct;168(1):318–321. doi: 10.1128/jb.168.1.318-321.1986

Purification and characterization of an inorganic pyrophosphatase from the extreme thermophile Thermus aquaticus.

J A Verhoeven, K M Schenck, R R Meyer, J M Trela
PMCID: PMC213453  PMID: 3020000

Abstract

An inorganic pyrophosphatase was purified over 600-fold to homogeneity as judged by polyacrylamide gel electrophoresis. The enzyme is a tetramer of Mr = 84,000, has a sedimentation coefficient of 5.8S, a Stokes radius of 3.5 nm, and an isoelectric point of 5.7. Like the enzyme of Escherichia coli, the pyrophosphatase appears to be made constitutively. The pH and temperature optima are 8.3 and 80 degrees C, respectively. The Km for PPi is 0.6 mM. A divalent cation is essential, with Mg2+ preferred. The enzyme uses only PPi as a substrate.

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Selected References

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