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

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.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Verhoeven JA,Schenck KM,Meyer RR,Trela JM

doi

10.1128/jb.168.1.318-321.1986

subject

Has Abstract

pub_date

1986-10-01 00:00:00

pages

318-21

issue

1

eissn

0021-9193

issn

1098-5530

journal_volume

168

pub_type

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