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Originally published In Press as doi:10.1074/jbc.C000581200 on September 21, 2000

J. Biol. Chem., Vol. 275, Issue 46, 35677-35679, November 17, 2000
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ACCELERATED PUBLICATION
The Primordial High Energy Compound: ATP or Inorganic Pyrophosphate?*

Andrew Chi and Robert G. KempDagger

From the Department of Biochemistry and Molecular Biology, The Chicago Medical School, North Chicago, Illinois 60064

The pyrophosphate-dependent phosphofructokinase (PPi-PFK) of Entamoeba histolytica displays a millionfold preference for inorganic pyrophosphate (PPi) over ATP (calculated as the ratio of kcat/Km). The introduction of a single mutation by site-directed mutagenesis changes its preference from PPi to ATP. The single mutant has an 8-fold preference for ATP whereas a related double mutant shows a preference exceeding 10,000-fold. The results suggest the presence of a latent nucleotide binding site aligned for a catalytic role in PPi-PFK. It is proposed that the ancestral PFK was an ATP-dependent enzyme and that PPi-PFKs are a later evolving adaptation.

* This work was supported by National Institutes of Health Grant AI34527.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, The Chicago Medical School, 3333 Green Bay Rd., North Chicago, IL 60064. Tel.: 847-578-3246; Fax: 847-578-3240; E-mail: kempr@finchcms.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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