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J Biol Chem. 2000 Nov 17;275(46):35677-9.

The primordial high energy compound: ATP or inorganic pyrophosphate?

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  • 1Department of Biochemistry and Molecular Biology, The Chicago Medical School, North Chicago, Illinois 60064, USA.


The pyrophosphate-dependent phosphofructokinase (PP(i)-PFK) of Entamoeba histolytica displays a million fold preference for inorganic pyrophosphate (PP(i)) over ATP (calculated as the ratio of k(cat)/K(m)). The introduction of a single mutation by site-directed mutagenesis changes its preference from PP(i) 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 PP(i)-PFK. It is proposed that the ancestral PFK was an ATP-dependent enzyme and that PP(i)-PFKs are a later evolving adaptation.

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