The primordial high energy compound: ATP or inorganic pyrophosphate?
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.[1]References
- The primordial high energy compound: ATP or inorganic pyrophosphate? Chi, A., Kemp, R.G. J. Biol. Chem. (2000) [Pubmed]
Annotations and hyperlinks in this abstract are from individual authors of WikiGenes or automatically generated by the WikiGenes Data Mining Engine. The abstract is from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg
