ArticleThe Biochemical journal2004
Identification of C-terminal motifs responsible for transmission of inhibition by ATP of mammalian phosphofructokinase, and their contribution to other allosteric effects.
Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 23 citations in OpenAlex.
- Bidirectional allosteric ligand regulation in a central glycolytic enzyme.bioRxiv : the preprint server for biology · 2026Article
- F26BP enables control of glycolysis rate independent of energy state.bioRxiv : the preprint server for biology · 2026Article
- Cooperativity inInternational journal of molecular sciences · 2025Article
- Small-molecule inhibitors of 6-phosphofructo-1-kinase simultaneously suppress lactate and superoxide generation in cancer cells.PloS one · 2025Article
- Roles ofFrontiers in physiology · 2023Article
- GFAT and PFK genes show contrasting regulation of chitin metabolism in Nilaparvata lugens.Scientific reports · 2021Article
- Unique PFK regulatory property from some mosquito vectors of disease, and from Drosophila melanogaster.Parasites & vectors · 2016Article
- Functional linkage of adenine nucleotide binding sites in mammalian muscle 6-phosphofructokinase.The Journal of biological chemistry · 2012Article
- Subunit interactions and composition of the fructose 6-phosphate catalytic site and the fructose 2,6-bisphosphate allosteric site of mammalian phosphofructokinase.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Systematic deletions and point mutations in the C-terminal extension of mammalian PFK (phosphofructokinase) led us to identify Leu-767 and Glu-768 of the M-type isoform (PFK-M) as the motifs responsible for the role of this region in inhibition by MgATP. These amino acids are the only residues of the C-terminus that are conserved in all mammalian isoforms, and were found to have a similar function in the C-type isoenzyme. Both residues in PFK-C and Leu-767 in PFK-M were also observed to be critical for inhibition by citrate, which is synergistic with that by MgATP. Binding studies utilizing titration of intrinsic protein fluorescence indicated that the C-terminal part of the enzyme participates in the signal transduction route from the MgATP inhibitory site to the catalytic site, but does not contribute to the binding of this inhibitor, whereas it is essential for the binding of citrate. Mutations of the identified structural motifs did not alter either the action of other allosteric effectors that also interact with MgATP, such as the inhibitor phosphoenolpyruvate and the strong activator fructose 2,6-bisphosphate, or the co-operative effect of fructose 6-phosphate. The latter data provide evidence that activation by fructose 2,6-bisphosphate and fructose 6-phosphate co-operativity are not linked to the same allosteric transition as that mediating inhibition by MgATP.
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