ArticleThe Journal of biological chemistry2012
Functional linkage of adenine nucleotide binding sites in mammalian muscle 6-phosphofructokinase.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 30 citations in OpenAlex.
- The Critical Role of Adenylate Kinase in Regulating the Glycolysis Rate in Cells.International journal of molecular sciences · 2026Article
- Activity-Based Acylome Profiling withJournal of the American Chemical Society · 2024Article
- Structural basis for allosteric regulation of human phosphofructokinase-1.Nature communications · 2024Article
- Gene expression and metabolite levels converge in the thermogenic spadix of skunk cabbage.Plant physiology · 2024Article
- Structural basis for allosteric regulation of human phosphofructokinase-1.bioRxiv : the preprint server for biology · 2024Article
- A critical review of ethanol effects on neuronal firing: A metabolic perspective.Alcohol, clinical & experimental research · 2024Review
- Biomimetic Synthesis and Chemical Proteomics Reveal the Mechanism of Action and Functional Targets of Phloroglucinol Meroterpenoids.Journal of the American Chemical Society · 2024Article
- Cancer-associated somatic mutations in human phosphofructokinase-1 reveal a critical electrostatic interaction for allosteric regulation of enzyme activity.The Biochemical journal · 2023Article
- Prediction of Oscillations in Glycolysis in Ethanol-Consuming Erythrocyte-Bioreactors.International journal of molecular sciences · 2023Article
- AMP deamination is sufficient to replicate an atrophy-like metabolic phenotype in skeletal muscle.Metabolism: clinical and experimental · 2021Article
- Article
- Cinnamon Oil InhibitsJournal of fungi (Basel, Switzerland) · 2021Article
- Structures, functions, and mechanisms of filament forming enzymes: a renaissance of enzyme filamentation.Biophysical reviews · 2019Review
- Phosphofructokinase-1 and fructose bisphosphatase-1 in canine liver and kidney.The Journal of veterinary medical science · 2019Article
- Functional Roles of Metabolic Intermediates in Regulating the Human Mitochondrial NAD(P)Scientific reports · 2019Article
- Yap regulates glucose utilization and sustains nucleotide synthesis to enable organ growth.The EMBO journal · 2018Article
- The glycolytic enzyme phosphofructokinase-1 assembles into filaments.The Journal of cell biology · 2017Article
- Article
- Structures of human phosphofructokinase-1 and atomic basis of cancer-associated mutations.Nature · 2015Article
- Crystallization and preliminary crystallographic analysis of human muscle phosphofructokinase, the main regulator of glycolysis.Acta crystallographica. Section F, Structural biology communications · 2014Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
6-Phosphofructokinases (Pfk) are homo- and heterooligomeric, allosteric enzymes that catalyze one of the rate-limiting steps of the glycolysis: the phosphorylation of fructose 6-phosphate at position 1. Pfk activity is modulated by a number of regulators including adenine nucleotides. Recent crystal structures from eukaryotic Pfk revealed several adenine nucleotide binding sites. Herein, we determined the functional relevance of two adenine nucleotide binding sites through site-directed mutagenesis and enzyme kinetic studies. Subsequent characterization of Pfk mutants allowed the identification of the activating (AMP, ADP) and inhibitory (ATP, ADP) allosteric binding sites. Mutation of one binding site reciprocally influenced the allosteric regulation through nucleotides interacting with the other binding site. Such reciprocal linkage between the activating and inhibitory binding sites is in agreement with current models of allosteric enzyme regulation. Because the allosteric nucleotide binding sites in eukaryotic Pfk did not evolve from prokaryotic ancestors, reciprocal linkage of functionally opposed allosteric binding sites must have developed independently in prokaryotic and eukaryotic Pfk (convergent evolution).
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.