pfkB Antibody

1. Data show that interactions between fructose-6-P and allosteric sites for ATP are operating within and between the phosphofructokinase-2 (Pfk-2) subunits. PMID: 27591700
2. Data show an unstructured monomeric phosphofructokinase-2 intermediate and that most part of the dimer structure is reached as a slow concerted folding/association step with a quite folded transition state in terms of solvent exposure. PMID: 21627967
3. Site-directed mutagenesis of R90 and D256 indicate that R90 participates in the binding of the phosphorylated substrate and that D256 is involved in the phosphoryl transfer mechanism. PMID: 20599671
4. the dimeric state of Pfk-2 is critical for the stability and the activity of the enzyme PMID: 15848164
5. The structure of E. coli phosphofructokinase Pfk-2 has been solved by X-ray diffraction. PMID: 16946484
6. Subunit contacts are critical for the maintenance of the overall structure of Pfk-2 and for the binding of ligands, explaining the reported importance of the dimeric state for enzymatic activity. PMID: 17469854
7. Results describe the structure of phosphofructokinase-2 in its inhibited tetrameric form, with each subunit bound to two ATP molecules and two Mg ions. PMID: 18762190
8. Pfk-2 undergoes a cooperative unfolding/dissociation process with the accumulation of an expanded and unstructured monomeric intermediate with a marginal stability and a large solvent accessibility with respect to the native dimer. PMID: 19465020

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KEGG: ecj:JW5280

STRING: 316385.ECDH10B_1861