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  2. Phosphofructokinase 2 - Wikipedia

    en.wikipedia.org/wiki/Phosphofructokinase_2

    Furthermore, the allosteric regulation of PFK2 is very similar to the regulation of PFK1. [20] High levels of AMP or phosphate group signifies a low energy charge state and thus stimulates PFK2. On the other hand, a high concentration of phosphoenolpyruvate (PEP) and citrate signifies that there is a high level of biosynthetic precursor and ...

  3. Phosphofructokinase - Wikipedia

    en.wikipedia.org/wiki/Phosphofructokinase

    PFK exists as a homotetramer in bacteria and mammals (where each monomer possesses 2 similar domains) and as an octomer in yeast (where there are 4 alpha- (PFK1) and 4 beta-chains (PFK2), the latter, like the mammalian monomers, possessing 2 similar domains [3]). This protein may use the morpheein model of allosteric regulation. [5]

  4. Allosteric regulation - Wikipedia

    en.wikipedia.org/wiki/Allosteric_regulation

    Allosteric regulation of an enzyme. In the fields of biochemistry and pharmacology an allosteric regulator (or allosteric modulator) is a substance that binds to a site on an enzyme or receptor distinct from the active site, resulting in a conformational change that alters the protein's activity, either enhancing or inhibiting its function.

  5. Allosteric modulator - Wikipedia

    en.wikipedia.org/wiki/Allosteric_modulator

    The site that an allosteric modulator binds to (i.e., an allosteric site) is not the same one to which an endogenous agonist of the receptor would bind (i.e., an orthosteric site). Modulators and agonists can both be called receptor ligands. [2] Allosteric modulators can be 1 of 3 types either: positive, negative or neutral.

  6. Allosteric enzyme - Wikipedia

    en.wikipedia.org/wiki/Allosteric_enzyme

    Allosteric regulation is also particularly important in the cell's ability to adjust enzyme activity. The term allostery comes from the Greek allos (ἄλλος), "other," and stereos (στερεὀς), "solid (object)." This is in reference to the fact that the regulatory site of an allosteric protein is physically distinct from its active site.

  7. Fructose 1,6-bisphosphatase - Wikipedia

    en.wikipedia.org/wiki/Fructose_1,6-bisphosphatase

    The arrangement of the catalytic side chains and metal ligands was found to be consistent with the three-metal ion assisted catalysis mechanism proposed for other FBPases. The fructose 1,6-bisphosphatases found within the Bacillota (low GC Gram-positive bacteria) do not show any significant sequence similarity to the enzymes from other organisms .

  8. What Doctors Want You to Know About Getting the New COVID-19 ...

    www.aol.com/doctors-want-know-getting-covid...

    The updated COVID-19 vaccine is now available. Infectious disease doctors recommend being smart about the timing of your shot. You can expect similar side effects to the previous vaccines if you ...

  9. Fructose 2,6-bisphosphate - Wikipedia

    en.wikipedia.org/wiki/Fructose_2,6-bisphosphate

    Fru-2,6-P 2 strongly activates glucose breakdown in glycolysis through allosteric modulation (activation) of phosphofructokinase 1 (PFK-1).Elevated expression of Fru-2,6-P 2 levels in the liver allosterically activates phosphofructokinase 1 by increasing the enzyme’s affinity for fructose 6-phosphate, while decreasing its affinity for inhibitory ATP and citrate.