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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 ...
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]
Whether the kinase and phosphatase domains of PFK-2/FBPase-2 are active or inactive depends on the phosphorylation state of the enzyme. Fructose-6-p-phosphate is phosphorylated by the kinase domain of PFK-2/FBPase-2 to Fru-2,6-P 2 when PFK-2/FBPase-2 is active in a dephosphorylated state. This dephosphorylated state is favored by high levels of ...
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.
In enzymology, 1-phosphofructokinase (EC 2.7.1.56) is an enzyme that catalyzes the chemical reaction. ATP + D-fructose 1-phosphate → ADP + D-fructose 1,6-bisphosphate. Thus, the two substrates of this enzyme are ATP and D-fructose 1-phosphate, whereas its two products are ADP and D-fructose 1,6-bisphosphate.
China, where COVID-19 was first detected, is currently one of the world’s biggest manufacturers of coronavirus test kits. Customs data show that the country exported $1.6 billion worth of such ...
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PFK1 is an allosteric enzyme and has a structure similar to that of hemoglobin in so far as it is a dimer of a dimer. [5] One half of each dimer contains the ATP binding site whereas the other half the substrate (fructose-6-phosphate or (F6P)) binding site as well as a separate allosteric binding site.