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Phosphofructokinase catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate, a key regulatory step in the glycolytic pathway. [ 2 ] [ 3 ] It is allosterically inhibited by ATP and allosterically activated by AMP , thus indicating the cell's energetic needs when it undergoes the glycolytic pathway. [ 4 ]
Similarly, inhibitors such as ATP and PEP bind to the same allosteric site and facilitate the formation of the T state, thereby inhibiting enzyme activity. The hydroxyl oxygen of carbon 1 does a nucleophilic attack on the beta phosphate of ATP. These electrons are pushed to the anhydride oxygen between the beta and gamma phosphates of ATP. [10 ...
Phosphofructokinase, or PFK, catalyzes the conversion of fructose-6-phosphate to fructose-1,6-bisphosphate and is an important point in the regulation of glycolysis. High levels of ATP, H +, and citrate inhibit PFK. If citrate levels are high, it means that glycolysis is functioning at an optimal rate. High levels of AMP stimulate PFK.
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. The enzyme was first described and ...
In enzymology, a 6-phosphofructo-2-kinase (EC 2.7.1.105) is an enzyme that catalyzes the chemical reaction: ATP + beta-D-fructose 6-phosphate ADP + beta-D-fructose 2,6-bisphosphate [16] Thus, the kinase domain hydrolyzes ATP to phosphorylate the carbon-2 of fructose-6-phosphate, producing Fru-2,6-P 2 and ADP.
The enzyme fructose bisphosphatase (EC 3.1.3.11; systematic name D-fructose-1,6-bisphosphate 1-phosphohydrolase) catalyses the conversion of fructose-1,6-bisphosphate to fructose 6-phosphate in gluconeogenesis and the Calvin cycle, which are both anabolic pathways: [1] [2]
An example of a coupled reaction is the phosphorylation of fructose-6-phosphate to form the intermediate fructose-1,6-bisphosphate by the enzyme phosphofructokinase accompanied by the hydrolysis of ATP in the pathway of glycolysis. The resulting chemical reaction within the metabolic pathway is highly thermodynamically favorable and, as a ...
Daniel Atkinson showed that when the energy charge increases from 0.6 to 1.0, the citrate lyase and phosphoribosyl pyrophosphate synthetase, two enzymes controlling anabolic (ATP-demanding) pathways are activated, [2] [3] while the phosphofructokinase and the pyruvate dehydrogenase, two enzymes controlling amphibolic pathways (supplying ATP as ...