a. ATP binds to the allosteric site as an inhibitor, decreasing PFK‑1 activity. b. ATP binds to PFK‑1 at the catalytic site as a competitive inhibitor, decreasing PFK‑1 activity. c. ATP binds to the allosteric site as an activator, increasing PFK‑1 activity. d. ATP binds to the catalytic site as a substrate, increasing PFK‑1 activity.

Question: PFK-1converts fructose 6-phosphate to fructose 2,6-bisphosphate.is allosterically inhibited by citrate.is indirectly stimulated by glucagon in liver.is part of the same polypeptide chain as FBPase-1.

Phosphofructokinase (PFK-1) is ____ when ATP levels are low, and ____ when ATP levels are high. a Activated; inhibited b Inhibited; inhibited c Inhibited; activated d Activated; activated Which of the following reactions is the most

QUESTION 7 Phosphofructokinase (PFK-1) is ____ when ATP levels are low, and ____ when ATP levels are high. O Activated; inhibited O Inhibited; inhibited Inhibited, activated O Activated, activated QUESTION 8 Which of the following reactions is the most exergonic? O Hydrolysis of ATP O All of the reactions are equally exergonic.

Under standard conditions, the PFK-1 reaction reaches equilibrium when the concentrations of all products and reactants are equal. In heart tissue, the PFK-1 reaction will be driven toward product formation. The PFK-1 reaction in heart tissue does not reach equilibrium. In heart tissue, the PFK-1 products are more abundant than reactants.

Phosphofructokinase-1 (PFK-1) is one of the most important regulatory enzymes of glycolysis. Your laboratory experiments with mice model indicates that PFK1 is allosterically inhibited by high levels of ATP but AMP reverses the inhibitory action of ATP. Therefore, the activity of the enzyme increases when the cellular ATP/AMP ratio is lowered.

A.ATP is a suicide inhibitor of PFK-1. B. ATP binds to the active site of PFK-1 only at high concentrations. C.ATP binds to an allosteric site on PFK-1 (at high concentrations) and raises the K m of fructose-6-phosphate (F6P). D.ATP binds to the active site PFK-1 and prevents fructose-6-phosphate (F6P) from binding. E.ATP binds to an allosteric ...

Phosphofructokinase (PFK-1) is one of the most regulated enzymes in metabolism. Based on all of the principles we have learned in this class, which of the following would be most likely to be an allosteric activator of PFK-1? glucose CO 2 Acetyl CoA Pyruvate

Case 18 Purification of Phosphofructokinase 1-C Focus concept The purification of the Cimaryme of PFK-1 is presented and the kinetic properties of the purified czyme are examined Prerequisites • Protein purification techniques • Enzyme kinetics and inition • The glycolytic pathway Background In this case, Foe and Kempparified the serme …

Question: The graph shows the effect of ATP on the allosteric enzyme phosphofructokinase-1 (PFK-1).For a given concentration of fructose 6-phosphate, the PFK-1 activity increases with increasing concentrations of ATP, but thereis a point beyond which increasing the concentration of ATP inhibits the enzyme.How does ATP regulate the activity of PFK-1?ATP binds to the