Phosphofructokinase is inhibited by H+ ions and hence the rate of gly...
Inhibition of Phosphofructokinase by H+ Ions
- Phosphofructokinase is a key enzyme in the glycolysis pathway that catalyzes the conversion of fructose-6-phosphate to fructose-1,6-bisphosphate.
- It is an allosteric enzyme, meaning its activity can be influenced by the binding of small molecules at a site other than the active site.
- H+ ions, or protons, can bind to specific regulatory sites on phosphofructokinase, inhibiting its activity.
Effect of pH on the Rate of Glycolysis
- When the pH of the cellular environment falls, the concentration of H+ ions increases.
- As the concentration of H+ ions increases, more of these ions bind to the regulatory sites on phosphofructokinase, inhibiting its activity.
- This inhibition of phosphofructokinase leads to a decrease in the rate of glycolysis.
Therefore, the correct answer is B: decreases when pH falls significantly. The rate of glycolysis decreases when pH falls due to the inhibitory effect of H+ ions on the activity of phosphofructokinase.
Phosphofructokinase is inhibited by H+ ions and hence the rate of gly...
Phosphofructokinase Inhibition by H+ Ions and its Effect on Glycolysis Rate
Phosphofructokinase (PFK) is a key regulatory enzyme in the glycolysis pathway, which converts glucose into pyruvate. It plays a crucial role in controlling the rate of glycolysis, and its activity can be modulated by various factors, including pH.
Effect of pH on Phosphofructokinase Activity
- PFK is allosterically regulated by several molecules, including ATP, ADP, and pH.
- Under normal physiological conditions, the pH inside the cell is slightly alkaline (around pH 7.2-7.4), which is optimal for PFK activity.
- However, when the pH falls (becomes more acidic), it can significantly affect the enzyme's activity.
Inhibition of Phosphofructokinase by H+ Ions
- H+ ions are known to inhibit PFK activity. As the pH decreases, the concentration of H+ ions increases.
- The inhibition of PFK by H+ ions occurs due to the effect of pH on the enzyme's structure and active site.
- The presence of excess H+ ions alters the electrostatic interactions within the enzyme molecule, leading to conformational changes that affect its catalytic activity.
- These conformational changes reduce the affinity of PFK for its substrate, fructose-6-phosphate, and decrease the enzyme's activity.
Effect of Phosphofructokinase Inhibition on Glycolysis Rate
- Glycolysis is a series of enzymatic reactions that generate ATP and pyruvate from glucose.
- PFK is the rate-limiting enzyme in glycolysis, meaning that its activity determines the overall rate of the pathway.
- When PFK is inhibited by H+ ions at lower pH levels, the enzymatic conversion of fructose-6-phosphate to fructose-1,6-bisphosphate is slowed down.
- This inhibition of PFK decreases the rate of glycolysis, as the key regulatory step is hindered.
- Consequently, the production of ATP and pyruvate from glucose is reduced, leading to a decrease in overall energy production in the cell.
Conclusion
In conclusion, phosphofructokinase is inhibited by H+ ions, leading to a decrease in the rate of glycolysis when the pH falls significantly. The inhibition of PFK by H+ ions alters the enzyme's structure and reduces its affinity for the substrate, resulting in a slowdown of the glycolytic pathway. This regulatory mechanism helps to maintain cellular energy production and metabolic balance under different physiological conditions.
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