Need help, please. In the following reaction, a molecule of ATP bound to the enzyme transfer a phosphate tofructose according to the reaction shown belowenzyme-ATP + fructose fructose-phosphate + enzyme-ADPWhen this enzyme catalyze the reaction, the activation energy barrier changes by 27.6kJ/mol for the forward rate constant. How will the activation energy barrier change for thereverse rate constant in this catalyzed reaction?Select one:a. The change in the activation energy barrier is less than 27.6 kJ/molb. The change in the activation energy barrier is greater than 27.6 kJ/molC. The change in the activation energy barrier is the same: 27.6 kJ/mol

Correct Option: b. The change in the activation energy barrier is greater than 27.6 kJ/molExplanation: Enzymes function as catalysts by lowering the activation energy required for a chemical reaction .In the given reaction, the enzyme facilitates the transfer of a phosphate from ATP to fructose. The fact that the activation energy barrier changes by 27.6 kJ/mol for the forward rate constant indicates that the enzyme is effectively reducing the energy required to initiate the reaction.For the reverse reaction, the enzyme still influences the activation energy barrier, but in this case, it works in the opposite direction. The enzyme facilitates the reverse reaction by lowering the activation energy required for the reverse rate constant. Since the forward and reverse reactions involve the same catalytic process, the change in activation energy for the reverse rate constant is typically greater than the change for the forward rate constant.Hence, option b. The change in the activation energy barrier is greater than 27.6 kJ/mol is correct.Incorrect Option: a. The change in the activation energy barrier is less than 27.6 kJ/molThis option is incorrect because, as explained above, enzymes influence both the forward and reverse reactions by altering the activation energy barrier. The catalysis provided by the enzyme affects both directions, and the change in activation energy for the reverse reaction is generally greater than the change observed for the forward reaction.Option c. The change in the activation energy barrier is the same: 27.6 kJ/molThis option is incorrect in the context of enzymatic reactions. When an enzyme catalyzes a reaction, it influences both the forward and reverse reactions, but the changes in activation energy barriers are not necessarily the same for these two directions.In a catalyzed reaction, the enzyme lowers the activation energy required for both the forward and reverse reactions, making it easier for the reaction to proceed in either direction. However, the degree of reduction in activation energy may differ for the forward and reverse reactions.Option c suggests that the change in the activation energy barrier is the same (27.6 kJ/mol) for both the forward and reverse rate constants. This is inconsistent with how enzymes typically function. Enzymes often exhibit specificity in their catalytic effects, and the changes in activation energy are usually tailored to facilitate the reaction in both directions but not necessarily to the same extent.The correct answer is **b. The change in the activation energy barrier is greater than 27.6 kJ/mol**. To understand this, let's delve into the principles of enzymatic catalysis and its impact on both forward and reverse reactions.Enzymes function as catalysts by providing an alternative reaction pathway with a lower activation energy, facilitating the conversion of substrates into products. In the given scenario, the enzyme catalyzes the transfer of a phosphate from ATP to fructose. The decrease in activation energy by 27.6 kJ/mol for the forward rate constant implies that the enzyme makes it energetically more favorable for this reaction to occur.When considering the reverse reaction (fructose-phosphate to enzyme-ADP), the enzyme still plays a role in lowering the activation energy barrier. However, the reduction in activation energy for the reverse rate constant is often greater than that for the forward reaction. This is a consequence of the enzyme's ability to stabilize the transition state, facilitating both the forward and reverse reactions but potentially having a more pronounced effect on the reverse direction.Enzymes do not alter the equilibrium constant of a reaction, but they do impact the kinetics by influencing activation energies. The catalytic activity of the enzyme is bidirectional, affecting both the forward and reverse reactions, but the magnitude of change in activation energy is not symmetric. Therefore, option **b. The change in the activation energy barrier is greater than 27.6 kJ/mol** accurately reflects the typical behavior of enzymes in catalyzing reversible reactions.