Chemistry 2710 Review Problems

1. Consider the following enzyme inhibition data:

   

   Calculate , and .

2. Consider the following mechanism:

   

   The last reaction is a reversible conformational change leading to an inactive form of the enzyme. Is this mechanism kinetically distinguishable from the Michaelis-Menten mechanism?

3. Use the steady-state approximation to derive a rate law for the mechanism

   

   The first step is an instance of cooperative binding: The binding of n molecules of S really happens one molecule at a time, but the first molecule to bind greatly increases the probability that the next will bind so that, on normal measurement time scales, it appears that all n molecules bind simultaneously.

   Write your rate law in a form similar to the Michaelis-Menten equation. Describe a graphical method for extracting the constants which appear in your rate equation.

4. For a certain enzyme reaction which follows the Michaelis-Menten rate law, the Michaelis constant of the substrate is while the Michaelis constant of the product (i.e. the Michaelis constant for the reverse reaction) is . The maximum reaction velocity for the forward reaction is . The equilibrium constant for the reaction is . Calculate the values of all the rate constants assuming that the reaction proceeds by the simple Michaelis-Menten mechanism.