This problem feature chymotrypsin, which catalyzes the hydrolysis of esters. We

Question

This problem feature chymotrypsin, which catalyzes the hydrolysis of esters. We will focus on esters that have the formula R' -O-CO CH_3. A commonly used substrate is p-nitrophenyl acetate, which is shown on the right: The following mechanism (also in the figure below) has been proposed for chymotrypsin: E + S implies ES right arrow E - Acyl + p- notrophenolate E-Acyl right arrow E + acetate The rate determining step is assumed to be the reaction leading to the formation of E-Acyl. Apply the steady-state approximation to E-Acyl and show that V_0 = (k_ cat [E]_ 0 [S])/(K_ M + [S]) K_ cat and K_M should be expressed as a function of K_s, k_ 2, and k_ 3. Note: Your solution must be detailed and presented in an organized and legible manner. Provide the mathematical equations and relationships that you are using to solve this question. Steady-state data collected for chymotrypsin are provided to you: Are these numbers consistent with the proposed mechanism, including the formation of a common intermediate? Explain your answer. Wild-type chymotrypsin acting on a peptide substrate exhibits burst kinetics. Is the late limiting step still the formation of E-acyl? Explain your answer. If the rate limiting step has changed, give a plausible explanation for the change.

Explanation / Answer

Solution:

b) on considering the given data of kcatalyst the ethyl formation is quick (not stable) in the other hand p-nitrophenyl is taking more time meanwhile the concentration of all the components is 5 which exhibits atable reversible process. Therefore the given data are valid as they shows strong stability in reversible reaction.

c) No, the rate limiting step initiates the reversible process, in order to get the E-acyl product formation, the rate determining of k1 must be enhanced to proceed to k2 kinetics this can be achieved by altering the activity of wild-catalyst.

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