Homework 8 (Due 4/25/16)

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Name: ______________________________

Section: _____________________________

Student ID#:__________________________

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Q8.1

If your student colleagues argues that a catalysts affects only the rate of only one direction of a reaction. Explain why he is correct or not.

Q8.2

The substrate N-acetylglycine ethyl ester can be catalyzed by the enzyme carbonic anhydrase. This enzyme has a turnover rate of 30,000 s^-1. Determine how long it will take carbonic anhydrase to cleave the substrate.

Q8.3

Is it appropriate to use the rapid equilibrium scheme to model the kinetics of a catalyzed reaction with the following rate constants?

$$ k_1 = 7 \times 10^7\ M^{-1}\ s^{-1} \]

$$ k_{-1} = 8 \times 10^5\ s^{-1} \]

$$ k_2 = 5 \times 10^4\ s^{-1} \]

HInt: Compare $K_s$ vs. $K_M$ for the standard enzyme kinetics model.

Q8.4

After reading 3.3: Chymotrypsin: A Case Study answer these questions

Speculate on how the catalytic rate constant can be determined from the measured kinetics.
How can product be consistently produced if the rate of change of the ES complex is 0?
How would the rate of product formation change if:
1. the substrate concentration was doubled?
2. the enzyme concentration was doubled?
3. The reaction was carried out in deuterated water (D₂O) instead of H₂O (comment qualitatively)?
Explain the role of hydrogen bonding in protein hydrolysis catalyzed by chymotrypsin.
What would the kinetics look like if the reaction proceeded via a steady-state mechanism instead of pre-equilibrium.

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