Homework 8 (Due 4/25/16)
- Page ID
- 47381
Name: ______________________________
Section: _____________________________
Student ID#:__________________________
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:
- the substrate concentration was doubled?
- the enzyme concentration was doubled?
- 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.