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Exam #2; CHE 310 || Already Graded A+.

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  • ; CHE 310 ||
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  • ; CHE 310 ||

Linweaver-Burk plots can be used to examine which of the following (select all that apply)? A. The type of inhibitor introduced into a reaction system B. The MM constant of a reaction C. The VMAX of a reaction D. The order of a reaction correct answers A,B,C Kcat is equal to which of the fol...

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  • October 31, 2024
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  • ; CHE 310 ||
  • ; CHE 310 ||
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Exam #2; CHE 310 || Already Graded A+.
Linweaver-Burk plots can be used to examine which of the following (select all that apply)?
A. The type of inhibitor introduced into a reaction system
B. The MM constant of a reaction
C. The VMAX of a reaction
D. The order of a reaction correct answers A,B,C

Kcat is equal to which of the following?
A. Maximum velocity of the reaction
B. Affinity of enzyme for substrate
C. The relationship between catalytic rate and substrate-binding affinity
D. The number of substrate molecules converted to product per unit time correct answers D

Increasing the temperature (Kelvin) in a system increases the likely hood of which of the
following (select all that apply)?
A. Decreases the chances of a catalyzed reaction occurring
B. Decreasing collisions between molecules
C. Increasing energy
D. Increases the chances of a catalyzed reaction failing correct answers A, C, D

Enzymes have identical active sites to every other enzyme.
True
False correct answers False

Enzymes alter what energetic principles of a chemical reaction?
A. Increase the change in standard free energy of a reaction
B. Increase the activation energy of a reaction
C. Decrease the change in standard free energy of a reaction
D. Decrease the activation energy of a reaction correct answers D

Of the molecules below which are water soluble vitamins?
A. Vitamin A
B. Vitamin D
C. Ascorbic acid
D. Thiamine correct answers C, D

All enzymes function "best" at the same temperature and pH.
True
False correct answers False

The Michaelis-Menten constant for a given enzyme-substrate interaction describes which of the
following?
A. Affinity of enzyme for substrate
B. Maximum velocity of the reaction
C. The number of substrate molecules converted to product per unit time

, D. The relationship between catalytic rate and substrate-binding affinity correct answers A

Apoenzymes have all necessary cofactors to allow them to function properly.
True
False correct answers False

Which of the following apply to characteristics of enzymes (select all that apply)?
A. Catalyze forward reactions only of reversible reactions
B. Subject to regulatory mechanisms
C. Change a reaction equilibrium's Keq
D. Decrease reaction rates
E. Bind the product of a reaction more tightly than transition state of a reactive substrate
F. Required to be present in high concentrations correct answers B

The velocity of a reaction is affected by the rate of the depletion of reactants and the formation of
products
True
False correct answers True

The calculated delta G of a reaction can inform us of the rate of a reaction.
True
False correct answers False

Allosteric modulation of an enzyme allows which of the following to occur (select all that
apply)?
A. Produce more products as a reaction proceeds forward
B. Increase reaction rate
C. Produce less products as a reaction proceeds forward
D. Decrease reaction rate correct answers All of the above

Kcat/KM defines which of the following?
A. The number of substrate molecules converted to product per unit time
B. Maximum velocity of the reaction
C. Affinity of enzyme for substrate
D. The relationship between catalytic rate and substrate-binding affinity correct answers D

Which of the following qualities of enzymes and their active sites cannot function together to
catalyze a chemical reaction?
A. Control over proximity/orientation of a substrate and electrostatic effects
B. Electrostatic effects and acid/base catalysis
C. None of the above
D. Acid/base catalysis and covalent catalysis correct answers C

Which of the following dissociation constants represent a more tightly bound enzyme-substrate
complex?
A. 144 x 10-4

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