Podcast
Questions and Answers
What does an inhibitor do in competitive inhibition?
What does an inhibitor do in competitive inhibition?
- Binds reversibly at the active site (correct)
- Binds at several different sites on an enzyme
- Binds only to the ES complex
- Binds covalently to the enzyme
Which statement about enzyme-catalyzed reactions is false?
Which statement about enzyme-catalyzed reactions is false?
- If enough substrate is added, the normal Vmax can be attained in the presence of a competitive inhibitor. (correct)
- The activation energy for the catalyzed reaction is the same as for the uncatalyzed reaction.
- At saturating levels of substrate, the rate is proportional to enzyme concentration.
- The Michaelis-Menten constant (Km) equals [S] at which V=1/2 Vmax.
What happens to Vmax for an enzyme-catalyzed reaction?
What happens to Vmax for an enzyme-catalyzed reaction?
- Increases in the presence of a competitive inhibitor (correct)
- Is unchanged in the presence of a uncompetitive inhibitor
What is the role of the Michaelis-Menten constant (Km) in enzyme kinetics?
What is the role of the Michaelis-Menten constant (Km) in enzyme kinetics?
How does the rate of a reaction change over time as substrate is depleted?
How does the rate of a reaction change over time as substrate is depleted?
What is a likely interpretation of Enzyme X's sharp decrease in activity when the pH goes much lower than 6.4?
What is a likely interpretation of Enzyme X's sharp decrease in activity when the pH goes much lower than 6.4?
What does a good transition-state analog do?
What does a good transition-state analog do?
What does a transition-state analog resemble?
What does a transition-state analog resemble?
What can serve as a substrate for a reaction with the terminal phosphate of ATP catalyzed by hexokinase?
What can serve as a substrate for a reaction with the terminal phosphate of ATP catalyzed by hexokinase?
Which property generally increases when pH increases?
Which property generally increases when pH increases?
What is a limitation for Enzyme X's activity?
What is a limitation for Enzyme X's activity?
What is a characteristic that differentiates enzymes from other catalysts?
What is a characteristic that differentiates enzymes from other catalysts?
What does the concept of 'induced fit' refer to in enzyme-substrate binding?
What does the concept of 'induced fit' refer to in enzyme-substrate binding?
What is the benefit of measuring the initial rate (V) of a reaction?
What is the benefit of measuring the initial rate (V) of a reaction?
What happens to the equilibrium point of a reaction when a catalyst is introduced?
What happens to the equilibrium point of a reaction when a catalyst is introduced?
Which statement about enzymes' influence on activation energy is correct?
Which statement about enzymes' influence on activation energy is correct?
What is true regarding the consumption of enzymes during a reaction?
What is true regarding the consumption of enzymes during a reaction?
