Enzyme X pH Activity Interpretation Quiz

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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?

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?

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?

[S] at which V=1/2 Vmax Signup and view all the answers

How does the rate of a reaction change over time as substrate is depleted?

Decreases steadily Signup and view all the answers

What is a likely interpretation of Enzyme X's sharp decrease in activity when the pH goes much lower than 6.4?

A Histidine residue on the enzyme is involved in the reaction Signup and view all the answers

What does a good transition-state analog do?

Binds to the enzyme more tightly than the substrate Signup and view all the answers

What does a transition-state analog resemble?

Resembling the transition-state structure of the normal enzyme-substrate complex Signup and view all the answers

What can serve as a substrate for a reaction with the terminal phosphate of ATP catalyzed by hexokinase?

Carbohydrates Signup and view all the answers

Which property generally increases when pH increases?

Enzyme specific activity Signup and view all the answers

What is a limitation for Enzyme X's activity?

Concentration of substrate supplied Signup and view all the answers

What is a characteristic that differentiates enzymes from other catalysts?

Usually display specificity toward a single reactant Signup and view all the answers

What does the concept of 'induced fit' refer to in enzyme-substrate binding?

Substrate binding may induce a conformational change in the enzyme, which then brings catalytic groups into proper orientation Signup and view all the answers

What is the benefit of measuring the initial rate (V) of a reaction?

Changes in [S] are negligible, so [S] can be assumed as constant Signup and view all the answers

What happens to the equilibrium point of a reaction when a catalyst is introduced?

The reaction equilibrium shifts to the right Signup and view all the answers

Which statement about enzymes' influence on activation energy is correct?

Enzymes decrease the activation energy required for a reaction Signup and view all the answers

What is true regarding the consumption of enzymes during a reaction?

Enzymes remain chemically unchanged and are not consumed in the reaction Signup and view all the answers

Enzyme X pH Activity Interpretation Quiz

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