Enzyme Inhibition Mechanisms

The video tutorial explains enzyme inhibition, focusing on competitive, non-competitive, and uncompetitive inhibition. It describes how inhibitors interact with enzymes and substrates, affecting enzyme activity and product formation. The tutorial also covers graphical analysis, illustrating how different inhibition types impact Vmax and Km values.

What is the main characteristic of competitive inhibition?

• Inhibitor competes with the substrate for the active site.

• Inhibitor binds to a different site on the enzyme.

• Inhibitor binds only to the enzyme-substrate complex.

• Inhibitor does not affect the enzyme's activity.

In non-competitive inhibition, where does the inhibitor bind?

• To the active site of the enzyme.

• To the enzyme-substrate complex only.

• To a different site on the enzyme.

• To the substrate directly.

Which type of inhibition involves the inhibitor binding only to the enzyme-substrate complex?

• Competitive inhibition

• Mixed inhibition

• Non-competitive inhibition

• Uncompetitive inhibition

How does increasing substrate concentration affect competitive inhibition?

• It has no effect on the inhibition.

• It decreases the enzyme's affinity for the substrate.

• It enhances the inhibition.

• It overcomes the inhibition.

In non-competitive inhibition, what happens to Vmax?

• Vmax decreases.

• Vmax remains unchanged.

• Vmax increases.

• Vmax becomes zero.

What is the effect of uncompetitive inhibition on Km and Vmax?

• Km decreases while Vmax increases.

• Km increases while Vmax decreases.

• Both Km and Vmax decrease.

• Both Km and Vmax increase.

Which type of inhibition cannot be overcome by increasing substrate concentration?

• Competitive inhibition

• All of the above

• Non-competitive inhibition

• Uncompetitive inhibition

What does an increase in Km indicate in competitive inhibition?

• No change in enzyme affinity.

• Increased maximum velocity.

• Decreased enzyme affinity for the substrate.

• Increased enzyme affinity for the substrate.

In the context of enzyme inhibition, what does Vmax represent?

• The maximum substrate concentration.

• The maximum velocity of the reaction.

• The minimum velocity of the reaction.

• The affinity of the enzyme for the inhibitor.

Which type of inhibition is considered most unfavorable due to its effects on both Km and Vmax?

• All types are equally unfavorable

• Uncompetitive inhibition

• Non-competitive inhibition

• Competitive inhibition