Enzyme Inhibitors | Mechanisms, Michaelis-Menten Plots, & Effects

The video tutorial provides an overview of enzyme inhibitors, focusing on competitive, uncompetitive, and noncompetitive types. It explains how these inhibitors affect the kinetic parameters KM and VMAX, using Michaelis-Menten plots to illustrate their impact on enzyme efficiency. Competitive inhibitors increase KM without changing VMAX, uncompetitive inhibitors decrease both KM and VMAX, and noncompetitive inhibitors only decrease VMAX. The tutorial aims to clarify the differences between these inhibitors and their effects on enzyme activity.

What are the two main kinetic parameters affected by enzyme inhibitors?

• VMAX and Kcat

• Kcat and Kd

• KM and Kcat

• KM and VMAX

How do competitive inhibitors affect the Michaelis-Menten plot?

• They decrease VMAX and increase KM

• They increase both KM and VMAX

• They increase KM without changing VMAX

• They decrease both KM and VMAX

Where do competitive inhibitors bind on the enzyme?

• At the allosteric site

• At the substrate site

• At the active site

• At the regulatory site

What is the effect of uncompetitive inhibitors on KM and VMAX?

• They increase both KM and VMAX

• They decrease both KM and VMAX

• They do not affect KM or VMAX

• They increase KM and decrease VMAX

How do uncompetitive inhibitors bind to the enzyme?

• They bind at the active site

• They bind at a site distinct from the active site

• They bind at the substrate site

• They bind at the regulatory site

What is the primary effect of noncompetitive inhibitors on enzyme kinetics?

• They increase KM and decrease VMAX

• They decrease VMAX without affecting KM

• They increase both KM and VMAX

• They do not affect KM or VMAX

Where do noncompetitive inhibitors typically bind on the enzyme?

• At the substrate site

• At the active site

• At the regulatory site

• At a site distinct from the active site