Enzyme Substrate Binding Theories Quiz

Which type of reversible inhibitor has a molecular structure similar to the normal substrate of the enzyme?

What type of inhibitor binds to the active site of an enzyme and competes with substrate molecules?

In the induced-fit model, what changes when the substrate binds to the enzyme?

Which theory describes the perfect fit between the enzyme's active site and the substrate?

What is the name for enzymes that catalyze the same reaction but differ in physical and chemical properties?

Which equation describes the rate of enzymatic reactions as a function of substrate concentration?

What model suggests that the active site of an enzyme forms a complementary shape to the substrate after the substrate has been bound?

Which theory explains that the active site changes shape as it interacts with the substrate?

In the lock and key theory, what does the active site of the enzyme resemble in terms of fitting with the substrate?

In the Michaelis-Menten equation, what does Km represent?

What happens when [S] is much less than Km in terms of the velocity of the reaction?

Which theory suggests that once the substrate is fully locked into position, catalysis can begin?

What does the Vmax in the Michaelis-Menten equation signify?

What is the main limitation of the lock and key theory in explaining enzyme-substrate binding?

How does the induced-fit model differ from the lock and key theory in terms of enzyme-substrate binding?

Which complex is formed when an enzyme reversibly combines with its substrate according to Michaelis and Menten?

What conclusion can be drawn about the relationship between enzyme concentration and reaction rate in Michaelis-Menten kinetics?

What aspect of the enzyme changes upon substrate binding in the induced-fit model?