Understanding Enzyme Kinetics: Vmax and Km

Hard Biochemistry Enzymes

Consider an enzyme that catalyzes a particular biochemical reaction. This enzyme has a maximum reaction velocity (V_max) of 200 μmol/min and an apparent Michaelis constant (K_m) of 50 μM for its substrate. If the substrate concentration in the reaction mixture is increased from 25 μM to 100 μM, what will happen to the reaction rate given that the enzyme follows Michaelis-Menten kinetics?

Additionally, which of the following statements correctly describes the relationship between V_max and K_m for this enzyme?

As substrate concentration increases beyond Km, the reaction rate will approach Vmax.

Km represents the substrate concentration at which the enzyme is 50% saturated.

Vmax is unaffected by enzyme concentration.

As substrate concentration increases beyond Vmax, the reaction rate increases exponentially.

Hint

Submitted1.9K

Correct1.8K

% Correct97%