Effect of Competitive Inhibition on Enzyme Kinetics

Very Hard Biochemistry Enzymes

Enzymes play a crucial role in biological systems by catalyzing biochemical reactions. Each enzyme has a specific mechanism and regulation that dictates its activity in metabolic pathways. Consider a hypothetical enzyme that follows Michaelis-Menten kinetics and has a Km (Michaelis constant) of 5 mM. In the presence of a competitive inhibitor that has a Ki (inhibition constant) of 10 mM, what effect will this inhibitor have on the enzyme's activity when analyzing its Vmax (maximum rate of reaction) and apparent Km?

Which of the following statements is correct regarding the impact of the competitive inhibitor on the enzyme's kinetic properties?

The competitive inhibitor decreases the Vmax but increases the apparent Km.

The competitive inhibitor does not affect the Vmax but increases the apparent Km.

The competitive inhibitor decreases both the Vmax and apparent Km.

The competitive inhibitor increases the Vmax and decreases the apparent Km.

Hint

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