Enzyme Kinetics and Allosteric Regulation

Very Hard Biochemistry Enzymes

A research team is studying a newly discovered enzyme that catalyzes the conversion of substrate A into product B while also exhibiting allosteric regulation. They find that the enzyme's activity is markedly influenced by its substrate concentration and the presence of a specific inhibitor which binds to the allosteric site rather than the active site. They want to evaluate the effects of enzyme kinetics in different environments.

Which of the following statements correctly describes the behavior of the newly discovered enzyme when exposed to both increased substrate concentrations and the allosteric inhibitor?

The maximum velocity (Vmax) of the reaction will increase while Km will decrease.

The enzyme will be less effective at low substrate concentrations regardless of the presence of the inhibitor.

The presence of the allosteric inhibitor will increase the apparent Km of the enzyme.

Substrate saturation will not be achieved, preventing the enzyme from reaching Vmax.

Hint

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