Question

EXTRA CREDIT 1. A pharmaceutical company has developed a new chemotherapy drug (STOP2D) which functions as an inhibitor of the enzyme Split2. This enzyme is part of a pathway that promotes cell division. Suppose that in clinical trials, some of the patients become resistant to the drug. In order to determine the mechanism of resistance, the proteome of the patients is examined and it is found that the expression of Split2 is normal; however, the levels of the substrate of Split2 are greatly increased. Patients who have not developed resistance to STOP2D, show normal levels of both the enzyme (Split2) and its substrate. Based on this information, what type of inhibitor is STOP2D? Provide a justification for your answer and explain the effect of this type of inhibitor on Km, and thus affinity of the enzyme for its substrate, as well as on Vmax (12.5 points) Answer:

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Answer 1

The competitive inhibitor binds to the active site and prevents the substrate from binding there.

The noncompetitive inhibitor binds to a different site on the enzyme; it doesn't block substrate binding, but it causes other changes in the enzyme so that it can no longer catalyze the reaction efficiently.

Explaination-

Because when no resistance was there, enzyme and substrate both are normal which means it is non competition inhibition (no increase in level of substrate unlike competitive inhibition)

And when resistance present, substrate levels increased to increase efficiency due to deformed expression of split2 by non competitive inhibition.

When a non-competitive inhibitor is added the Vmax is changed, while theKm remains unchanged.

In non-competitive inhibition, the inhibitor binds to an allosteric site and prevents the enzyme-substrate complex from performing a chemical reaction. This does not affect the Km (affinity) of the enzyme (for the substrate).