Question

what happens to the values of $v_{max(app)}$ and $k_{m(app)}$ in the presence of a uncompetitive inhibitor, respectively?
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a) unchanged; decreased
b) decreased; decreased
c) increased; unchangedd) decreased; increased

Explanation:

Uncompetitive inhibitors bind only to the enzyme-substrate (ES) complex. This reduces the effective concentration of functional enzyme-substrate complexes available to form product, which lowers the apparent maximum reaction velocity ($V_{max(app)}$). Additionally, since the inhibitor stabilizes the ES complex, it appears as if the enzyme has a higher affinity for the substrate, which decreases the apparent Michaelis constant ($K_{m(app)}$). Both values decrease.

Answer:

b) Decreased; decreased