Question

what happens to the values of $v_{max(app)}$ and $k_{m(app)}$ in the presence of a noncompetitive inhibitor, respectively?
you can click the view image button to find information to help answer this question.
a) increased; unchanged
b) decreased; unchanged
c) decreased; decreased
d) increased; decreased

Explanation:

Noncompetitive inhibitors bind to an enzyme at a site separate from the active site, reducing the enzyme's catalytic activity without affecting its affinity for the substrate. $V_{max(app)}$ (apparent maximum reaction rate) decreases because fewer functional enzyme-substrate complexes can form product. $K_{m(app)}$ (apparent Michaelis constant, a measure of substrate affinity) remains unchanged since the inhibitor does not interfere with substrate binding.

Answer:

b) Decreased; unchanged