Question

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

Explanation:

Competitive inhibitors bind to the active site of an enzyme, competing with the substrate. Adding excess substrate can overcome this inhibition, so the maximum reaction rate ($V_{max(app)}$) remains unchanged. However, the inhibitor reduces the enzyme's apparent affinity for the substrate, which increases the apparent Michaelis constant ($K_{m(app)}$), as more substrate is needed to reach half the maximum rate.

Answer:

d) Unchanged; increased