Enzyme Catalysis

AP Biology· difficulty 3/5

With inhibitor Y, Vmax is reduced but Km is unchanged.

Inhibitor Y most likely acts via:

A
$Noncompetitive inhibition at an allosteric site$
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B
$Competitive binding to the active site$
C
$Substrate-level activation$
D
$Increased substrate affinity at the active site$

Explanation

Noncompetitive inhibitors bind an allosteric site, decreasing functional enzyme. This lowers Vmax while leaving Km (affinity) unchanged.

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