In uncompetitive inhibition, the inhibitor can bind to the enzyme only after the substrate binds first. (T/F)

True

Explanation:

In an uncompetitive inhibition, initially the substrate [S] binds to the active site of the enzyme [E] and forms an enzyme-substrate activated complex [ES].

The inhibitor molecule then binds to the enzyme - substrate complex [ES], resulting in the formation of [ESI] complex, thereby inhibiting the reaction.

This inhibition is called uncompetitive because the inhibitor does not compete with the substrate to bind on the active site of the enzyme.

Therefore, in an uncompetitive inhibition, the inhibitor molecule can not bind on the active site of the enzyme directly. The inhibitor can only bind to the enzyme-substrate complex formed.