195k views
24 votes
How does a noncompetitive inhibitor decrease the rate of an enzyme-catalyzed reaction?.

1 Answer

2 votes

Answer:

In fact, the inhibitor and substrate don't affect one another's binding to the enzyme at all. However, when the inhibitor is bound, the enzyme cannot catalyze its reaction to produce a product. Thus, noncompetitive inhibition acts by reducing the number of functional enzyme molecules that can carry out a reaction.

User Rickygrimes
by
3.7k points