How does a noncompetitive inhibitor decrease the rate of an enzyme-catalyzed reaction?.

Chemistry

1 answer:

Stella [2.4K]3 years ago

6 0

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.

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