How does inhibition of an enzyme-catalyzed reaction by a competitive inhibitor differ from inhibition by a noncompetitive inhibitor?

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04-10-2019
Biology

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How does inhibition of an enzyme-catalyzed reaction by a competitive inhibitor differ from inhibition by a noncompetitive inhibitor?

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sciguy101 sciguy101 · Answer 1 · 2019-10-06T00:47:33+02:00

A competitive inhibitor is "competitive" because it binds to the same active site as the enzyme's natural substrate - the inhibitor competes with the substrate to occupy the active site. This is why if you add more substrate, it can overcome the inhibition because the substrate outcompetes the inhibitor. If you have green circles and blue circles both competing to occupy a round hole, the more circles of one colour you have, the more likely that colour will be to occupy the hole.

A noncompetitive inhibitor usually binds to a part of the enzyme other than the active site. The act of it binding to this other part can induce a shape change of the active site such that it will no longer be able to bind to its natural substrate. If you have a circular substrate for a round hole, but then the shape of the hole is changed to a triangle when the inhibitor binds, the circular substrate won't be able to interact with the enzyme no matter how much of it you have.

luisvaschetto luisvaschetto · Answer 2 · 2021-10-02T02:58:23+02:00

A competitive inhibitor binds to the active site of the enzyme, thereby competing with the substrate. Conversely, a noncompetitive inhibitor does not compete with the substrate.

The binding of an inhibitor with the active site of the enzyme results in the formation of the enzyme-inhibitor complex, thereby the enzyme cannot catalyze the reaction until this inhibitor dissociates.

Km refers to the concentration of substrate required to convert half the concentration of the enzyme into the enzyme-substrate complex.

This value (Km) is inversely associated with the affinity of the enzyme for its substrate.

Vmax refers to the velocity of the reaction when the enzyme is saturated by its specific substrate.

This value (Vmax) is directly associated with enzyme concentration.

Competitive inhibition increases the Km value, whereas Vmax remains unchanged.

On the other hand, in noncompetitive inhibition, the Km value remains unchanged, but it decreases the Vmax of the enzyme.

In conclusion, a noncompetitive inhibitor binds to the enzyme in a site different from the active site, whereas a competitive inhibitor binds to the active site of the enzyme. These phenomena differentially alter the Km and Vmax values of the enzyme.

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