Enzyme Inhibitors

9 important questions on Enzyme Inhibitors

What is an irreversible inhibitor?

An irreversible inhibitor dissociates very slowly from its target enzyme because it has become tightly bound to the enzyme (covalently & noncovalently)

*Penicillin

What is Reversible inhibition and which forms are there?

Reversible inhibition is characterized by a rapid dissociation of the enzyme-inhibitor complex.

1. Competitive
2. Uncompetitive
3. Noncompetitive
4. Mixed

What is competitive inhibition?

The enzyme can either bind the substrate or the inhibitor, but not both.
The competitive inhibitor often resembles the substrate and binds to the active site of the enzyme, leaving it blocked for the substrate.

A competitive inhibitor diminishes the rate of catalysis by reducing the proportion of enzyme molecules bound to a substrate.

Competitive inhibition can be relieved by increasing the substrate concentration. Then the substrate successfully competes with the inhibitor for the active site.
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What is uncompetitive inhibition?

Uncompetitive inhibition is substrate-dependent inhibition; the inhibitor only binds to the enzyme-substrate complex.

Binds only to ES-complex

* cannot be overcome by the addition of more substrate

What is noncompetitive inhibition?

In noncompetitive inhibition both the inhibitor and substrate can bind simultaneously to an enzyme at different binding site.

A noncompetitive inhibitor acts by decreasing the concentration of functional enzyme rather than by diminishing the proportion of enzyme molecules that are bound to the substrate.

Decreases the turnover number.  

What is mixed inhibition?

This is when a single inhibitor both hinders the binding of substrate and decreases the turnover number of the enzymes.

What happens with the Km and Vmax when a competitive inhibitor is used?

Km is increased (more substrate is needed to obtain the same reaction rate) and the Vmax stays the same.

What is the effect of uncompetitive inhibtion on the Km and Vmax?

Km and Vmax will be lower.
Km is lower because the inhibitor binds to ES to form ESI, depleting ES.

What happens with Km and Vmax when a noncompetitive inhibitor is used?

Vmax is decreased and Km stays unchanged.

The question on the page originate from the summary of the following study material:

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