Enzyme inhibition

Enzyme Inhibition is a process that decreases the activity of an enzyme. Enzyme inhibitors are molecules that bind to enzymes and decrease their activity. Since blocking an enzyme's activity can kill a pathogen or correct a metabolic imbalance, many drugs are enzyme inhibitors.

Types of Enzyme Inhibition

There are two major types of enzyme inhibition: reversible and irreversible.

Reversible Inhibition

In reversible inhibition, the inhibitor binds to the enzyme to form an enzyme-inhibitor complex, but can be removed by dilution or dialysis. There are three types of reversible inhibition: competitive, noncompetitive, and uncompetitive.

Competitive Inhibition

In competitive inhibition, the inhibitor and the substrate compete for the same active site on the enzyme. The inhibitor resembles the substrate and can bind to the active site, preventing the substrate from binding.

Noncompetitive Inhibition

In noncompetitive inhibition, the inhibitor binds to an allosteric site, not the active site. This changes the shape of the enzyme and prevents the substrate from binding.

Uncompetitive Inhibition

In uncompetitive inhibition, the inhibitor binds to the enzyme-substrate complex, preventing the complex from releasing the products.

Irreversible Inhibition

In irreversible inhibition, the inhibitor permanently binds to the enzyme, often with covalent bonds, permanently inactivating the enzyme.

Clinical Significance

Enzyme inhibition has important clinical significance. Many drugs are enzyme inhibitors that block the activity of enzymes and can kill pathogens or correct metabolic imbalances.

See Also

• Enzyme
• Enzyme Kinetics
• Enzyme Activator
• Enzyme Induction

References

Enzyme inhibition Resources
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