Irreversible enzyme inhibitor

Irreversible enzyme inhibitors are a type of enzyme inhibitor that binds to enzymes in a permanent manner, often with covalent bonds. They are different from reversible inhibitors, which bind to enzymes temporarily.

Mechanism of Action

Irreversible inhibitors work by permanently binding to an enzyme, which prevents the enzyme from functioning. This is often achieved through the formation of a covalent bond with the enzyme, which is a strong type of chemical bond that is not easily broken. This means that the enzyme is permanently deactivated and can no longer catalyze reactions.

Types of Irreversible Inhibitors

There are several types of irreversible inhibitors, including:

• Active site-directed inhibitors: These inhibitors bind to the active site of the enzyme, which is the region of the enzyme where the substrate binds and the reaction takes place.
• Suicide inhibitors (also known as mechanism-based inhibitors): These inhibitors bind to the enzyme and are initially processed by the enzyme as if they were a substrate. However, during this process, the inhibitor is converted into a reactive form that covalently binds to the enzyme, permanently deactivating it.

Examples of Irreversible Inhibitors

Some examples of irreversible inhibitors include:

• Aspirin: Aspirin irreversibly inhibits the enzyme cyclooxygenase, which is involved in the production of prostaglandins and thromboxanes.
• Penicillin: Penicillin irreversibly inhibits the enzyme transpeptidase, which is involved in the synthesis of bacterial cell walls.

Clinical Significance

Irreversible inhibitors have important clinical applications. They are often used as drugs to treat various diseases. For example, aspirin is used as an anti-inflammatory and antithrombotic drug, while penicillin is used as an antibiotic.

See Also

• Enzyme inhibitor
• Reversible inhibitor
• Active site
• Suicide inhibitor
• Aspirin
• Penicillin

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