Enzyme Inhibitor

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Enzyme Inhibitor

An Enzyme Inhibitor (pronunciation: /ˈɛnzaɪm ɪnˈhɪbɪtər/) is a molecule that binds to an Enzyme and decreases its activity. The process of inhibiting or reducing the activity of an enzyme is known as Enzyme Inhibition.

Etymology

The term "Enzyme Inhibitor" is derived from the Greek words "en zyme" meaning "in yeast" and the Latin word "inhibitor" meaning "restrainer".

Types of Enzyme Inhibitors

There are two main types of enzyme inhibitors: Reversible Inhibitors and Irreversible Inhibitors. Reversible inhibitors bind to enzymes with non-covalent interactions such as hydrogen bonds, hydrophobic interactions, and ionic bonds. On the other hand, irreversible inhibitors bind with covalent bonds and cause permanent loss of enzymatic activity.

Mechanism of Action

Enzyme inhibitors work by binding to the active site, or to the allosteric site of the enzyme, which prevents the binding of the substrate and thus, the formation of the Enzyme-Substrate Complex. This results in the decrease or complete halt of the reaction catalyzed by the enzyme.

Clinical Significance

Enzyme inhibitors have significant therapeutic value and are often used as drugs. For example, Protease Inhibitors are used in the treatment of HIV and Hepatitis C. Angiotensin-Converting Enzyme (ACE) Inhibitors are used to treat hypertension and heart failure.

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