Enzyme inhibitors

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Enzyme Inhibitors

Enzyme inhibitors (/ɛnˌzaɪm ɪnˈhɪbɪtərs/) 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. They are also used as Herbicides and Pesticides.

Etymology

The term "Enzyme Inhibitor" comes from the Greek words "en zyme" meaning "in yeast", and the Latin word "inhibitor" meaning "to restrain".

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 inactivate the enzyme permanently.

Examples of Enzyme Inhibitors

Some examples of enzyme inhibitors include Aspirin, Statins, and Protease inhibitors. Aspirin works by irreversibly inhibiting the enzyme cyclooxygenase, which is involved in the production of prostaglandins and thromboxanes. Statins are a class of drugs that inhibit the enzyme HMG-CoA reductase, which plays a central role in the production of cholesterol. Protease inhibitors are used in antiretroviral therapy to inhibit the action of proteases, enzymes used by HIV to replicate.

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