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Enzyme inhibition is the process of reducing or stopping the activity of an enzyme by the presence of certain
molecules called inhibitors. There are two main types of enzyme inhibition: reversible and irreversible.

Reversible inhibition occurs when the inhibitor binds to the enzyme through weak, non-covalent
interactions, such as hydrogen bonds, ionic bonds, or hydrophobic interactions. This means that the
inhibitor can be removed from the enzyme, allowing it to regain its activity. Reversible inhibitors can be
classified into four subtypes: competitive, non-competitive, uncompetitive, and mixed inhibitors,
depending on how and where they bind to the enzyme or the enzyme-substrate complex.
Irreversible inhibition occurs when the inhibitor binds to the enzyme through strong, covalent bonds,
such as disulfide bonds, alkylation, or acylation. This means that the inhibitor permanently modifies the
enzyme, rendering it inactive unless the bond is broken. Irreversible inhibitors can be classified into two
subtypes: suicide inhibitors and allosteric inhibitors, depending on whether they bind to the active site or
a different site of the enzyme.

Enzyme inhibition is an important biological phenomenon that regulates various metabolic pathways, protects
cells from harmful enzymes, and serves as a potential therapeutic strategy. For more information, you can
check out these web pages:

Difference Between Reversible and Irreversible Enzyme Inhibition

Enzyme Inhibition - Definition, Types, Mechanism, Examples
Enzyme Inhibition - Chemistry LibreTexts