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Enzyme Inhibition:

Enzyme inhibition is a process where a molecule (inhibitor) binds to an enzyme, reducing its activity. Inhibition can be reversible or non-reversible.

Reversible Inhibition:

Reversible inhibition occurs when the inhibitor binds to the enzyme through weak intermolecular forces, allowing the enzyme to regain its activity once the inhibitor is removed.

Competitive Inhibition:

Competitive inhibition occurs when the inhibitor competes with the substrate for binding to the active site of the enzyme. The inhibitor has a similar shape to the substrate, allowing it to bind to the active site, thereby reducing enzyme activity.

Characteristics:
Inhibitor binds to active site
Increases Km (Michaelis constant)
Does not affect Vmax (maximum velocity)
Can be overcome by increasing substrate concentration

Non-Competitive Inhibition:

Non-competitive inhibition occurs when the inhibitor binds to a site other than the active site, altering the enzyme's conformation and reducing its activity.

Characteristics:
Inhibitor binds to allosteric site
Decreases Vmax
Does not affect Km
Cannot be overcome by increasing substrate concentration

Non-Reversible Inhibition:

Non-reversible inhibition occurs when the inhibitor forms a covalent bond with the enzyme, permanently inactivating it.

Characteristics:
Inhibitor forms covalent bond with enzyme
Irreversibly inactivates enzyme
Cannot be overcome by increasing substrate concentration or removing inhibitor

Examples:

Competitive inhibition: succinate dehydrogenase inhibited by malonate
Non-competitive inhibition: alkaline phosphatase inhibited by phosphate ions
Non-reversible inhibition: acetylcholinesterase inhibited by organophosphates


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