Enzyme Inhibitors

• Enzyme inhibitors are molecules that interact with enzymes to regulate their activities.
• They are vital for cellular control and pharmaceutical development of Enzyme Inhibitors, targeting specific enzymatic pathways to treat diseases.
• Inhibitors can be classified based on their reversibility and mode of action.

Reversible Enzyme Inhibitors

• Reversible inhibitors temporarily bind to enzymes and are classified into three types:

1. Competitive Enzyme Inhibitors

   • Mechanism: Compete with the substrate for the active site due to structural similarity.
   • Overcoming Inhibition: Increasing substrate concentration can reduce inhibition.
   • Example: Methotrexate inhibits dihydrofolate reductase, used in cancer and autoimmune disease treatment.

2. Non-competitive Inhibitors

   • Mechanism: Bind to an allosteric site, causing conformational changes that reduce enzyme function.
   • Example: Allopurinol inhibits xanthine oxidase, reducing uric acid production to treat gout and prevent kidney stones.

3. Uncompetitive Inhibitors

   • Mechanism: Bind exclusively to the enzyme-substrate complex, preventing product release.
   • Example: Lithium ions inhibit inositol monophosphates, used in managing bipolar disorder.

Irreversible Inhibitors

• Irreversible inhibitors bind covalently to enzymes, causing permanent deactivation.
• They often target critical amino acids in the active site.
• Example: Aspirin irreversibly inhibits cyclooxygenase (COX) enzymes by acetylating a serine residue, blocking prostaglandin synthesis, and providing anti-inflammatory, analgesic, and antipyretic effects.

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