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Interact with specific sites on enzymes and can prevent the binding of enzyme to substrate or alter the catalytic activity. Example: EDTA inhibits metalloproteases by chelating metal ions.

Binds to the enzyme and reduces its catalytic efficiency without fully inactivating it. Example: Statins partially inhibit HMG-CoA reductase, leading to decreased cholesterol synthesis.

Binds to an allosteric site causing change in enzyme shape and function. Substrate can still bind but reaction is less effective. Example: Chloramphenicol (inhibits peptidyl transferase).

Initially binds to the enzyme loosely, but after a slow conformational change, it forms a tight and stable complex, leading to prolonged inhibition. Example: Methotrexate after prolonged administration.

A small peptide that mimics a protein or peptide substrate of an enzyme, which then competitively inhibits the enzyme. Example: Protease inhibitors used in HIV treatment, such as saquinavir.

Binds to the active site and competes with the substrate, preventing its binding. Increase in substrate can overcome inhibition. Example: Methotrexate (inhibits dihydrofolate reductase).

Forms a covalent bond with an enzyme, causing permanent inactivation. Example: Aspirin (acetylates and inhibits cyclooxygenase).

Product of an enzymatic reaction inhibits the enzyme that produced it, providing negative feedback to regulate enzymatic activity. Example: ATP is a product inhibitor of hexokinase.

A compound that increases the activity of an enzyme, typically by binding to an allosteric site leading to a conformation that has higher catalytic activity. Example: Activators of glucokinase for diabetes treatment.

Irreversibly inactivates the enzyme by forming a stable covalent bond, often with a functional group in the active site. Example: Aspirin acetylates serine residue in cyclooxygenase.

Binds only to the enzyme-substrate complex, locking the substrate in place and preventing the reaction. Example: Lithium ions (inhibit inositol monophosphatase).

Phosphorylation alters the conformation of the enzyme and can decrease its activity. Example: Kinase inhibitors such as lapatinib block enzymatic activity by preventing phosphorylation.

Binds to enzymes transiently, possibly at the active site or allosteric site without destroying enzymatic activity. Can be competed away by substrate or removed by dialysis. Example: Imatinib (inhibits tyrosine kinase).

Binds to an allosteric site different from the active site. This results in the conformational change of the enzyme, reducing its activity. Example: Ribonucleotide reductase is inhibited by dATP.

Mimics the transition state of a substrate in an enzymatic reaction. Binds very tightly to the enzyme, preventing the actual substrate from binding. Example: Allopurinol (inhibits xanthine oxidase).

End product of a metabolic pathway inhibits an enzyme that acts earlier in the pathway. Example: Threonine deaminase is inhibited by isoleucine.

Binds to the enzyme as a substrate and is initially processed, but ultimately results in irreversible enzyme inactivation. Example: Penicillin (inhibits transpeptidase).

Also known as a 'suicide inhibitor', it undergoes partial transformation by the enzyme before inactivating it. Example: 5-fluorouracil (converted by thymidylate synthase into an inhibitor).

Binds to an enzyme with or without a substrate at different sites. It affects both the substrate binding and the turnover rate of the enzyme. Example: Warfarin (inhibits vitamin K epoxide reductase).