Question

1) Please explain what the difference b/t reversible and irreversible inhibition mechanism?

Also provide 2 examples from each category.

2) Bring a couple of examples for covalent inhibitors and describe how they work.

Answer 1

Enzymes

1) Reversible enzymes inhibitors as the name suggests are enzymes that binds to an enzyme site and then can be reverted back to free inhibitor state without it undergoing any reaction or any changes during the process. These inhibitors bind to enzymes by weak non-covalent type of interactions such as hydrogen bond, hydrophobic type of interaction etc. For example chemical reactions are often used with inhibitor to provide specific type of product or amount of product formed.

Irreversible inhibition are permanent inhibition. The binding of inhibitors to enzyme canot be reversed and they undergo reactions during the process. The binding in this case is strong covalent interactions The major application of it is in pharmaceutical treatment of diseases. For example inhibition of proteases, organophosphorous compounds which inhibit eznyme acetylcholinesterase, cyanide posiioning, etc.

2) Covalent inhibitors : binds by covalent interactions. For example a protease inhibitor binds to the enzyme by a strong peptide bond. A drug disulfiram inhibits aldehyde oxidase by sulfide bond formation.