Question

Are enzyme inhibitors bad?

Answer 1

Enzyme Inhibitors:

1. Molecules that interact with enzymes & reduce the rate of an enzyme-catalyzed reaction.
2. They prevent enzymes from working in their usual manner.
3. Sometimes, inhibition of regular enzyme functioning may result in adverse drug interactions.
4. They regulate various metabolic processes that are pivotal in homeostasis.
5. They are used as medicines, pesticides, etc.
6. Example- methotrexate is used in the treatment of rheumatoid arthritis, Organophosphates(pesticides) are used as an enzyme inhibitor for acetylcholinesterase (AChE).

There are two types of enzyme inhibitors:

1. Competitive inhibitors – compete with the substrate for binding at the active site.
2. Example- methotrexate competes with folic acid.
3. Non-competitive inhibitors – bind to a site other than the active site known as an allosteric site and bring about the conformational changes in the enzyme structure.
4. Example- binding of heavy metals to the enzyme cytochrome oxidase(in electron transport chain).