Explain the enzyme inhibitors? Their types with their difference?

Enzyme inhibitors are molecules that bind to enzymes and decrease their activity. There are two main types of enzyme inhibitors: reversible inhibitors and irreversible inhibitors.

1. Reversible inhibitors:
- Competitive inhibitors: These inhibitors compete with the substrate for binding to the active site of the enzyme. They are structurally similar to the substrate and can be overcome by increasing the concentration of the substrate.
- Non-competitive inhibitors: These inhibitors bind to a site on the enzyme that is not the active site, causing a conformational change in the enzyme that reduces its activity. They cannot be overcome by increasing the substrate concentration.
- Uncompetitive inhibitors: These inhibitors bind to the enzyme-substrate complex and prevent the enzyme from releasing the product. They are only effective when the substrate is already bound to the enzyme.

2. Irreversible inhibitors:
- Irreversible inhibitors covalently bind to the enzyme, permanently inactivating it. They are often used as drugs to target specific enzymes in diseases such as cancer.

The main difference between reversible and irreversible inhibitors is that reversible inhibitors can be overcome by increasing the substrate concentration, while irreversible inhibitors permanently inactivate the enzyme. Additionally, reversible inhibitors can bind and unbind from the enzyme, while irreversible inhibitors form a permanent bond with the enzyme.