Endopeptidase

Endopeptidases are enzymes that cleave peptide bonds anywhere on a protein molecule, also called a peptide chain. They are important components of many biological processes such as digestion, the immune system and metabolism.

Endopeptidase is a protein that contains the active site required to break the peptide bond. This protein can be either exogenous or endogenous. Endogenous endopeptidases are found within cells and are involved in various metabolic processes, including digestion, protein synthesis, tissue remodeling, and the immune response.

There are many endopeptidases, each with unique functions and substrate specificities. Some of the best known endopeptidases include caspases, serine proteases, and metalloproteases. Caspases play an important role in the regulation of the cell cycle and apoptosis, and serine and metalloproteases are involved in the processes of protein degradation and regulation of cellular functions.

In addition, endopeptidases have a wide range of applications in biotechnology and medicine. For example, they are used to study the structure of proteins, produce vaccines and diagnose diseases. In addition, some endopeptidases can be used as therapeutic agents to treat various diseases such as cancer and autoimmune diseases.

In general, endopeptidases are an important class of enzymes that play key roles in various biological processes. Their study and application for scientific and medical purposes continue to be urgent tasks for researchers and scientists around the world.

Endopeptides are synthetic enzymes (proteases) that are designed to cleave peptide bonds, including protein molecules, peptides and oligopeptides.

The *creation* of endoproteases was caused by the need to obtain a protein product - insulin, a specific method in the treatment of various diseases associated with disorders of carbohydrate metabolism. During the breakdown of proteins and the metabolites they produce, toxic substances ammonia, pyruvate and acetone accumulate, which causes a number of undesirable consequences. Complications boil down to the development of ketoacidosis, damage to the nervous system, and diabetic coma. Another important aspect is the lack of enzymes in the body of patients with diabetes. To obtain a hypoglycemic agent that acts at the molecular level, proteases have been developed that destroy excess insulin when it enters the body.

*Functional load* of enzymes with antidiabetic action is aimed at