What is endopeptidase?
endopeptidase is a type of protease, an enzyme from a large group that degrades proteins. Enzymes are proteins that cause reactions to take place much faster. Proteins consist of chains of amino acids connected by peptide bonds. This connection connects the carboxyl end of one amino acid with the amino -end another. Endopeptidases break down the peptide bonds of amino acids inside the protein, unlike exopeptidase that breaks down at the ends of the protein.
endopeptidases are found in all classes of organisms and have a wide range of biological activities. They are involved in the digestion of proteins in food. This includes enzymes Pepsin, trypsin and chymotrypsin. Proteases are also involved in cell signaling by breaking down other proteins such as antibodies or hormones. They can turn on or off the paths.
Proteases are usually first made as a larger molecule that is inactive. This protects the cell that synthesizes it from Damaged. Once the protease is delivered to your goalE, for example, a stomach, a piece of molecule is removed. This activates protease.
Given their countless roles in cellular function, there is many medical interest in endopeptidase activity. One examples are endopeptidase, which is cleared specifically over the amino acid proling. He was associated with psychological disorders such as depression, mania and schizophrenia. There is a clinical interest in the inhibitors of endopeptidase inhibitors, as is possible antidepressants.
Another example is neutral endopeptidase, which has several other names. It is also known as non -fellow and common acute lymphoblastic leukemic antigen (Calla). This protease degrades small secreted peptides, including peptide, which was implicated as the cause of Alzheimer's disease and several important signaling peptides. Neutral endopeptidase is sometimes used as a marker of cancer, but its role in cancer is unclear. Were developed inhIbitors that help to relieve pain and control high blood pressure.
endopeptidases are located in different families, depending on the structure of their active place and the conditions they prefer. There are serine proteases that have an amino acid serine at their active place. Members of this family include Trypsin's digestive proteases and chymotrypsin along with endopeptidase. One inhibitor often used in biochemical research laboratories is a highly toxic compound of phenylmethanesulphonylflouride (PMSF). It is used during insulation and cleaning of proteins to inhibit serine protease activity that can degrade the protein that is purified.
cysteine proteases have a group of sulfur in their active place and are common in fruit. These enzymes are found in wooden fabrics. Papain is an example of such endopeptidase and is used to treat bees and wasps Stings.
Active place of aspartic proteases generally contains two groups of aspartate. MetalloendopeptIdasis require a metal capping for activity. Neutral endopeptidases are part of this family and require zinc for activity.