What is Zymogen?
Zymogen is an inactive pre -surgery of the enzyme. The molecule is composed of amino acids that are hired in the peptide. When zymogen is in the presence of an enzyme specially designed to disintegrate peptides called protease, some of the amino acids are removed. This cleavage makes zymogen functional enzyme by changing the shape of the peptide and creating an active place where the enzymatic effect occurs. For this reason, the commission is also called Proenzym.
The active location is a key feature of the enzyme. It is a place where the molecule on which the enzyme operates is called a substrate, binds and is subject to chemical change. The active place and the overall function of the enzyme depends on the shape of the enzyme. This is determined by four structural levels.
The primary structure of the enzyme is simply an amino acid sequence. The secondary structure represents how the peptide folds and circles on itself due to the interactions between amino acids. The other structures include the target alpha helix and beta pleated leaves that resemble the composition of the accordion.
tertiaryThe structure describes the overall folding of the whole peptide, with the secondary structures consisting of each other to form a globular ball, an active conformation of the protein. Some proteins have a quaternary structure that describes how two or more peptides are connected to form a complex protein. For example, hemoglobin, which carries oxygen in the blood, consists of four individual peptides associated with the creation of a functional molecule.
The body usually excludes zymogens rather than active enzymes, as they can be stored and transported safely without damaging the surrounding tissues and relaxed when conditions are favorable for optimal activity. For example, pepsinogen is excreted in the stomach and cleaved to form pepsin, an enzyme that breaks down the proteins of Ingested as food. In fact, highly acidic stomach conditions cause pepsinogen cleavage and promote pepsin activity. Once digestion moves to tEnk intestines, drastic pH change inactivates Pepsin and two other zymogens are released.
Chymotrysinogen and trypsinogen, also enzymes for proteins, are key ingredients of digestive juice released with pancreas. They travel through the main pancreatic channel to the twelve of the small intestine, where they are then cleaved into their active forms. By releasing zymogens instead of active enzymes Chymotrypsin and trypsin with the pancreas avoids self -confidence.
Other zymogens in the body include prothrombin and fibrinogen, both necessary for the formation of clots. Both exist as plasma proteins. If they are needed to lose blood due to tissue damage, these zymogens are easily accessible and have caused any damage to the circulatory system in which they are stored.