Chymotrypsin Lab Report

1254 Words6 Pages
Chymotrypsin is an enzyme that is produced in the pancreas that aids in the digestion of mammals. It is a catalyst that speeds up the hydrolysis of proteins into amino acids and polypeptides. It goes through a specific mechanism, called the ping-pong mechanism, for its reaction, and has been studied for many years. From these studies has come the knowledge that it can be used in a variety of diseases and/or problems. Chymotrypsinogen is the inactive form of an enzyme that is produced in the pancreas, so it is found in all mammals. It is created in its inactive form so it does not start to digest the proteins of the pancreas. It travels from the pancreas with other digestive enzymes to the small intestine, where it works as a catalyst. So it…show more content…
The first step is where the substrate enters the active site on the enzyme. It is held there by hydrophobic interactions between the exposed non-polar groups of the enzyme residues and the side chain of the substrate. The second step is where the hydroxyl group on Serine 195, aided by the histidine-serine hydrogen bonding, preforms its nucleophilic attack on the carbonyl carbon of an aromatic amino acid. While this happens, it also transfers the hydroxyl hydrogen to the histidine nitrogen. The nucleophilic attack pushes the carbonyl electrons onto the carbonyl oxygen, which forms a short-lived intermediate. The third step is where the oxyanion electrons reform the bond with the aromatic amino acid. Then the bond between the carboxyl-terminus of the amino acid and the n-terminus of the residue is cleaved and its electrons are used to take out the hydrogen of the nitrogen on the Histidine 57. The c-terminal side of the polypeptide is free to dissociate form the active site. Step four is basically just where water can now enter and bind to the active site through hydrogen bonding, which is between the hydrogen atoms of water and the Histidine-57 nitrogen. The fifth step is the step where the water and oxygen make a nucleophilic attack on the carbonyl carbon of the acyl-enzyme intermediate. This pushes the carbonyl’s electrons onto the carbonyl carbon, while the Histidine-57 takes one proton from the…show more content…
So far it has been used as a digestive aid and an anti-inflammatory agent. It has mostly been used in the treatment of pancreatic insufficiency. This insufficiency is characterized by impaired digestion, malabsorption, passing of undigested food into the stool, nutrient deficiencies, gas, and abdominal bloating and discomfort7. Pancreatic deficiency can also occur in those with cystic fibrosis, chronic pancreatitis, and the elderly. Chronic stress, physical injuries, and chemotherapy could also result in chymotrypsin deficiency7. When used as an anti-inflammatory agent, it prevents tissue damage during inflammation and the formation of fibrin clots. In auto-immune diseases, chymotrypsin aids in the breakdown of immune complexes, which are antibodies that are produced by the immune system. Some specific cases in which chymotrypsin would be used for treatment would include soft tissue injuries, hematomas, infections, arthritis, cancer (controversial), acne, shingles, and sports injuries. Chymotrypsin is mostly produced from fresh hog, beef, or oxen pancreas. It can be taken orally, topically, or by injection (by injection only by a physician in severe life-threatening situations), but is most commonly taken orally in tablet form7. Someone who has a family history of clotting disorders,

More about Chymotrypsin Lab Report

Get Access