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trypsin |
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trypsin, enzyme enzyme, biological catalyst . The term enzyme comes from zymosis, the Greek word for fermentation , a process accomplished by yeast cells and long known to the brewing industry, which occupied the attention of many 19th-century chemists. ..... Click the link for more information. that acts to degrade protein protein, any of the group of highly complex organic compounds found in all living cells and comprising the most abundant class of all biological molecules. Protein comprises approximately 50% of cellular dry weight. ..... Click the link for more information. ; it is often referred to as a proteolytic enzyme, or proteinase. Trypsin is one of the three principal digestive proteinases, the other two being pepsin pepsin, enzyme produced in the mucosal lining of the stomach that acts to degrade protein. Pepsin is one of three principal protein-degrading, or proteolytic, enzymes in the digestive system , the other two being chymotrypsin and trypsin . ..... Click the link for more information. and chymotrypsin chymotrypsin (kī'mōtrĭp`sĭn), proteolytic, or protein-digesting, enzyme active in the mammalian intestinal tract. ..... Click the link for more information. . In the digestive process, trypsin acts with the other proteinases to break down dietary protein molecules to their component peptides and amino acids. Trypsin continues the process of digestion (begun in the stomach) in the small intestine where a slightly alkaline environment (about pH 8) promotes its maximal enzymatic activity. Trypsin, produced in an inactive form by the pancreas, is remarkably similar in chemical composition and in structure to the other chief pancreatic proteinase, chymotrypsin. Both enzymes also appear to have similar mechanisms of action; residues of histidine histidine (hĭs`tĭdēn), organic compound, one of the 22 α- amino acids commonly found in animal proteins. ..... Click the link for more information. and serine serine (sĕr`ēn), organic compound, one of the 20 amino acids commonly found in animal proteins. ..... Click the link for more information. are found in the active sites of both. The chief difference between the two molecules seems to be in their specificity, that is, each is active only against the peptide bonds in protein molecules that have carboxyl groups donated by certain amino acids. For trypsin these amino acids are arginine and lysine, for chymotrypsin they are tyrosine, phenylalanine, tryptophan, methionine, and leucine. Trypsin is the most discriminating of all the proteolytic enzymes in terms of the restricted number of chemical bonds that it will attack. Good use of this fact has been made by chemists interested in the determination of the amino acid sequence of proteins; trypsin is widely employed as a reagent for the orderly and unambiguous cleavage of such molecules. How to thank TFD for its existence? Tell a friend about us, add a link to this page, add the site to iGoogle, or visit webmaster's page for free fun content. |
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