Chymotrypsin
Chymotrypsin
Chymotrypsin (pronounced: kai-mo-trip-sin) is a digestive enzyme component of pancreatic juice acting in the duodenum where it performs proteolysis, the breakdown of proteins and polypeptides.
Etymology
The term "Chymotrypsin" comes from the Greek words "chymo" meaning juice and "trypsin" another enzyme which it is related to.
Function
Chymotrypsin is synthesized in the pancreas by protein biosynthesis as a precursor called chymotrypsinogen that is enzymatically inactive. When chymotrypsinogen is secreted into the duodenum, it is activated by trypsin, another protease enzyme, to form chymotrypsin.
Chymotrypsin cleaves peptide bonds by hydrolysis, a process where water is used to break up molecules. This is a common process in the body, used to break down many other kinds of molecules.
Related Terms
- Protease: A group of enzymes whose catalytic function is to hydrolyze (breakdown) peptide bonds of proteins. Chymotrypsin is a type of protease.
- Pancreas: A glandular organ in the digestive system and endocrine system of vertebrates. It is both an endocrine gland producing several important hormones, including insulin, glucagon, somatostatin, and pancreatic polypeptide, and a digestive organ, secreting pancreatic juice containing digestive enzymes that assist the absorption of nutrients and the digestion in the small intestine.
- Duodenum: The first section of the small intestine immediately beyond the stomach, leading to the jejunum.
- Trypsin: A serine protease, an enzyme that helps with digestion by breaking down proteins in the small intestine. Trypsin is produced in the pancreas as the inactive proenzyme trypsinogen.
External links
- Medical encyclopedia article on Chymotrypsin
- Wikipedia's article - Chymotrypsin
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