Serine protease
Serine Protease
Serine protease (pronunciation: /ˈsɛrɪn ˈproʊtiːz, -eɪz/) is a type of protease that cleaves peptide bonds in proteins. It is named after the serine residue in its active site that functions as a nucleophile during proteolysis.
Etymology
The term "serine protease" is derived from the amino acid serine, which plays a crucial role in its catalytic activity, and the term "protease", which is a general term for enzymes that catalyze the breakdown of proteins.
Function
Serine proteases play a significant role in many biological processes, including digestion, immune response, blood coagulation, and cell signaling. They are involved in the cleavage of peptide bonds in proteins, a process that is essential for the digestion of dietary proteins.
Classification
Serine proteases are classified into clans and families based on their structural similarities and evolutionary relationships. The two main clans of serine proteases are the chymotrypsin clan (PA) and the subtilisin clan (SB).
Related Terms
- Protease: An enzyme that performs proteolysis, the breakdown of proteins into smaller polypeptides or single amino acids.
- Peptide bond: The chemical bond formed between two molecules when the carboxyl group of one molecule reacts with the amino group of the other molecule.
- Serine: An amino acid that is used in the biosynthesis of proteins.
- Chymotrypsin: A digestive enzyme component of pancreatic juice acting in the small intestine where it breaks down proteins into their amino acid components.
- Subtilisin: A type of serine protease produced by bacteria that is used in laundry detergent for its ability to break down protein stains.
External links
- Medical encyclopedia article on Serine protease
- Wikipedia's article - Serine protease
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