Endopeptidase
Endopeptidase
Endopeptidase (pronunciation: /ˌɛndoʊˈpɛptɪˌdeɪz/), also known as protease, is a type of enzyme that breaks down proteins into smaller peptides or amino acids.
Etymology
The term "endopeptidase" is derived from the Greek words "endo", meaning "within", and "peptos", meaning "digested". This refers to the enzyme's ability to cleave peptide bonds within proteins.
Function
Endopeptidases play a crucial role in various biological processes, including digestion, immune response, and cell signaling. They are responsible for the initial breakdown of proteins in the digestive system, which are then further degraded by exopeptidases into individual amino acids.
Types
There are several types of endopeptidases, each with a specific function and preference for certain peptide bonds. These include:
- Trypsin: This endopeptidase cleaves peptide bonds on the carboxyl side of arginine and lysine residues.
- Chymotrypsin: This enzyme preferentially cleaves peptide bonds on the carboxyl side of tyrosine, tryptophan, and phenylalanine residues.
- Pepsin: This endopeptidase, found in the stomach, cleaves peptide bonds primarily on the carboxyl side of aromatic amino acids.
Related Terms
- Exopeptidase: An enzyme that cleaves peptide bonds at the end of proteins, producing individual amino acids.
- Proteolysis: The breakdown of proteins into smaller peptides or amino acids, often through the action of enzymes like endopeptidases.
- Protease inhibitor: A molecule that inhibits the activity of proteases, including endopeptidases.
External links
- Medical encyclopedia article on Endopeptidase
- Wikipedia's article - Endopeptidase
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