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Pepsin A
| Field | Value |
|---|---|
| Name | Pepsin A |
| EC_number | 3.4.23.1 |
| CAS_number | 9001-75-6 |
| image | 1pso.jpg |
| width | 270 |
| caption | Pepsin + inhibitor (l.blue), Human |
Pepsin A (, pepsin, lactated pepsin, pepsin fortior, fundus-pepsin, elixir lactate of pepsin, P I, lactated pepsin elixir, P II, pepsin R, pepsin D) is an enzyme. This enzyme catalyses the following chemical reaction
: Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves Phe1-Val, Gln4-His, Glu13-Ala, Ala14-Leu, Leu15-Tyr, Tyr16-Leu, Gly23-Phe, Phe24-Phe and Phe25-Tyr bonds in the B chain of insulin
The enzyme is a predominant endopeptidase in the gastric juice of vertebrates.
References
References
- (September 1967). "Pepsinogen D. A fourth proteolytic zymogen from pig gastric mucosa". The Biochemical Journal.
- (September 1967). "Pepsin D. A minor component of commercial pepsin preparations". The Biochemical Journal.
- (1981). "Gastric proteinases--structure, function, evolution and mechanism of action". Essays in Biochemistry.
- (1986). "Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 A resolution". Nature.
- (1987). "New Comprehensive Biochemistry: Hydrolytic Enzymes". Elsevier.
- (January 1987). "Evolution in the structure and function of aspartic proteases". Journal of Cellular Biochemistry.
- (June 1988). "Secondary enzyme-substrate interactions: kinetic evidence for ionic interactions between substrate side chains and the pepsin active site". Biochemistry.
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