Pepsin A
| Pepsin A | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Pepsin + inhibitor (l.blue), Human | |||||||||
| Identifiers | |||||||||
| EC no. | 3.4.23.1 | ||||||||
| CAS no. | 9001-75-6 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Pepsin A (EC 3.4.23.1, 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.
See also
References
- ↑ Lee D, Ryle AP (September 1967). "Pepsinogen D. A fourth proteolytic zymogen from pig gastric mucosa". The Biochemical Journal. 104 (3): 735–41. doi:10.1042/bj1040735. PMC 1271213. PMID 4167464.
- ↑ Lee D, Ryle AP (September 1967). "Pepsin D. A minor component of commercial pepsin preparations". The Biochemical Journal. 104 (3): 742–8. doi:10.1042/bj1040742. PMC 1271214. PMID 4860638.
- ↑ Foltmann B (1981). "Gastric proteinases--structure, function, evolution and mechanism of action". Essays in Biochemistry. 17: 52–84. PMID 6795036.
- ↑ James MN, Sielecki AR (1986). "Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 A resolution". Nature. 319 (6048): 33–8. Bibcode:1986Natur.319...33J. doi:10.1038/319033a0. PMID 3941737.
- ↑ Fruton, J.S.; Brocklehurst, K. (1987). "Aspartyl proteinases". In Neuberger, A. (ed.). New Comprehensive Biochemistry: Hydrolytic Enzymes. Vol. 16. Amsterdam: Elsevier. pp. 1–38.
- ↑ Tang J, Wong RN (January 1987). "Evolution in the structure and function of aspartic proteases". Journal of Cellular Biochemistry. 33 (1): 53–63. doi:10.1002/jcb.240330106. PMID 3546346.
- ↑ Pohl J, Dunn BM (June 1988). "Secondary enzyme-substrate interactions: kinetic evidence for ionic interactions between substrate side chains and the pepsin active site". Biochemistry. 27 (13): 4827–34. doi:10.1021/bi00413a037. PMID 3139029.
External links
- Pepsin+A at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
