Pepsin A

Pepsin A
Pepsin + inhibitor (l.blue), Human
Identifiers
EC no.3.4.23.1
CAS no.9001-75-6
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
PubMedarticles
NCBIproteins

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

  1. ↑ 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.
  2. ↑ 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.
  3. ↑ Foltmann B (1981). "Gastric proteinases--structure, function, evolution and mechanism of action". Essays in Biochemistry. 17: 52–84. PMID 6795036.
  4. ↑ 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.
  5. ↑ Fruton, J.S.; Brocklehurst, K. (1987). "Aspartyl proteinases". In Neuberger, A. (ed.). New Comprehensive Biochemistry: Hydrolytic Enzymes. Vol. 16. Amsterdam: Elsevier. pp. 1–38.
  6. ↑ 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.
  7. ↑ 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.