Pepsin A

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Pepsin A
1pso.jpg
Pepsin + inhibitor (l.blue), Human
Identifiers
EC number3.4.23.1
CAS number9001-75-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB 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.[1][2][3][4][5][6][7] 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[edit]

References[edit]

  1. ^ Lee D, Ryle AP (September 1967). "Pepsinogen D. A fourth proteolytic zymogen from pig gastric mucosa". The Biochemical Journal. 104 (3): 735–41. 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. 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. doi:10.1038/319033a0. PMID 3941737.
  5. ^ Fruton, J.S.; Brocklehurst, K. (1987). "Aspartyl proteinases". In Neuberger, A. New Comprehensive Biochemistry: Hydrolytic Enzymes. 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.

External links[edit]