Pepsin A
      
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 
 References 
- ↑  Lee, D. and Ryle, A.P. (1967). "Pepsinogen D. A fourth proteolytic zymogen from pig gastric mucosa". Biochem. J. 104 (3): 735–741. PMID 4167464. 
 - ↑  Lee, D. and Ryle, A.P. (1967). "Pepsin D. A minor component of commercial pepsin preparations". Biochem. J. 104 (3): 742–748. PMID 4860638. 
 - ↑  Foltmann, R. (1981). "Gastric proteinases -structure, function, evolution and mechanism of action". Essays Biochem. 17: 52–84. PMID 6795036. 
 - ↑  James, M.N.G. and Sielecki, A.R. (1986). "Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 Å resolution". Nature 319 (6048): 33–38. doi:10.1038/319033a0. PMID 3941737. 
 - ↑  Fruton, J.S. (1987). "Aspartyl proteinases".  In Neuberger, A. and Brocklehurst, K. New Comprehensive Biochemistry: Hydrolytic Enzymes 16. Amsterdam: Elsevier. pp. 1–38. 
 - ↑  Tang, J. and Wong, R.N.S. (1987). "Evolution in the structure and function of aspartic proteases". J. Cell. Biochem. 33: 53–63. doi:10.1002/jcb.240330106. PMID 3546346. 
 - ↑  Pohl, J. and Dunn, B.M. (1988). "Secondary enzyme-substrate interactions: kinetic evidence for ionic interactions between substrate side chains and the pepsin active site". Biochemistry 27 (13): 4827–4834. doi:10.1021/bi00413a037. PMID 3139029. 
 
 
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