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
^Lee D, Ryle AP (September 1967). "Pepsinogen D. A fourth proteolytic zymogen from pig gastric mucosa". The Biochemical Journal. 104 (3): 735–41. PMC1271213. PMID 4167464.
^Lee D, Ryle AP (September 1967). "Pepsin D. A minor component of commercial pepsin preparations". The Biochemical Journal. 104 (3): 742–8. PMC1271214. 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. 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.
pepsin, pepsin, lactated, pepsin, pepsin, fortior, fundus, pepsin, elixir, lactate, pepsin, lactated, pepsin, elixir, pepsin, pepsin, enzyme, this, enzyme, catalyses, following, chemical, reactionpepsin, inhibitor, blue, humanidentifiersec, 1cas, 9001, 6databa. 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 reactionPepsin APepsin inhibitor l blue HumanIdentifiersEC no 3 4 23 1CAS no 9001 75 6DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumSearchPMCarticlesPubMedarticlesNCBIproteins 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 editPepsinReferences edit 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 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 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 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 editPepsin A at the U S National Library of Medicine Medical Subject Headings MeSH Portal nbsp Biology Retrieved from https en wikipedia org w index php title Pepsin A amp oldid 1172356410, wikipedia, wiki, book, books, library,
