Subsite Specificity of Porcine Pepsin

  • James C. Powers
  • A. Dale Harley
  • Dirck V. Myers
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 92)


The specificity of porcine pepsin toward small synthetic substrates has been extensively investigated (1–4), but only a few papers have dealt with the specificity of this enzyme toward polypeptide or protein substrates. Tang analyzed cleavage sites of 4 proteins by pepsin and concluded that the enzyme possessed a hydrophobic binding site (5). In addition, bonds split by pepsin in seven peptides or proteins of established sequence have been summarized by Hill (6). In neither study was the sample size large enough to yield any information other than the primary specificity of pepsin. Antonov and his coworkers (7) recently reported a more extensive analysis of pepsin specificity toward protein substrates and concluded that the enzyme possessed five subsites.


Amino Acid Residue Basic Residue Terminal Residue Peptide Bond Cleavage Porcine Pepsin 
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  1. 1.
    Fruton, J. S. (1970) Adv. Enzymol. 33, 401–443PubMedGoogle Scholar
  2. 2.
    Fruton, J. S. (1971) The Enzymes (3rd edition) 3, 119–164Google Scholar
  3. 3.
    Fruton, J. S. (1976) Adv. Enzymol. 44, 1–36PubMedGoogle Scholar
  4. 4.
    Clement, G. E. (1973) Prog. in Bioorg. Chem. 2, 177–238Google Scholar
  5. 5.
    Tang, J. (1963) Nature 199, 1094–1095PubMedCrossRefGoogle Scholar
  6. 6.
    Hill, R. L. (1965) Adv. Protein Chem. 20, 37–107PubMedCrossRefGoogle Scholar
  7. 7.
    Zinchenko, A. A., Rumsh, L. D., and Antonov, V. K. (1976) Bioorg. Khim. 2, 803–810Google Scholar
  8. 8.
    Schechter, I., and Berger, A. (1967) Biochem. Biophys. Res. Commun. 27, 157–162PubMedCrossRefGoogle Scholar
  9. 9.
    Poulous, T., Alden, R. A., Freer, S. T., Birktoft, J. J., and Kraut, J. (1976) J. Biol. Chem. 251, 1097–1103Google Scholar
  10. 10.
    Hartsuck, J. A., and Lipscomb, W. N. (1971) The Enzymes (3rd edition) 3, 1–56Google Scholar
  11. 11.
    Anderson, W., and Harthill, J. E. (1973) Nature 243, 417–419PubMedCrossRefGoogle Scholar
  12. 12.
    Ong, E. B., and Perlmann, G. E. (1968) J. Biol. Chem. 243, 6104–6109PubMedGoogle Scholar
  13. 13.
    Harboe, M., Andersen, P. M., Foltmann, B., Kay, J., and Kassell, B. (1974) J. Biol. Chem. 249, 4487–4494PubMedGoogle Scholar
  14. 14.
    Umezawa, H. (1972) in Enzyme Inhibitors of Microbial Origin, pp. 15–52, Baltimore, Md., University Park Press.Google Scholar
  15. 15.
    Tang, J. (1976) Trends in Biochem. Sci. 1, 205–208Google Scholar

Copyright information

© Springer Science+Business Media New York 1977

Authors and Affiliations

  • James C. Powers
    • 1
    • 2
  • A. Dale Harley
    • 1
    • 2
  • Dirck V. Myers
    • 1
    • 2
  1. 1.School of ChemistryGeorgia Institute of TechnologyAtlantaUSA
  2. 2.Corporate Research and Development DepartmentThe Coca Cola CompanyAtlantaUSA

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