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Pepstatin Inhibition Mechanism

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 95))

Abstract

Pepstatin is a strong inhibitor for all acid proteases. It does not inhibit other groups of proteases, such as the neutral and alkaline proteases (1). The unusual potency of pepstatin toward acid proteases is indicated by its Ki which was reported by Kunimoto et al. (2) to be about 1 × 10−10 M for porcine pepsin. Although its chemical structure has been shown (3) to be a hexapeptide which contains two residues of an unusual amino acid, 4-amino-3-hydroxy-6-methylhepatanoic acid (statine), the mode of inhibition by pepstatin is unknown.

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References

  1. Umezawa, H. (1972) Enzyme Inhibitors of Microbial Origin, pp. 31, University Park Press, Baltimore

    Google Scholar 

  2. Kunimoto, S., Aoyagi, T., Nishizawa, R., Komai, T., Takeuchi, T., and Umezawa, H. (1974) J. Antibiotics 27, 413–418

    Article  CAS  Google Scholar 

  3. Morishima, H., Takita, T., Aoyagi, T., Takeuchi, T., and Umezawa, H. (1970) J. Antibiotics 23, 263–265

    Article  CAS  Google Scholar 

  4. Kunimoto, S., Aoyagi, T., Morishima, H., Takeuchi, T., and Umezawa. (1972) J. Antibiotics 25, 251–255

    Article  CAS  Google Scholar 

  5. Aoyagi, T., Morishima, H., Nishizawa, R., Kunimoto, S., Takeuchi, T., Umezawa, H., and Ikezawa, H. (1972) J. Antibiotics 25, 689–694

    Article  CAS  Google Scholar 

  6. Lundblad, R. L., and Stein, W. H. (1969) J. Biol. Chem. 244, 154–160

    CAS  PubMed  Google Scholar 

  7. Bayliss, R. S., Knowles, J. R., and Wybrandt, G. B. (1969) Biochem. J. 113, 377–386

    Article  CAS  Google Scholar 

  8. Tang, J. (1971) J. Biol. Chem. 246, 4510–4517

    CAS  PubMed  Google Scholar 

  9. Chen, C. S., and Tang, J. (1972) J. Biol. Chem. 247, 2566–2574

    CAS  PubMed  Google Scholar 

  10. Marciniszyn, J., Jr., Hartsuck, J. A., and Tang, J. (1976) J. Biol. Chem. 251, 7088–7094

    CAS  PubMed  Google Scholar 

  11. Cleland, W. W. (1967) Advances in Enzymology 29, 1–33

    CAS  Google Scholar 

  12. Dixon, M. (1953) Biochem. J. 55, 170–171

    Article  CAS  Google Scholar 

  13. Webb, J. L. (1963) Enzyme and Metabolic Inhibitors, Vol. I, pp. 58 Academic Press, New York

    Google Scholar 

  14. Inouye, K., and Fruton, J. S. (1968) Biochem. 7, 1611–1615

    Article  CAS  Google Scholar 

  15. Knowles, J. R., Sharp, H., and Greenwell, P. (1969) Biochem. J. 113, 343–351

    Article  CAS  Google Scholar 

  16. Hartsuck, J. A., and Tang, J. (1972) J. Biol. Chem. 247, 2575–2580

    CAS  PubMed  Google Scholar 

  17. Green, N. M., and Work, E. (1953) Biochem. J. 54, 347–352

    Article  CAS  Google Scholar 

  18. Subramanian, E., Swan, I. D. A., and Davies, D. R. (1976) Biochem. Biophys. Res. Commun. 68, 875–880

    Article  CAS  Google Scholar 

  19. Rich, D. H., Sun, E., and Sengh, J. (1977) Biochem. Biophys. Res. Commun. 74, 762–767

    Article  CAS  Google Scholar 

  20. McKown, M. M., Workman, R. J., and Gregerman, R. I. (1974) J. Biol. Chem. 249, 7770–7774

    CAS  PubMed  Google Scholar 

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Marciniszyn, J., Hartsuck, J.A., Tang, J. (1977). Pepstatin Inhibition Mechanism. In: Tang, J. (eds) Acid Proteases: Structure, Function, and Biology. Advances in Experimental Medicine and Biology, vol 95. Springer, New York, NY. https://doi.org/10.1007/978-1-4757-0719-9_12

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  • DOI: https://doi.org/10.1007/978-1-4757-0719-9_12

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  • Publisher Name: Springer, New York, NY

  • Print ISBN: 978-1-4757-0721-2

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