Abstract
Penicillopepsin is an acid protease produced by the mold Penicillium janthinellum at pH’s less than 4.1 (1). Enzyme production occurs after the mycelial growth has ceased and sporulation has begun (2). The specificity and catalytic mechanism of penicillo-pepsin are very similar to those of porcine pepsin (3). The two active site aspartic acid residues, Asp-32 and Asp-215, occur in peptide sequences of at least eight amino acid residues which are almost identical in penicillopepsin, pepsin and chymosin (1,4–10). In addition, there is an overall 32% identity of amino acid sequence between penicillopepsin and porcine pepsin; a tentative sequence alignment of these two enzymes is given in Table I using this sequence numbering of porcine pepsin (5). These facts indicate that the fungal enzyme penicillopepsin is an evolutionary homologue of the mammalian acid proteases.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Sodek, J., and Hofmann, T. (1970) Can. J. Biochem. 48, 1014–1017
Mackinlay, A. G., and Wake, R. G. (1971) in Milk Proteins: Chemistry and Moleculary Biology Vol. 2 (McKenzie, H. A. ed) pp. 175–215, Academic Press, New York
Mains, G., Takahashi, M., Sodek, J., and Hofmann, T. (1971) Can. J. Biochem. 49, 1134–1149
Cunningham, A., Wang, H.-M., Jones, S. R., Kurosky, A., Rao, L., Harris, C. I., Rhee, S. H., and Hofmann, T. (1976) Can. J. Biochem. 54, 902–914
Tang, J., Sepulveda, P., Marciniszyn, Jr., J., Chen, K. C. S., Huang, W.-Y., Tao, N., Lin, D., and Lanier, J. P. (1973) Proc. Natl. Acad. Sci. U.S.A. 70, 3437–3439
Rajogopalan, T. G., Stein, W. H., and Moore, S. J. (1966) J. Biol. Chem. 241, 4295–4297
Bayliss, R. S., Knowles, J. R., and Wybrandt, G. B. (1969) Biochem. J. 113, 377–386
Meitner, P. A. (1971) Biochem. J. 124, 673–676
Foltmann, B., Kauffman, D., Parl, M., and Andersen, P. M. (1973) Netherlands Milk Dairy J. 27, 165–175
Takahashi, K., Mizobe, F., and Chang, W. J. (1972) J. Biochem. ( Tokyo ) 71, 161–164
Camerman, N., Hofmann, T., Jones, S., and Nyburg, S. C. (1969) J. Mol. Biol. 44, 569–570
Hsu, I-N., Hofmann, T., Nyburg, S. C., and James, M. N. G. (1976) Biochem. Biophys. Res. Commun. 72, 363–368
Codding, P. W., Delbaere, L. T. J., Hayakawa, K., Hutcheon, W. L. B., James, M. N. G., and Jurasek, L. (1974) Can. J. Biochem. 52, 208–220
Delbaere, L. T. J., Hutcheon, W. L. B., James, M. N. G., and Thiessen, W. E. (1975) Nature 257, 758–763
Blow, D. M., and Crick, F. H. C. (1959) Acta Crystallogr. 12, 794–802
Subramanian, E., Swan, I. D. A., and Davies, D. R. (1976) Biochem. Biophys. Res. Commun. 68, 875–880
Jenkins, J. A., Blundell, T. L., Tickle, I. J., and Ungaretti, L. (1975) J. Mol. Biol. 99, 583–590
Richardson, J. S. (1976) Proc. Natl. Acad. Sci. U.S.A. 73, 2619–2623
Fruton, J. S. (1970) Adv. Enzymol. 33, 401–443
Delpierre, G. R., and Fruton, J. S. (1966) Proc. Natl. Acad. Sci. U.S.A. 56, 1817–1822
Knowles, J. R., and Wybrandt, G. B. (1968) FEBS Lett. 1, 211
Chen, K. C. S., and Tang, J. (1972) J. Biol. Chem. 247, 2566–2574
Hartsuck, J. A., and Tang, J. (1972) J. Biol.Chem. 247, 2575–2580
Cornish-Bowden, A. J., and Knowles, J. R. (1969) Biochem. J. 113, 353–362
Kitson, T. M., and Knowles, J. R. (1971) FEBS Lett. 16, 337–338
James, M. N. G., and Williams, G. J. B. (1971) J. Med. Chem. 14, 670–675
James, M. N. G., and Williams, G. J. B. (1974) Can. J. Chem. 52, 1872–1879
James, M. N. G., and Williams, G. J. B. (1974) Acta Crystallogr. B30, 1249–1257
Wang, J. H. (1970) in Structure-Function Relationships of Proteolytic Enzymes (Desnuelle, P., Neurath, H. and Otteson, M.,eds) pp. 251–252, Munksgaard, Copenhagen
Knowles, J. R. (1970) Philos. Trans. R. Soc. London Ser B 257, 135–146
Delpierre, C. R., and Fruton, J. S. (1965) Proc. Natl. Acad. Sci. U.S.A. 54, 1161–1167
Hofmann, T. (1974) Adv. Chem. Series 136, 146–185
Takahashi, M., and Hofmann, T. (1975) Biochem. J. 147, 549–563
Wang, T.-T., and Hofmann, T. (1976) Biochem. J. 153, 701–712
Knowles, J. R., Bayliss, R. S., Cornish-Bowden, A. J., Greenwell, P., Kitson, T. M., Sharp, H. C., and Wybrandt, G. B. (1970) in Structure-Function Relationships of Proteolytic Enzymes“ (Desnuelle, P., Neurath, H., and Otteson, M. eds) pp. 237–250, Munksgaard, Copenhagen
Fruton, J. S. (1976) in Advances in Enzymology (Meister, A., ed) pp. 1–36, Interscience, John Wiley and Sons, New York
Lipscomb, W. N., Hartsuck, J. A., Reeke, G. N., Quiocho, F. A., Bethge, P. H., Ludwig, M. L., Steitz, T. A., Muirhead, H., and Coppola, J. C. (1968) Brookhaven Symp. Biol. 21, 24–90
Quiocho, F. A., and Lipscomb, W. N. (1971) in Advances Protein Chemistry (Afinsen, C. B., Edsall, J. T., and Richards, F. M. eds) pp. 1–78, Academic Press, New York
Newmark, A. K., and Knowles, J. R. (1975) J. Amer. Chem. Soc. 97, 3557–3559
Wang, T.-T., and Hofmann, T. (1976) Biochem. J. 153, 691–699
Lenhert, P. G. L. (1975) J. Appl. Crystallogr. 8, 568–570
Biochem. J. (1969) 113, 1–4
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1977 Springer Science+Business Media New York
About this chapter
Cite this chapter
Hsu, IN., Delbaere, L.T.J., James, M.N.G., Hofmann, T. (1977). Penicillopepsin: 2.8 a Structure, Active Site Conformation and Mechanistic Implications. 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_5
Download citation
DOI: https://doi.org/10.1007/978-1-4757-0719-9_5
Published:
Publisher Name: Springer, New York, NY
Print ISBN: 978-1-4757-0721-2
Online ISBN: 978-1-4757-0719-9
eBook Packages: Springer Book Archive