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Penicillopepsin: 2.8 a Structure, Active Site Conformation and Mechanistic Implications

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Book cover Acid Proteases: Structure, Function, and Biology

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

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.

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Author information

Authors and Affiliations

  1. MRC Group on Protein Structure and Function, University of Alberta, Edmonton, Alberta, T6G 2H7, Canada

    I-Nan Hsu, Louis T. J. Delbaere & Michael N. G. James

  2. Department of Biochemistry, University of Toronto, Toronto, Canada, M5S lA8

    Theo Hofmann

Authors
  1. I-Nan Hsu
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  2. Louis T. J. Delbaere
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  3. Michael N. G. James
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  4. Theo Hofmann
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Editors and Affiliations

  1. Oklahoma Medical Research Foundation, USA

    Jordan Tang

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© 1977 Springer Science+Business Media New York

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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

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  • DOI: https://doi.org/10.1007/978-1-4757-0719-9_5

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