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The Roles of the Basic Residues in the Prosegment of Aspergillopepsinogen I

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Aspartic Proteinases

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 436))

Abstract

Aspartic proteinases are normally synthesized as inactive precursors. In many cases, the precursor. is activated by proteolytic removal of the propart under acidic conditions. The propart is considered to participate not only in inactivation of the proenzyme by masking the active site, but also in control of the activation.1–3 Additionally, the prose-quence is considered to play an essential role in folding.4,5

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Author information

Authors and Affiliations

  1. School of Life Science, Tokyo University of Pharmacy and Life Science, Japan

    H. Inoue, X.-P. Huang, H. Yamagata & K. Takahashi

  2. Graduate School of Agriculture, University of Tokyo, Japan

    X.-P. Huang

  3. Graduate School of Science, University of Tokyo, Japan

    T. Hayashi

  4. Department of Biochemistry, Faculty of Medicine, University of Peradeniya, Sri Lanka

    S. B. P. Athauda

  5. Department of Brewing and Fermentation Faculty of Agriculture, Tokyo University of Agriculture, Japan

    S. Udaka

Authors
  1. H. Inoue
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  2. X.-P. Huang
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  3. T. Hayashi
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  4. S. B. P. Athauda
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  5. H. Yamagata
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  6. S. Udaka
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  7. K. Takahashi
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Editor information

Editors and Affiliations

  1. University of Alberta, Edmonton, Alberta, Canada

    Michael N. G. James

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© 1998 Springer Science+Business Media New York

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Inoue, H. et al. (1998). The Roles of the Basic Residues in the Prosegment of Aspergillopepsinogen I. In: James, M.N.G. (eds) Aspartic Proteinases. Advances in Experimental Medicine and Biology, vol 436. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5373-1_33

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  • DOI: https://doi.org/10.1007/978-1-4615-5373-1_33

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-7452-7

  • Online ISBN: 978-1-4615-5373-1

  • eBook Packages: Springer Book Archive

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