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Site-Directed Mutagenesis of Rhizopuspepsin: An Analysis of Unique Specificity

  • W. Todd Lowther
  • Ben M. Dunn
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 362)

Abstract

Rhizopuspepsin is an aspartic proteinase from the fungus Rhizopus chinensis. Interest in rhizopuspepsin as a model system for studying active site interactions stems principally from the need to understand interactions which may be exploited in rational drug design. Targets for these therapeutics are renin, which plays a role in hypertension, the HIV proteinase, essential to the HIV life cycle, and a variety of related, secreted Candida yeast aspartic proteinases[1, 2].

Keywords

Aspartic Proteinase Rational Drug Design Unique Specificity Porcine Pepsin Oklahoma Medical Research Foundation 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1995

Authors and Affiliations

  • W. Todd Lowther
    • 1
  • Ben M. Dunn
    • 1
  1. 1.Department of Biochemistry and Molecular BiologyUniversity of Florida, JHMHCGainesvilleUSA

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