Aspartic proteinases: The structures and functions of a versatile superfamily of enzymes


This paper reviews the structure and function of monomeric eukaryotic aspartic proteinases and their inhibitors, including recent analyses of the sequences and the three-dimensional structural models of the plant aspartic proteinases, which contain a very large inserted domain that is homologous to saposins. The three-dimensional structures of renins, cathepsin D and cathepsin E complexed with inhibitors are described. These have provided an understanding of the relation between structure, catalysis and specificity useful for drug design. Finally, studies are presented of homologues of aspartic proteinases which are found during pregnancy in livestock; these have lost the catalytic residues characteristic of active enzymes, although they have the capacity to bind peptides.

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Correspondence to Tom L. Blundell.

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Guruprasad, K., Dhanaraj, V., Groves, M. et al. Aspartic proteinases: The structures and functions of a versatile superfamily of enzymes. Perspectives in Drug Discovery and Design 2, 329–341 (1995).

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Key words

  • Renin
  • Cathepsin D
  • Cathepsin E
  • Plant aspartic proteinases
  • Pregnancy-associated glycoproteins
  • Drug design