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Naturally-occurring and recombinant forms of the aspartic proteinases plasmepsins I and II from the human malaria parasitePlasmodium falciparum

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
454
Issue
3
Identifiers
DOI: 10.1016/s0014-5793(99)00805-4
Keywords
  • Malaria
  • Aspartic Proteinase
  • Plasmepsin
  • Plasmodium Falciparum
Disciplines
  • Biology

Abstract

Abstract Comparable kinetic parameters were derived for the hydrolysis of peptide substrates and the interaction of synthetic inhibitors with recombinant and naturally-occurring forms of plasmepsin II. In contrast, recombinant plasmepsin I was extended by 12 residues at its N-terminus relative to its naturally-occurring counterpart and a 3–10-fold diminution in the k ent values was measured for substrate hydrolysis by the recombinant protein. However, comparable K 1 values were derived for the interaction of two distinct inhibitors with both forms of piasmepsin I, thereby validating the use of recombinant material for drug screening. The value of plasmepsin I inhibitors was determined by assessing their selectivity using human aspartic proteinases.

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