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

Lorraine Tyas, Ilya Gluzman, Richard P. Moon, Katharina Rupp, Jennifer Westling, Robert G. Ridley, John Kay, Daniel E. Goldberg, Colin Berry

Research output: Contribution to journalArticle

36 Scopus citations

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(cat) values was measured for substrate hydrolysis by the recombinant protein. However, comparable K(i) values were derived for the interaction of two distinct inhibitors with both forms of plasmepsin 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. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)210-214
Number of pages5
JournalFEBS Letters
Volume454
Issue number3
DOIs
StatePublished - Jul 9 1999
Externally publishedYes

Keywords

  • Aspartic proteinase
  • Malaria
  • Plasmepsin
  • Plasmodium falciparum

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