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

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 Ki 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.

• Authors: L Tyas, I Gluzman, R P Moon, K Rupp, J Westling, R G Ridley, J Kay, D E Goldberg, C Berry
• Journal: FEBS letters (FEBS Lett) Vol. 454 Issue 3 Pg. 210-4 (Jul 09 1999) ISSN: 0014-5793 [Print] England
• PMID: 10431809 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Protozoan Proteins
• Recombinant Proteins
• Aspartic Acid Endopeptidases
• plasmepsin
• plasmepsin II

Topics

• Amino Acid Sequence
• Animals
• Aspartic Acid Endopeptidases (genetics, metabolism)
• Humans
• Malaria, Falciparum (parasitology)
• Molecular Sequence Data
• Plasmodium falciparum (enzymology)
• Protozoan Proteins
• Recombinant Proteins (genetics, metabolism)