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Naturally‐occurring and recombinant forms of the aspartic proteinases plasmepsins I and II from the human malaria parasite Plasmodium f alciparum
Author(s) -
Lorraine Tyas,
Ilya Y. Gluzman,
Richard P. Moon,
Katharina Rupp,
Jennifer Westling,
Robert G. Ridley,
John Kay,
Daniel E. Goldberg,
Colin Berry
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00805-4
Subject(s) - recombinant dna , biochemistry , peptide , chemistry , enzyme , stereochemistry , biology , gene
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.