A distinct member of the aspartic proteinase gene family from the human malaria parasite Plasmodium falciparum
Open Access
- 26 March 1999
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 447 (2-3) , 149-154
- https://doi.org/10.1016/s0014-5793(99)00276-8
Abstract
A gene (hap) transcribed during the intra‐erythrocytic life cycle stages of the human malaria parasite Plasmodium falciparum was cloned and sequenced. It was found to encode a protein belonging to the aspartic proteinase family but which carried replacements of catalytically crucial residues in the hallmark sequences contributing to the active site of this type of proteinase. Consideration is given as to whether this protein is the first known parasite equivalent of the pregnancy‐associated glycoproteins that have been documented in ungulate mammals. Alternatively, it may be operative as a new type of proteinase with a distinct catalytic mechanism. In this event, since no counterpart is known to exist in humans, it affords an attractive potential target against which to develop new anti‐malarial drugs.Keywords
This publication has 26 references indexed in Scilit:
- Expression and Characterisation of Plasmepsin I from Plasmodium falciparumEuropean Journal of Biochemistry, 1997
- Involvement of a residue at position 75 in the catalytic mechanism of a fungal aspartic proteinase, Rhizomucor pusilus pepsin. Replacement of tyrosine 75 on the flap by asparagine enhances catalytic efficiencyProtein Engineering, Design and Selection, 1996
- Comparative modelling and analysis of amino acid substitutions suggests that the family of pregnancy-associated glycoproteins includes both active and inactive aspartic proteinasesProtein Engineering, Design and Selection, 1996
- High level expression and characterisation of Plasmepsin II, an aspartic proteinase from Plasmodium falciparumFEBS Letters, 1994
- Order and specificity of the Plasmodium falciparum hemoglobin degradation pathway.Journal of Clinical Investigation, 1994
- Rabbit procathepsin E and cathepsin EEuropean Journal of Biochemistry, 1993
- Assessment of protein models with three-dimensional profilesNature, 1992
- Human immunodeficiency virus-1 protease. 1. Initial velocity studies and kinetic characterization of reaction intermediates by oxygen-18 isotope exchangeBiochemistry, 1991
- A malarial cysteine proteinase is necessary for hemoglobin degradation by Plasmodium falciparum.Journal of Clinical Investigation, 1988
- The active site of aspartic proteinasesFEBS Letters, 1984