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Functional characterization of an alternative [lactate dehydrogenase-like] malate dehydrogenase in Plasmodium falciparum

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Abstract

The catalysis of malate dehydrogenase (MDH) in Plasmodium falciparum (pfMDH) which involves NAD/NADH coupling is crucial for the parasite’s pathogenicity. Primers were designed based on the P. falciparum genome resource, and these facilitated the cloning of a gene coding for pfMDH from a local clinical isolate. The DNA sequence of the cloned gene revealed an open-reading frame that encodes a protein of 313 amino acids. After induction in Escherichia coli BL21, enzyme assays of the expressed pfMDH purified by affinity chromatography exhibited significant enzyme activity of about 50 U/mg, where one unit (U) of enzyme activity is defined as the amount of enzyme oxidising 1 μol NADH/min. Based on its phylogenetic status amongst MDHs and lactate dehydrogenases (LDHs), the cloned gene was clearly defined as belonging to the NADH-dependent [LDH-like] MDHs. It is noteworthy that pfMDH harbours unique structural characteristics potentially useful for screening drugs specific for disabling parasitic enzymes.

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Authors and Affiliations

  1. Department of Microbiology, Faculty of Medicine, National University of Singapore, Block MD4, 5 Science Drive 2, 117597, Singapore

    M. Chan & T. S. Sim

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  1. M. Chan
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  2. T. S. Sim
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Correspondence to T. S. Sim.

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Chan, M., Sim, T.S. Functional characterization of an alternative [lactate dehydrogenase-like] malate dehydrogenase in Plasmodium falciparum . Parasitol Res 92, 43–47 (2004). https://doi.org/10.1007/s00436-003-0996-1

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  • DOI: https://doi.org/10.1007/s00436-003-0996-1

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