Exploiting Unique Structural and Functional Properties of Malarial Glycolytic Enzymes for Antimalarial Drug Development

<div>Differential posttranslational modifications in<i> P. falciparum</i> and human enzymes, enolase (a) and GAPDH (b). PfENO, HsENO1, PfGAPDH, and HsGAPDH represent<i> P. falciparum</i> enolase, human enolase 1,<i> P. falciparum</i> GAPDH, and human GAPDH, respectively. Residues predicted to be modified are shown in boxes. Posttranslational modification sites were predicted by using online available tools. (Phosphorylation with NetPhos 2.0 (<a href="http://www.cbs.dtu.dk/services/NetPhos/">http://www.cbs.dtu.dk/services/NetPhos/</a>), methylation with BPB-PPMS (<a href="http://www.bioinfo.bio.cuhk.edu.hk/bpbppms/intro.jsp">http://www.bioinfo.bio.cuhk.edu.hk/bpbppms/intro.jsp</a>), and ubiquitination with UbiPred (<a href="http://www.ubpred.org/">http://www.ubpred.org/</a>), resp.)</div>

Malaria Research and Treatment

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Figure 4

Figure 4: Exploiting Unique Structural and Functional Properties of Malarial Glycolytic Enzymes for Antimalarial Drug Development 