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Article in English | IMSEAR | ID: sea-124247

ABSTRACT

Previous publications have clearly demonstrated that hydroxymethylglutaryl coenzyme A [HMG-CoA] reductase activity of Schistosoma mansoni is vital for parasite reproductive activity and that drugs which inhibit this enzyme have been found to be effective antischistosomal agents. In this report we describe the expression and purification of enzymatically active schistosome HMG-CoA reductase enzyme. The recombinant protein was tested, in parallel with the mammalian enzyme, against well-known mammalian HMG-CoA reductase inhibitors obtained from various pharmaceutical companies. We demonstrated that there were significant differences in the response of the two proteins to an array of HMG-CoA reductase inhibitors. The difference in the characteristics between mammalian and schistosome enzyme could be exploited for rational drug design.


Subject(s)
Animals , Catalytic Domain , Humans , Hydroxymethylglutaryl CoA Reductases/drug effects , Hydroxymethylglutaryl-CoA Reductase Inhibitors/chemistry , Recombinant Proteins , Schistosoma mansoni/enzymology
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