Plasmodium lactate dehydrogenase (pLH) is one of the enzymes in glycolysis with potential target for chemotherapy. This study aimed to clone, overexpress and characterize soluble recombinant lactate dehydrogenase from in a bacterial system. Synthetic lactate dehydrogenase (-LDH) gene was cloned into pET21a expression vector, transformed into strain BL21 (DE3) expression system and then incubated for 18 h, 20 °C with the presence of 0.
View Article and Find Full Text PDFEthnopharmacological Relevance: Medicinal plants have been used for ages by indigenous communities around the world to help humankind sustain its health. Graviola (Annona muricata), also called soursop, is a member of the Annonaceae family and is an evergreen plant that is generally distributed in tropical and subtropical areas of the world. Graviola tree has a long history of traditional use due to its therapeutic potential including anti-inflammatory, antimicrobial, antioxidant, insecticide and cytotoxic to tumor cells.
View Article and Find Full Text PDFOne of the oldest reservoirs in Peninsular Malaysia, Bukit Merah Reservoir, is a place in which locals participate in fishing activities. Inland fisheries are important to individuals, society and the environment; whereby they generate a source of income and food security. It is essential to gauge the nutrition value of fish caught in this location as food source, especially in terms of fatty acid composition, to better demonstrate its potential towards the betterment of human health and general well-being.
View Article and Find Full Text PDFThree structurally distinct forms of phosphoglycerate mutase from the trypanosomatid parasite Leishmania mexicana were isolated by standard procedures of bacterial expression and purification. Analytical size-exclusion chromatography coupled to a multi-angle scattering detector detected two monomeric forms of differing hydrodynamic radii, as well as a dimeric form. Structural comparisons of holoenzyme and apoenzyme trypanosomatid cofactor-independent phosphoglycerate mutase (iPGAM) X-ray crystal structures show a large conformational change between the open (apoenzyme) and closed (holoenzyme) forms accounting for the different monomer hydrodynamic radii.
View Article and Find Full Text PDFProduction of ATP by the glycolytic pathway in the mammalian pathogenic stage of protists from the genus Trypanosoma is required for the survival of the parasites. Cofactor-independent phosphoglycerate mutase (iPGAM) is particularly attractive as a drug target because it shows no similarity to the corresponding enzyme in humans, and has also been genetically validated as a target by RNAi experiments. It has previously been shown that trypanosomatid iPGAMs require Co(2+) to reach maximal activity, but the biologically relevant metal has remained unclear.
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