The glyoxalase system of malaria parasites—Implications for cell biology and general glyoxalase research

Low-Molecular-Mass Antioxidants in Parasites

“…4) (17,119,253). Upon infection, the glucose consumption of the red blood cell increases up to 75-fold (226).…”

“…Both the erythrocyte and the parasite harbor a functional GLX system (for a recent review see ref. 253).…”

Malaria-associated hypoglycaemia in children

“…The high-power metabolism of Plasmodium leads to a significantly increased glucose consumption of infected erythrocytes [64], but is considered a "contributing factor" rather than the "causative factor" of hypoglycaemia because of the big difference in glucose demand between the parasites and the severely ill patient [65].…”

Bacterial glyoxalase I enzymes: structural and biochemical investigations

“…Glo1 from Saccharomyces cerevisiae was found early on to be a monomeric enzyme, but with approximately twice the protein length of the human and E. coli enzymes and follow-up studies indicated that the yeast enzyme has two functioning active sites with somewhat different enzymatic activities and possibly different metallation [35][36][37][38][39]. Insightful studies of Plasmodium falciparum Glo1 determined that the two active sites of this monomeric enzyme are allosterically coupled and have different affinities for substrate; at low substrate concentrations, P. falciparum Glo1 appears to exist in a 'high-affinity' conformation, but in a 'high-activity' conformation at high substrate levels [40][41][42][43]. This is an intriguing molecular assembly which could point to very interesting Plasmodium intracellular biochemistry [43].…”

“…Insightful studies of Plasmodium falciparum Glo1 determined that the two active sites of this monomeric enzyme are allosterically coupled and have different affinities for substrate; at low substrate concentrations, P. falciparum Glo1 appears to exist in a 'high-affinity' conformation, but in a 'high-activity' conformation at high substrate levels [40][41][42][43]. This is an intriguing molecular assembly which could point to very interesting Plasmodium intracellular biochemistry [43]. An alternate quaternary structure different from the homodimeric structural arrangement found for human and E. coli Glo1 enzymes was reported recently from high-throughput structural genomics initiatives led by the New York Structural Genomics Research Consortium on Clostridium acetobutylicum proteins [44].…”