title: Regulation of the energy metabolism of Plasmodium berghei.
abstract: Energy metabolism of malaria parasites was investigated in P. berghei infected red blood cells of rat. Although Plasmodia contain mitochondria most of their ATP is formed by glycolysis. Lactate formation is two orders of magnitude higher than in noninfected erythrocytes. The coupling of respiration and glycolysis is very loose, a Pasteur-effect was not found. The key enzymes of glycolysis hexokinase and phosphofructokinase have been partially purified and kinetically characterized. The kinetic properties of both enzymes significantly differ from those of erythrocytes. They are less efficiently inhibited and PFK is activated only by PEP, Fru6P and Pi. The high rate of glycolytic proton formation in Plasmodia inhibits the PFK and thus the anaerobic energy metabolism of the host cell but not that of the parasite. Nevertheless the ATP concentrations in the host and the parasite compartment were found to be nearly identical. This supports the assumption that the parasites make ATP available to their host cell, probably by an adenine nucleotide translocator.
authors: Institute of Biochemistry, Humboldt-University, Berlin, GDR.
authors: G
authors: G
authors: Jacobasch
authors: D
authors: D
authors: Buckwitz
authors: C
authors: C
authors: Gerth
authors: R
authors: R
authors: Thamm
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D004734:Energy Metabolism / Q000502:physiology*; D004906:Erythrocyte Count; D004912:Erythrocytes / Q000469:parasitology*; D006019:Glycolysis; D007700:Kinetics; D007773:Lactates / Q000096:biosynthesis; D010732:Phosphofructokinase-1 / Q000378:metabolism; D010962:Plasmodium berghei / Q000378:metabolism*; D051381:Rats
chemical_list: D007773:Lactates; D000255:Adenosine Triphosphate; D010732:Phosphofructokinase-1