title: Phosphofructokinase from Plasmodium berghei: a kinetic model of allosteric regulation.
abstract: As in mammalian cells, phosphofructokinase (PFK) is of major regulatory importance in the glucose metabolism of Plasmodium berghei. The malarial enzyme shows allosteric properties similar to PFK from various sources; it is activated by fructose-6-phosphate and inhibited by ATP, but differs with respect to allosteric regulation. Enzyme activity is only marginally increased by AMP, a potent activator of many phosphofructokinases. Phosphoenolpyruvate, which is reported to inhibit PFK activity, efficiency activates the malarial enzyme. No activation by ADP was observed. Instead, ADP inhibits the enzyme non-allosterically and competitively to the substrate MgATP. Phosphate stimulates the catalytic activity of malarial PFK independently of the activation by F6P and PEP.
authors: Institute of Biochemistry, Humboldt University, Berlin, G.D.R.
authors: D
authors: D
authors: Buckwitz
authors: G
authors: G
authors: Jacobasch
authors: C
authors: C
authors: Gerth
mesh_terms: D000244:Adenosine Diphosphate / Q000494:pharmacology; D000494:Allosteric Regulation; D000818:Animals; D004789:Enzyme Activation / Q000187:drug effects; D007700:Kinetics; D008954:Models, Biological; D010710:Phosphates / Q000494:pharmacology; D010728:Phosphoenolpyruvate / Q000494:pharmacology; D010732:Phosphofructokinase-1 / Q000378:metabolism*; D010962:Plasmodium berghei / Q000187:drug effects / Q000201:enzymology*
chemical_list: D010710:Phosphates; D000244:Adenosine Diphosphate; D010728:Phosphoenolpyruvate; D010732:Phosphofructokinase-1