Phosphofructokinase from Plasmodium berghei: a kinetic model of allosteric regulation.
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.
Buckwitz
D
D
Institute of Biochemistry, Humboldt University, Berlin, G.D.R.
Jacobasch
G
G
Gerth
C
C
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*
D010710:Phosphates; D000244:Adenosine Diphosphate; D010728:Phosphoenolpyruvate; D010732:Phosphofructokinase-1