Phosphofructokinase of Leishmania donovani and Leishmania braziliensis and its role in glycolysis.
It was shown in an investigation of the phosphofructokinases of Leishmania donovani and Leishmania braziliensis that both enzymes are similar to that of Crithidia fasciculata. Although the enzymes are allosteric with respect to their substrates and require AMP for activation, there is no influence by other heterotropic modifiers. The Mg2+-ATP chelate activates these enzymes in a first order process and they can be inhibited by free ATP. The inhibition is reversed by the activator, AMP, in a competitive manner. The requirement for the nucleotide in L. donovani can be eliminated by decreasing the pH. The data indicate that phosphofructokinase, a pivotal enzyme in glycolysis for most organisms, probably does not play an important role in glycolysis in Leishmania.
D000249:Adenosine Monophosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D005636:Fructosephosphates / Q000378:metabolism; D005947:Glucose / Q000378:metabolism; D006019:Glycolysis; D006863:Hydrogen-Ion Concentration; D007891:Leishmania / Q000201:enzymology*; D010732:Phosphofructokinase-1 / Q000378:metabolism*
D005636:Fructosephosphates; D000249:Adenosine Monophosphate; D000255:Adenosine Triphosphate; D010732:Phosphofructokinase-1; D005947:Glucose