Eimeria tenella contains a pyrophosphate-dependent phosphofructokinase and a pyruvate kinase with unusual allosteric regulators.
Sporozoites and unsporulated oocysts of Eimeria tenella were shown to contain a pyrophosphate-dependent phosphofructokinase (PPi-PFK) but apparently lack an ATP-specific activity. The PPi-PFK resembles those that occur in a number of other protists in being reversible and not subject to metabolic control. In contrast, the ADP-utilising pyruvate kinase, present in two developmental stages of the parasite, exhibited strong positive cooperativity with respect to its substrate, phosphoenolpyruvate, and was shown to be allosterically activated by glucose 6-phosphate, fructose 6-phosphate and AMP. It is suggested that the PPi-PFK represents an adaptation of the parasite towards life in an environment containing only low concentrations of oxygen and that the unusual allosteric regulation of pyruvate kinase evolved to compensate for glycolysis not being controlled at the PPi-PFK step.
Denton
H
H
Department of Zoology, University of Glasgow, UK.
Thong
K W
KW
Coombs
G H
GH
D000494:Allosteric Regulation; D000818:Animals; D016786:Eimeria tenella / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010732:Phosphofructokinase-1 / Q000378:metabolism*; D011755:Pyrophosphatases / Q000378:metabolism; D011770:Pyruvate Kinase / Q000378:metabolism*; D013379:Substrate Specificity
D010732:Phosphofructokinase-1; D011770:Pyruvate Kinase; D011755:Pyrophosphatases