Comparison of the phosphofructokinase and pyruvate kinase activities of Cryptosporidium parvum, Eimeria tenella and Toxoplasma gondii.
Oocysts of Cryptosporidium parvum were shown to contain a pyrophosphate-dependent phosphofructokinase (PPi-PFK) similar to those previously described for Eimeria tenella and Toxoplasma gondii. PPi-PFK of C. parvum displayed simple hyperbolic kinetics with respect to its substrate fructose 6-phosphate and was not affected by fructose 2,6-bisphosphate, the major allosteric activator of most ATP-PFKs. Inorganic pyrophosphatase was not detectable in any of the three parasites. T. gondii tachyzoites and C. parvum cysts both contained a pyruvate kinase (PK) specific for ADP rather than PPi/AMP. The PK of T. gondii was similar to that of E. tenella in that it displayed strong positive cooperativity with respect to its substrate phosphoenolpyruvate and was heterotropically activated by glucose 6-phosphate, fructose 6-phosphate and fructose 1,6-bisphosphate. PK of C. parvum showed no evidence of allosteric properties. The results suggest that the three coccidia are similar in depending heavily on anaerobic energy production via glycolysis but that the mechanisms for regulating glycolysis are not common to all species.
Denton
H
H
Institute of Biomedical and Life Sciences, University of Glasgow, UK.
Brown
S M
SM
Roberts
C W
CW
Alexander
J
J
McDonald
V
V
Thong
K W
KW
Coombs
G H
GH
D000693:Anaerobiosis; D000818:Animals; D016785:Cryptosporidium parvum / Q000201:enzymology*; D016786:Eimeria tenella / Q000201:enzymology*; D006019:Glycolysis; D010732:Phosphofructokinase-1 / Q000302:isolation & purification / Q000378:metabolism*; D011755:Pyrophosphatases / Q000378:metabolism; D011770:Pyruvate Kinase / Q000302:isolation & purification / Q000378:metabolism*; D014122:Toxoplasma / Q000201:enzymology*
D010732:Phosphofructokinase-1; D011770:Pyruvate Kinase; D011755:Pyrophosphatases