Regular paperComparison of the phosphofructokinase and pyruvate kinase activities of Cryptosporidium parvum, Eimeria tenella and Toxoplasma gondii
References (24)
- et al.
Metabolic studies on T. gondii
Exp. Parasitol.
(1960) - et al.
Purification and properties of pyrophosphate-dependent phosphofructokinase from Toxoplasma gondii
Mol. Biochem. Parasitol.
(1992) - et al.
Pyrophosphate:D-fructose 6-phosphate 1-phosphotransferase: a new enzyme with the glycolytic function of 6-phosphofructokinase
J. Biol. Chem.
(1974) - et al.
Presence of a fructose 2,6-bisphosphate-insensitive pyrophosphate:fructose 6-phosphate phosphotransferase in the anaerobic protozoa Tritrichomonas foetus, Trichomonas vaginalis and Isotricha prostoma
Mol. Biochem. Parasitol.
(1989) Pyrophosphate-dependent phosphofructokinase, an anaerobic glycolytic enzyme
FEBS Lett.
(1991)- et al.
Evolution of glycolysis
Progr. Biophys. Mol. Biol.
(1993) ATP versus pyrophosphate: Glycolysis revisited in parasitic protists
Parasitol. Today
(1993)A new enzyme with the glycolytic function of pyruvate kinase
J. Biol. Chem.
(1968)- et al.
A method for the determination of inorganic phosphate in the presence of labile organic phosphate and high concentrations of protein: application to lens ATPases
Anal. Biochem.
(1988) - et al.
Inorganic pyrophosphatase of Trichomonas vaginalis
Mol. Biochem. Parasitol.
(1991)
Inorganic pyrophosphatase and nucleoside diphosphatase in the parasitic protozoon, Entamoeba histolytica
Biochem. Biophys. Res. Commun.
Some phosphonic acid analogs as inhibitors of pyrophosphate-dependent phosphofructokinase, a novel target in Toxoplasma gondii
Biochem. Pharmacol.
Cited by (59)
Effects of diclazuril on the expression of enolase in second-generation merozoites of Eimeria tenella
2020, Poultry ScienceCitation Excerpt :To finish its life cycle, E. tenella must adjust its metabolism to the different living conditions. Energy metabolism is a necessary process of biological survival (Mi et al., 2017), and the energy source of E. tenella is largely dependent on anaerobic energy by glycolysis (Denton et al., 1996). Enolase, as a key enzyme in the glycolysis pathway, catalysts the reversible interconversion of 2-phospho-d-glycerate to phosphoenolpyruvate (Mi et al., 2017).
Lactate dehydrogenase: An important molecule involved in acetamizuril action against Eimeria tenella
2020, Journal of Integrative AgricultureIn-silico screening of small molecule inhibitors against Lactate Dehydrogenase (LDH) of Cryptosporidium parvum
2018, Computational Biology and ChemistryCitation Excerpt :Genome sequencing of C. parvum indicates that it does not have a functional mitochondrion and lacks an active Kreb’s cycle but encodes all glycolytic enzymes (Abrahamsen et al., 2004). The parasite primarily depends on anaerobic oxidation of glucose for energy metabolism (Denton et al., 1996; Coombs, 1999), and enzymes in the glycolytic pathways to produce ATP. Studies on other apicomplexan parasites have revealed that inhibition of glycolysis may be a valuable approach for antiparasitic treatment (Wang, 1984; Basco et al., 1995; Bressi et al., 2000).
Biochemical and structural characterization of Cryptosporidium parvum Lactate dehydrogenase
2015, International Journal of Biological MacromoleculesCitation Excerpt :Genome sequencing indicates that C. parvum does not have a functional mitochondrion and lacks an active Krebs’ cycle [1] but encodes all glycolytic enzymes. Since the parasite appears to depend primarily on anaerobic oxidation of glucose for energy metabolism [12,16,18], enzymes in the glycolytic pathway and those that play regulatory roles may offer potential targets for anti-cryptosporidial drugs. Studies with other apicomplexan parasites have shown that inhibition of glycolysis may be a useful strategy for antiparasitic therapy [2,4,13,15,46].
The Hsp90 co-chaperone p23 of Toxoplasma gondii: Identification, functional analysis and dynamic interactome determination
2010, Molecular and Biochemical ParasitologyPlant-like phosphofructokinase from Plasmodium falciparum belongs to a novel class of ATP-dependent enzymes
2009, International Journal for Parasitology