Glycolysis (glycose+lysis= breaking of glucose) is a sequence of 10 definite reactions which leads to breaking of glucose into pyruvate. This is the first of four steps of aerobic respiration. This cytosolic metabolic pathway produces a net gain of 2 ATPs. This step is also common to anaerobic respiration as it does not require O2. In anaerobic respiration, pyruvate will then be converted to lactate (e.g. skeletal musles) or ethanol and carbon dioxide (e.g. yeast) to re-oxidise electron carrier NADH to provide NAD+ for glycolysis.
The apicomplexans Toxoplasma gondii, Plasmodium falciparum and Cryptosporidium species possess all the ten enzymes of glycolysis in the genome. Cryptosporidium species possess one lactate dehydrogenase enzyme (converts pyruvate to lactate) as in P. falciparum , whereas T. gondii possesses 2 lactate dehydrogenase isoforms. Of the enzymes NAD-dependent glycerol-3-phosphate dehydrogenase and FAD-dependent glycerol-3-phophate dehydrogenase (catalyse bidirectional conversion of glycerol-3-phosphate to glycerone phosphate) added to the glycolysis pathway for T. gondii, only the NAD dependent enzyme is present in the Cryptosporidium species. The above mentioned enzymes and other enzymes added in T. gondii glycolysis pathway such as aldehyde reductase, phosphoglucomutase and acylphosphatase are also present in Cryptosporidium muris and added to the pathway here. In addition, gluconeogenesis enzyme, fructose bisphosphatase present in T. gondii is absent in Cryptosporidium and P. falciparum.
All the enzymatic activities of the glycolytic pathway except hexokinase were detected in the Cryptosporidium parvum oocysts in the cytosolic fractions. The absence of hexokinase activity being detected is mainly due to the fact that at oocysts stage, amylopectin is degraded to glucose-1-phosphate and the glycolysis starts with phosphoglucomutase activity. In addition, this pathway is characterised by the presence of pyrophosphate dependent phosphofructokinase rather than ATP-dependent enzyme increasing the net yield of ATP to 3 from 2 . The substrate specificities of pyrophosphate specific phosphofructokinase and ADP-specific pyruvate kinase were observed in C. parvum, T. gondii and Eimeria tenella . The recombinant versions of three of these C. parvum enzymes, glyceraldehyde-3-phosphate dehydrogenase, pyruvate kinase and lactate dehydrogenase were expressed, purified and crystallised by Senkovich et al . In addition, the structure of triose phosphate isomerase of C. parvum was also elucidated .
|Enzyme||EC Number||Gene id|
|Glyceraldehyde 3-P dehydrogenase||18.104.22.168||CMU_017050|
|Triose phosphate isomerase||22.214.171.124||CMU_029840|
Sources and fates of metabolites
|Substrate||Source pathways||Product||Fate pathways|
|alpha-D-Glucose||Host, Starch metabolism||alpha-D-Glucose-6P||Starch metabolism|
|alpha-D-Glucose-1P||Starch metabolism, Pyrimidine metabolism|
|beta-D-Fructose-6P||Aminosugars metabolism, Starch metabolism|
|sn-glycerol-3P||Phosphatidylethanolamine and phosphatidylserine metabolism|