title: [Glycolysis in a pancreatic parasite of cattle, the trematode Eurytrema pancreaticum].
abstract: Phosphoenol pyruvate carboxykinase activity in cytosol of E. pancreaticum is approximately 10 times higher than pyruvate kinase activity. Malate dehydrogenase converts oxaloacetate to malate 27 times more actively than malate to oxaloacetate. The main end product of the glycolysis is presented by succinate. Probably, the most important glycolytic pathway in the trematode investigated is the fixation of CO2 to phosphoenol pyruvate to produce oxaloacetate.
mesh_terms: D000818:Animals; D002417:Cattle / Q000469:parasitology; D006003:Glycogen / Q000378:metabolism; D006019:Glycolysis; D010179:Pancreas / Q000469:parasitology; D014200:Trematoda / Q000201:enzymology / Q000378:metabolism*; D014201:Trematode Infections / Q000469:parasitology / Q000662:veterinary
chemical_list: D006003:Glycogen
vernacular_title: Glikoliz u parazita podzheludochnoĭ zhelezy krupnogo rogatogo skota--trematody Eurytrema pancreaticum.