The enigmatic presence of all gluconeogenic enzymes in Schistosoma mansoni adults.
作者： A. G. M. Tielens , P. Van Der Meer , J. M. Van Den Heuvel , S. G. Van Den Bergh
DOI: 10.1017/S0031182000062582
关键词: Gluconeogenesis 、 Lactate dehydrogenase 、 Schistosoma mansoni 、 Enzyme 、 Pyruvate kinase 、 Phosphoenolpyruvate carboxykinase 、 Biochemistry 、 Glycogen 、 Biology 、 Pyruvate carboxylase
摘要: The activities of glucose-6-phosphatase (G6Pase), fructose-1,6-bisphosphatase (FBPase), phosphoenolpyruvate carboxykinase (PEPCK) and pyruvate carboxylase (PC) were determined in homogenates adult Schistosoma mansoni worms compared with the rat liver skeletal muscle, tissues a high low gluconeogenic capacity, respectively. All four enzymes present S. mansoni. less active than liver, but G6Pase, PEPCK PC at least an order magnitude higher muscle whereas FBPase was approximately equally muscle. Experiments 14C-labelled substrates or [14C]NaHCO3 failed to demonstrate actual occurrence gluconeogenesis Some possible other functions investigated. inhibitors gave no indications that this enzyme involved degradation glucose. This confirmed by 13C-NMR experiments which indicated lactate formed from via actions kinase dehydrogenase, did not participate formation lactate. Substrate cycling between fructose-6-dehydrogenase, fructose-1,6-bisphosphate demonstrated occur shows participates glucose metabolism parasite.
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