Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.9 (glucose-6-phosphatase)
 3,081 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activities of glucose-6-phosphatase (G6Pase), fructose-1,6-bisphosphatase (FBPase), phosphoenolpyruvate carboxykinase (PEPCK) and pyruvate carboxylase (PC) were determined in homogenates of adult Schistosoma mansoni worms and compared with the activities in homogenates of rat liver and rat skeletal muscle, tissues with a high and a low gluconeogenic capacity, respectively. All four gluconeogenic enzymes were present in S. mansoni. The enzymes were less active than in rat liver, but the activities of G6Pase, PEPCK and PC were at least an order of magnitude higher than in rat skeletal muscle whereas FBPase was approximately equally active in S. mansoni and in rat muscle. Experiments with 14C-labelled substrates or [14C]NaHCO3 failed to demonstrate the actual occurrence of gluconeogenesis in S. mansoni. Some possible other functions of the gluconeogenic enzymes were investigated. Experiments with inhibitors of PEPCK gave no indications that this enzyme was involved in the degradation of glucose. This was confirmed by 13C-NMR experiments which indicated that lactate was formed from phosphoenolpyruvate via the actions of pyruvate kinase and lactate dehydrogenase, and that PEPCK did not participate in the formation of lactate. Substrate cycling between fructose-6-dehydrogenase, and fructose-1,6-bisphosphate was demonstrated to occur in adult S. mansoni. This shows that FBPase participates in the glucose metabolism of this parasite.
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PMID:The enigmatic presence of all gluconeogenic enzymes in Schistosoma mansoni adults. 164 28

Purified brush border membrane of Cotugnia digonopora showed the presence of a number of phosphohydrolases. Among these, alkaline phosphatase was extremely active. Other enzymes such as glucose-6-phosphatase, fructose-1,6-diphosphatase, cAMP-phosphodiesterase, 5'-nucleotidase and adenosine-triphosphatase were also active. Observations were made on the activities of various ATPases; whereas the enzyme was activated by Ca++ and Mg++ in an additive manner, its sensitivity to ouabain was negligible. Furthermore, in the presence of EDTA the enzyme activity was quite significant. The treatment of isolated brush border membrane with mebendazole, niclosamide and praziquantel in vitro did not alter the activity of these enzymes. However, treatment of intact worms drastically affected the integrity of the membrane.
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PMID:Enzymes of isolated brush border membrane of Cotugnia digonopora, and their insensitivity to anthelmintics in vitro. 299 11

The present study deals with the comparative efficacy of Hetrazan, levamisole and tetramisole on the enzyme activities of adult Setaria cervi worms. The drugs were administered orally to white rats, intraperitoneally infected with the bovine filariid, Setaria cervi. Biochemical assays revealed the decreased activities of glucose-6-phosphatase, fructose-1,6-diphosphatase, lactate dehydrogenase and adenosine triphosphatase in the drug-treated worms. Hetrazan was relatively more effective than tetramisole and levamisole. A possible role of these enzymes in the energy supply and survival of the worm has been briefly discussed.
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PMID:Effect of anthelmintics on the enzyme activities of Setaria cervi (Nematoda: Filarioidea). 661 75

The distribution of Dirofilaria immitis acid proteinase in adult worm tissue was examined biochemically and immunohistochemically. About 45% of the total proteinase activity of 700g supernatant, which was obtained from the 0.25 M sucrose homogenate of live adult worms, was found in the 100,000g supernatant by subcellular centrifugation analysis. The distribution pattern of the proteinase activity observed by Percoll density gradient centrifugation coincided with that of glucose-6-phosphatase, a marker cytosolic enzyme, suggesting that the acid proteinase was present in vivo in a membrane-free form, possibly in the cytosol or secretory fluid. Immunostaining for the proteinase in the parasite tissue using the IgG1 (kappa-type) monoclonal antibody, H-1, revealed immunoreactive enzyme primarily inside the cell as small grains, but not on the cell surface, and immunoreactivity was distributed widely in worm tissues such as lateral cords, dorsal and ventral median cords, the anterior end of the parasite, and intestinal epithelial cells in granular form. In the male reproductive system, the testicular wall and germ cells were labeled with the antibody, and in the female, uterine walls, fertilized eggs, and developing eggs as well as microfilaria were labeled. In conclusion, D. immitis acid proteinase is widely distributed in the parasite tissue, possibly functioning not only in nutrition metabolism but also in production of sperm and microfilariae, etc.
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PMID:Dirofilaria immitis: immunohistochemical localization of acid proteinase in the adult worm. 762 68