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Gene Review

G6PD  -  glucose-6-phosphate dehydrogenase

Sus scrofa

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Disease relevance of G6PD

  • Inhibition of G6PD by low levels of aluminum further strengthens the suggested role of aluminum toxicity in the energy metabolism of the brain [1].
  • Maximum increases in G6PD activity occurred at an IgG concentration of 50 micrograms/ml in all patients who had goitrous Graves' disease and in 5:7 who had diffuse non-toxic goitres [2].
  • Here we show that protein synthesis inhibitors chloramphenicol and erythromycin, which bind to domain V of 23S rRNA of E. coli, can inhibit reactivation of denatured pig muscle lactate dehydrogenase and fungal glucose-6-phosphate dehydrogenase by 23S rRNA completely [3].
  • Monospecific (affinity-purified) anti-(yeast glucose-6-phosphate dehydrogenase) IgG inhibits three different NADPH-requiring enzymes, chicken liver dihydrofolate reductase, pigeon liver fatty acid synthetase and chicken liver malic enzyme [4].
  • Mammalian lactate dehydrogenase and phosphofructokinase are more susceptible in vitro to superoxide (O2) and hydroxyl (.OH) radicals than pyruvate kinase and glucose-6-phosphate dehydrogenase, suggesting that differential inactivation of regulatory enzymes contributes to the metabolic disintegration in stenoxic tissues during transient hypoxia [5].

High impact information on G6PD


Biological context of G6PD


Anatomical context of G6PD


Associations of G6PD with chemical compounds

  • When kidney segments were incubated with 1,25(OH)2D3 (0, 0.15, 0.30, 1.5 or 3.0 nM) during the initial 5 h maintenance culture, G6PD activity at each steroid concentration decreased gradually to reach its stable basal level, which was higher in proportion to the increasing concentration of 1,25(OH)2D3 [12].
  • Kmapp values of the G6PD isozymes were similar for NADP+ (6-8 microM), but different for G6P (56-180 microM) [21].
  • In the present communication we have studied the isoenzymatic pattern activity of the glucose 6-phosphate dehydrogenase (G6PD) in Oesophagostomum venulosum, Trichuris ovis and T. suis, parasites of Capra hircus (goat), Ovis aries (sheep) and Sus scrofa domestica (pig) respectively, by polyacrylamide gel electrophoresis [22].
  • However, when the G6PD isozymes were completely inactivated by aluminum, only citrate, NaF, and apotransferrin restored the enzyme activity [1].
  • Preincubation of aluminum with citrate, NADP+, EDTA, NaF, ATP, and apotransferrin protected the G6PD isozymes against aluminum inactivation [1].

Other interactions of G6PD


Analytical, diagnostic and therapeutic context of G6PD


  1. Inactivation of glucose-6-phosphate dehydrogenase isozymes from human and pig brain by aluminum. Cho, S.W., Joshi, J.G. J. Neurochem. (1989) [Pubmed]
  2. Thyroid growth-stimulating immunoglobulins in goitrous disease: relationship to thyroid-stimulating immunoglobulins. Smyth, P.P., McMullan, N.M., Grubeck-Loebenstein, B., O'Donovan, D.K. Acta Endocrinol. (1986) [Pubmed]
  3. Reactivation of denatured proteins by 23S ribosomal RNA: role of domain V. Chattopadhyay, S., Das, B., Dasgupta, C. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  4. Purification of nucleotide-requiring enzymes by immunoaffinity chromatography. Stapleton, S.R., Porter, J.W. Biochem. J. (1985) [Pubmed]
  5. Preservation of phosphagen kinase function during transient hypoxia via enzyme abundance or resistance to oxidative inactivation. Dykens, J.A., Wiseman, R.W., Hardin, C.D. J. Comp. Physiol. B, Biochem. Syst. Environ. Physiol. (1996) [Pubmed]
  6. Tissue distribution and evolution of fructosamine 3-kinase and fructosamine 3-kinase-related protein. Delplanque, J., Delpierre, G., Opperdoes, F.R., Van Schaftingen, E. J. Biol. Chem. (2004) [Pubmed]
  7. CO2 adducts as reactive analogues of carboxylate substrates for aconitase and other enzymes of carbohydrate metabolism. Porter, D.J., Alston, T.A., Bright, H.J. J. Biol. Chem. (1987) [Pubmed]
  8. A kinetic study of glucose-6-phosphate dehydrogenase. Kanji, M.I., Toews, M.L., Carper, W.R. J. Biol. Chem. (1976) [Pubmed]
  9. Enzymatic determination of 1-14C-glucose in pig plasma. Schäffer, L., Tronier, B. Diabetologia (1989) [Pubmed]
  10. The inter-ligand Overhauser effect: a powerful new NMR approach for mapping structural relationships of macromolecular ligands. Li, D., DeRose, E.F., London, R.E. J. Biomol. NMR (1999) [Pubmed]
  11. The localization of genes for HPRT, G6PD, and alpha-GAL onto the X-chromosome of domestic pig (Sus scrofa domesticus). Leong, M.M., Lin, C.C., Ruth, R.F. Can. J. Genet. Cytol. (1983) [Pubmed]
  12. Calcium-dependent activation of glucose-6-phosphate dehydrogenase by 1,25-dihydroxycholecalciferol in the guinea pig distal convoluted tubule. Sakaguchi, K., Fukase, M., Kobayashi, I., Fujita, T. Bone and mineral. (1987) [Pubmed]
  13. Morphologic, biometric, and isoenzyme characterization of Trichuris suis. Oliveros, R., Cutillas, C., Arias, P., Guevara, D. Parasitol. Res. (1998) [Pubmed]
  14. Metabolic activity of deciduous porcine dental pulp in different phases of root development. Siquara-Da-Rocha, M.C., Nicolau, J. J. Dent. Res. (1980) [Pubmed]
  15. The development of adipocytes in primary stromal-vascular culture of fetal pig adipose tissue. Hausman, G.J., Novakofski, J.E., Martin, R.J., Thomas, G.B. Cell Tissue Res. (1984) [Pubmed]
  16. An important role for pentose cycle in the synthesis of citrulline and proline from glutamine in porcine enterocytes. Wu, G. Arch. Biochem. Biophys. (1996) [Pubmed]
  17. Ultraviolet light-induced changes in the glucose-6-phosphate dehydrogenase activity of porcine corneas. Tsubai, T., Matsuo, M. Cornea (2002) [Pubmed]
  18. Effect of the source of dietary fat on postweaning lipogenesis in lean and fat pigs. Freire, J.P., Mourot, J., Cunha, L.F., Almeida, J.A., Aumaitre, A. Ann. Nutr. Metab. (1998) [Pubmed]
  19. Differentiation of adipose tissue and muscle in hypophysectomized pig fetuses. Hausman, G.J., Hentges, E.J., Thomas, G.B. J. Anim. Sci. (1987) [Pubmed]
  20. Purification of guinea pig small intestinal peroxisomes and the subcellular localization of glucose-6-phosphate dehydrogenase. Tappia, P.S., Jones, C.J., Connock, M.J. Mol. Cell. Biochem. (1998) [Pubmed]
  21. Characterization of glucose-6-phosphate dehydrogenase isozymes from human and pig brain. Cho, S.W., Joshi, J.G. Neuroscience (1990) [Pubmed]
  22. Glucose 6-phosphate dehydrogenase: isoenzymatic pattern in Oesophagostomum venulosum, Trichuris ovis and T. suis. Rodriguez, B., Cutillas, C., German, P., Guevara, D. J. Helminthol. (1991) [Pubmed]
  23. Lipogenic enzyme activities in subcutaneous adipose tissue and skeletal muscle from neonatal pigs consuming maternal or formula milk. Gerfault, V., Louveau, I., Mourot, J., Le Dividich, J. Reprod. Nutr. Dev. (2000) [Pubmed]
  24. The influence of hydrocortisone (HC) on differentiation of adipose tissue is dependent on fetal age. Hausman, G.J., Wright, J.T. Obes. Res. (1994) [Pubmed]
  25. Dietary conjugated linoleic acid consumption during pregnancy and lactation influences growth and tissue composition in weaned pigs. Bee, G. J. Nutr. (2000) [Pubmed]
  26. Anti-oxidant enzymes in fetal guinea pig brain during development and the effect of maternal hypoxia. Mishra, O.P., Delivoria-Papadopoulos, M. Brain Res. (1988) [Pubmed]
  27. Effect of a high linoleic acid diet on delta 9-desaturase activity, lipogenesis and lipid composition of pig subcutaneous adipose tissue. Kouba, M., Mourot, J. Reprod. Nutr. Dev. (1998) [Pubmed]
  28. Inhibition and adaptation of red cell glucose-6-phosphate dehydrogenase (G6PD) in vivo to chronic sublethal dietary cyanide in an animal model. Jackson, L.C., Chandler, J.P., Jackson, R.T. Hum. Biol. (1986) [Pubmed]
  29. Isoenzymatic pattern of glucose 6-phosphate dehydrogenase from Ascaris suum. Cutillas, C., Rodriguez, B., German, P., Guevara, D. J. Helminthol. (1993) [Pubmed]
  30. Analysis of Chinese isolates of Trichinella spiralis by molecular biotechnology. Zhang, Y., Wang, H., Lao, W., Zhou, M., Wu, Z., Liu, H., Shi, H. Chin. Med. J. (1996) [Pubmed]
  31. Regulation of skeletal muscle development by the central nervous system in the fetal pig. Campion, D.R., Richardson, R.L., Kraeling, R.R., Reagan, J.O. Growth. (1978) [Pubmed]
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