Abstract
The enzyme glucose-6-phosphate dehydrogenase (G6PD) catalyzes the oxidation of D-glucose-6-phosphate to 6-phospho-D-gluconolactone with the simultaneous reduction of NADP+ to NADPH. The enzyme is the first in the pentose phosphate pathway (hexose monophosphate shunt), which produces pentose phosphates used for nucleotide and nucleic acid synthesis, and reducing equivalents in the form of NADPH for use in biosynthetic reduction reactions, including fatty acid synthesis and hydroxlations. G6PD has been purified and characterized from the tissue cytosols of several mammalian species, including human erythrocytes, rat mammary gland, rat and mouse liver, and bovine adrenal cortex (Bonsignore and DeFlora, 1972; Levy, 1979). In general, the enzymes from these sources are “similar” and are composed of subunits that, by immunological and molecular weight criteria, may be identical proteins within a species. The monomeric subunits have a molecular weight of about 60,000, based on their rate of migration on SDS-polyacrylamide gels. The monomers are catalytically inactive. In the presence of NADP+, the inactive monomers form a catalytically active dimer containing 1 or perhaps 2 moles of NADP+ per mole of dimer; at reduced ionic strength and pH, and in the presence of Mg2+, the dimers aggregate to form tetramers and hexamers.
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© 1981 Plenum Press, New York
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Barker, K.L., Adams, D.J., Donohue, T.M. (1981). Regulation of the Levels of mRNA for Glucose-6-phosphate Dehydrogenase and Its Rate of Translation in the Uterus by Estradiol. In: Glasser, S.R., Bullock, D.W. (eds) Cellular and Molecular Aspects of Implantation. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-3180-3_20
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DOI: https://doi.org/10.1007/978-1-4613-3180-3_20
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