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- W2024349135 abstract "1.|The saturation function of NADP+ for glucose-6-phosphate dehydrogenase (d-glucose 6-phosphate: NADP oxidoreductase, EC 1.1.1.49) from human erythrocytes (electrophoretic type A) is sigmoid-shaped under certain experimental conditions. If the data are plotted in terms of Hill's equation (J. Monod, J.-P. Changeux and F. Jacob, J. Mol. Biol., 6 (1963) 306), the value of the interaction coefficient is n = 1.69 at 27° and pH 8.0. 2.|These kinetic data can be interpreted as indicative of the existence of at least two NADP+-binding sites on the enzyme, with a transition from low to high affinity for NADP+ when the concentration of NADP+ is increased. A simple method for calculating the two corresponding dissociation constants is presented, and the approximate values obtained are Ks1 = 45 μM, Ks2 = 13 μM rrespectively. 3.|NADPH inhibits erythrocyte glucose-6-phosphate dehydrogenase (Ki = 16 μM). The kinetics of inhibition can be interpreted in terms of the superimposition of two effects of NADPH: (a) competition with NADP+ for (possibly identical) binding site(s), and (b) enhancement of the affinity for NADP+ of the remaining binding site(s). As a result, the cooperativity of NADP+ molecules is decreased in the presence of NADPH, and NADPH has a paradoxical activating effect when the concentration of NADP+ is very low. 4.|Since the concentrations of NADP+ and NADPH, in erythrocytes, are of the same order of magnitude, as the dissociation constants derived here, it appears that the changes in affinity induced by NADP+ and the product inhibition by NADPH may represent a physiological mechanism for the regulation of glucose-6-phosphate dehydrogenase activity in the red cell." @default.
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- W2024349135 date "1967-09-01" @default.
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- W2024349135 title "Regulation of the activity of glucose-6-phosphate dehydrogenase by NADP+ and NADPH" @default.
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- W2024349135 doi "https://doi.org/10.1016/0005-2744(67)90069-1" @default.
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