Genetic variants of human erythrocyte glucose-6-phosphate dehydrogenase. Discrete conformational states stabilized by NADP + and NADPH.

1 Analysis of thermal inactivation profiles of human erythrocyte glucose-6-phosphate dehydrogenase, type B, reveals three distinct forms of the enzyme. The form with the lowest stability is observed at very low NADP+ concentration, and probably consists of the monomeric molecular species. As the NADP+ concentration is increased, the enzyme undergoes two successive transitions to forms of higher stability, which probably consist of two different conformational states of the dimer, in equilibrium with tetramer. Enzyme type A behaves similarly, but may have less tendency to monomer formation. 2 NADPH, like NADP+, is competent to stabilize the enzyme under suitable conditions and to induce dimer formation, but probably not to induce formation of the dimer with the highest thermostability. NADPH nay be integral part of the enzyme structure. 3 Stopped-flow experiments suggest that the monomer of glucose-6-phosphate dehydrogenase is catalytically inactive, but that it recovers activity within 100 ms when exposed to a high concentration of NADPH+. By contrast, with the enzyme in dimeric form, the reaction starts immediately upon addition of glucose-6-phosphate.

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