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- W2024915521 abstract "When intact chloroplasts are incubated in the dark with dihydroxyacetone phosphate, an increase in fructose 1,6-bisphosphatase activity occurs which resembles the reductive activation observed in illuminated chloroplasts. Under optimum conditions, the activity increases to about 150 μmol · h−1 · mg−1 chlorophyll within 60 min. The dark activation of the enzyme is reversed by electron acceptors such as oxaloacetate, nitrite, and 3-phosphoglycerate plus ATP. Activation is most marked under strictly anaerobic conditions, being strongly inhibited by O2. It is concluded that NADPH, generated from dihydroxyacetone phosphate in situ in the reaction catalyzed by NADP+-dependent glyceraldehyde phosphate dehydrogenase, can provide electrons for the reductive activation of fructose 1,6-bisphosphatase in the dark." @default.
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- W2024915521 date "1981-12-01" @default.
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- W2024915521 title "Activation of fructose 1,6-bisphosphatase in darkened intact chloroplasts by NADPH" @default.
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- W2024915521 doi "https://doi.org/10.1016/0003-9861(81)90408-2" @default.
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