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- W76080475 abstract "SUMMARY treatment. A simple procedure is described for the purification, from rat None of a variety of other monophosphate and diphosphate liver, of a diphosphatase activity which cleaves both fructose esters tested as substrates was cleaved by the purified enzyme diphosphate and sedoheptulose diphosphate to fructose 6-phos- at significant rates. These results suggest an absolute require- phate and sedoheptulose 7-phosphate, respectively. ment for the presence of two phosphate groups and also for the Evidence that a single enzyme is responsible for both reactions configuration found in FDP and SDP. n-Bibulose 1,5-diphos- is derived from the results of the purification steps, from kinetic phate differs in the configuration at C-3 and is not attacked. measurements, and from other properties. The enzyme has no With respect to the physiological role of the diphosphatase, activity with a variety of monophosphate esters and other di- although it has been generally recognized that fructose diphos- phosphate esters. phatase may represent a key enzyme in the synthesis of glycogen Both activities are present in the liver of all mammalian species from 3 carbon fragments, no direct evidence for a role of sedo- studied. heptulose diphosphatase has yet been obtained. REFERENCES Three possibilities may be considered with respect to the physiological significance of the latter activity. (a) It may be 1. GOMORI, G., J." @default.
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- W76080475 date "1963-10-01" @default.
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- W76080475 title "Cleavage of Sedoheptulose 1,7-Diphosphate by a Purified Rat Liver Diphosphatase" @default.
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- W76080475 doi "https://doi.org/10.1016/s0021-9258(18)48639-5" @default.
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