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- W2056521487 abstract "1. Phosphorolytic cleavage of Ap4A was demonstrated in cell-free extracts from two protozoan organisms, Euglena gracilis and Acanthamoeba castellanii. 2. A specific dinucleoside oligophosphate (DNOP) α,β-phosphorylase which degrades substrates with formation of corresponding nucleoside 5'-diphosphate (NDP) as one of the reaction products was purified 625-fold from Euglena gracilis cells. 3. In addition to Ap4A, the phosphorylase degrades Ap3A, Ap5A, Gp4G and one of phosphonate analogs, ApppCH2pA. The Km values for Ap4 A and Ap3A are 27 and 25 μM, and relative velocities 100 and 14, respectively. The Km for phosphate is 0.5 mM. 4. Some anions (arsenate, chromate, molybdate and vanadate) can substitute for phosphate in the catalyzed reactions and in their presence the DNOPs yield corresponding nucleoside 5'-monophosphate as one of the reactions' product. The enzyme supports also an anion-dependent dephosphorylation of NDPs. 5. Molecular weight of the native Euglena phosphorylase is 30,000. Optimum pH for its activity is at 8.0 Divalent metal cations are essential for the phosphorolysis of DNOPs but are not for the NDP dephosphorylation mentioned." @default.
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- W2056521487 date "1988-01-01" @default.
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- W2056521487 title "Specific phosphorylase from euglena gracilis splits diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A and diadenosine 5',5'''-P1,P3-triphosphate (Ap3A" @default.
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- W2056521487 doi "https://doi.org/10.1016/0020-711x(88)90214-5" @default.
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