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- W2088396951 abstract "Inorganic pyrophosphatase activity is regulated by kinase-free phosphorylation. Phosphorylation by ATP activates the enzyme and that by Pi eliminates the activating effect of ATP. Acyl phosphate formed in the reaction with ATP is a covalent intermediate of ATP hydrolysis in the regulatory site of the enzyme. Therefore, kinase-free phosphorylation shares the properties of both regulatory and catalytic phosphorylations." @default.
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- W2088396951 date "1989-02-27" @default.
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- W2088396951 title "Regulation of enzymatic activity by kinase-free phosphorylation" @default.
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- W2088396951 doi "https://doi.org/10.1016/0014-5793(89)80543-5" @default.
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