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Regulation of enzymatic activity by kinase-free phosphorylation
1A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
FEBS Letters
|February 27, 1989
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.