Regulation of enzymatic activity by kinase-free phosphorylation |
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| Authors: | A V Vener |
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| Affiliation: | A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR. |
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| 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. |
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