title: Regulation of enzymatic activity by kinase-free phosphorylation.
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.
authors.affiliation: A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
authors.forename: A V
authors.initials: AV
authors.lastname: Vener
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D006868:Hydrolysis; D043564:Inorganic Pyrophosphatase; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D010758:Phosphorus; D010766:Phosphorylation; D011755:Pyrophosphatases / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology
chemical_list: D010758:Phosphorus; D000255:Adenosine Triphosphate; D011755:Pyrophosphatases; D043564:Inorganic Pyrophosphatase