Tightly bound pyrophosphate inEscherichia coliinorganic pyrophosphatase
А. А. Шестаков, Alexander A. Baykov, Svetlana M. Avaeva
Abstract
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А. А. Шестаков, Alexander A. Baykov, Svetlana M. Avaeva
Abstract
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Hexameric inorganic pyrophosphatase of Escherichia coli contains about 1 mol/mol of 'structural' pyrophosphate, which survives gel filtration and prolonged incubation with Mg2+, does not exchange with medium phosphate and pyrophosphate but is removed with 0.8 M perchloric acid. The site of pyrophosphate binding seems to be another than the active site. An additional 0.9 mol of enzyme-bound pyrophosphate is formed in the presence of phosphate and Mg2+ but this pyrophosphate is in fast equilibrium with medium phosphate and appears to be bound to the active site.
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Hexameric inorganic pyrophosphatase of Escherichia coli contains about 1 mol/mol of 'structural' pyrophosphate, which survives gel filtration and prolonged incubation with Mg2+, does not exchange with medium phosphate and pyrophosphate but is removed with 0.8 M perchloric acid. The site of pyrophosphate binding seems to be another than the active site. An additional 0.9 mol of enzyme-bound pyrophosphate is formed in the presence of phosphate and Mg2+ but this pyrophosphate is in fast equilibrium with medium phosphate and appears to be bound to the active site.
Key concepts: Pyrophosphate, Inorganic pyrophosphatase, Pyrophosphatases, Pyrophosphatase, Chemistry, Phosphate, Escherichia coli, Enzyme