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Tightly bound pyrophosphate in Escherichia coli inorganic pyrophosphatase.

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.[1]


  1. Tightly bound pyrophosphate in Escherichia coli inorganic pyrophosphatase. Shestakov, A.A., Baykov, A.A., Avaeva, S.M. FEBS Lett. (1990) [Pubmed]
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