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- W1486012839 abstract "Abstract Escherichia coli pyrophosphatase was inactivated by reaction with reagents which modify the e-amino groups of lysine residues. These reagents included 2,4,6-trinitrobenzene sulfonic acid (TNBS), potassium cyanate, diazonium-1H-tetrazole, and the anhydrides of maleic and succinic acids. The enzyme was unaffected by diisopropyl phosphorofluoridate, N-acetylimidazole, and sulfhydryl reagents (N-ethylmaleimide and p-hydroxymercuribenzoate). The inactivation by lysine-modifying agents followed pseudo first-order kinetics with respect to enzyme sites. Detailed analyses with TNBS indicated that interaction of 1 molecule with an enzyme lysine residue led to inactivation with a second-order rate constant of 86 m-1 min-1 in 0.5 m NaHCO3, pH 8.5. Inorganic pyrophosphate, a competitive inhibitor of the enzyme in the absence of divalent cation, partially protected against TNBS inactivation, but kinetic analyses of this effect showed that TNBS could react with the enzyme-pyrophosphate complex, although with a lower rate constant (52 m-1 min-1). These results can be interpreted either in terms of active site modification or effect on a lysine residue apart from the active site but whose integrity is essential for function of the enzyme." @default.
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- W1486012839 date "1970-09-01" @default.
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- W1486012839 title "Constitutive Inorganic Pyrophosphatase of Escherichia coli" @default.
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- W1486012839 doi "https://doi.org/10.1016/s0021-9258(19)63803-2" @default.
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