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• W1996743355 abstract "The 2′,3′-dialdehydes of ADP and ATP (oADP and oATP), obtained by periodate oxidation of ADP and ATP, inhibited the hydrolytic activity of the purified Ca2+.Mg2+-activated ATPase of Escherichia coli. Nonspecific labeling of amino groups by these dialdehydes was corrected by carrying out the reactions in the presence of 15 mm ATP. Two types of modification of “ATP-protectable” binding sites by oATP could be detected. The binding of 2 mol “ATP-protectable” oATP/mol ATPase was without affect on ATPase activity and still occurred in the hydrolytically inactive ATPase of an unc A mutant. The binding of a further 3 mol “ATP-protectable” oATP/mol ATPase resulted in almost complete loss of ATPase activity although much of the loss occurred during the binding of the first additional molecule of oATP. This additional ATP-protectable oATP binding did not occur in the unc A mutant and so resembled both the inhibitory effect of oADP on the ATPase activity of normal strains and its lack of binding to the unc A ATPase (P. D. Bragg and C. Hou, 1980, Biochem. Biophys. Res. Commun.95, 952–957). The “ATP-protectable” binding sites for oADP and oATP were located on the α subunit of the ATPase. Binding of oADP or oATP did not result in release of the tightly bound ADP and ATP from the enzyme. We conclude that separate binding sites for oADP and oATP occur on the α subunits of the E. coli ATPase and that the former may be the active site(s) for ATP hydrolysis while the latter are involved in regulation of the ATPase complex." @default.
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• W1996743355 date "1981-04-01" @default.
• W1996743355 modified "2023-09-26" @default.
• W1996743355 title "Affinity labeling of purified Ca2+,Mg2+-activated ATPase of Escherichia coli by the 2′,3′-dialdehydes of adenosine 5′-di- and triphosphates" @default.
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• W1996743355 doi "https://doi.org/10.1016/0003-9861(81)90036-9" @default.
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