Abstract
Abstract Polynucleotide ligase, isolated from Escherichia coli infected with bacteriophage T4, catalyzes (a) the repair of an interrupted strand in a DNA duplex by the formation of phosphodiester bonds, with a concomitant cleavage of ATP to AMP and PPi, and (b) an ATP-PPi exchange reaction which is not dependent on the presence of DNA. The two activities elute together from diethylaminoethyl cellulose and phosphocellulose. An enzyme-adenylate complex has been isolated and is found to mediate both the formation of phosphodiester bonds in the absence of ATP and the formation of ATP from PPi. These findings suggest that as the first step of the ligase reaction, ATP and enzyme react to form an enzyme-adenylate intermediate accompanied by the release of PPi.
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