Abstract
DNA ligases are polypeptides that catalyze phosphodiester bond formation during DNA replication, recombination, and repair. These enzymes, along with RNA ligases and mRNA capping enzymes, belong to a superfamily of nucleotidyl transferases. DNA ligases can be subdivided into two groups based on cofactor specificity. Prokaryotic enzymes utilize either nicotinamide adenine dinucleotide or adenosine triphosphate (ATP) as a cofactor, whereas viral, archael, and eukaryotic DNA ligases use ATP almost exclusively. Eukaryotic ATP-dependent DNA ligases are subdivided into three families with members of the DNA ligase III family being restricted to vertebrates. DNA ligases are comprised of a common catalytic region that encircles the DNA substrate during ligation and divergent N- and C-terminal flanking regions that mediate the specific participation of DNA ligases in different DNA transactions through interactions with different partner proteins.
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