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The burden of structural evidence favors the idea that an ATP-dependent ligase is the ancestral condition from which NAD+-dependent ligases evolved, by acquisition of the specialized structural area (Ia) that binds the NMN leaving group. All recognised NAD+-dependent ligases have domain Ia, and they can't use ATP as being a substrate for ligase adenylylation, presumably because LigA enzymes absence “motif IV” in the OB area, the ingredient of ATP-dependent DNA ligases that is believed to communicate with the PPi leaving team of ATP (5, 19). This “both/or” state of affairs of DNA ligase substrate specificity has actually been roiled by numerous seemingly conflicting experiences concerning the nucleotide specificity of archaeal DNA ligases.
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The undifferentiated nucleotide specificities of certain archaeal ligases have tantalizing implications for enzyme evolution and also the feasible use of ADP to be a substrate by ancestors of recent DNA ligases. The power of some archaeal ligases to use ATP and NAD+ or ATP and ADP as substrates may very well be described if they regarded only the ADP component prevalent to all 3 nucleotides.
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