| 别名 |
beta-NAD+ -dependent DNA ligase, beta-NAD+-dependent DNA ligase, Deoxyribonucleate ligase, Deoxyribonucleic acid joinase, Deoxyribonucleic acid ligase, Deoxyribonucleic joinase, Deoxyribonucleic ligase, Deoxyribonucleic repair enzyme, Deoxyribonucleic-joining enzyme, DNA joinase, DNA ligase, DNA ligase (NAD), DNA repair enzyme, DNA-joining enzyme, LigA, Ligase, polynucleotide (nicotinamide adenine dinucleotide), LigN, MimiLIG, MsEPV DNA ligase, MtuLigA, NAD(+)-dependent DNA ligase, NAD+ dependent DNA ligase, NAD+ DNA ligase, NAD+-dependent DNA ligase, NAD+-dependent DNA ligase A, NAD-dependent DNA ligase, NDL, Polydeoxyribonucleotide synthase (NAD+), Polydeoxyribonucleotide synthase [NAD+], Polynucleotide ligase, Polynucleotide synthetase, Polynucleotide synthetase (nicotinamide adenine dinucleotide), Rv3014c, Synthetase, polydeoxyribonucleotide (nicotinamide adenine dinucleotide), T4 DNA ligase, Taq DNA ligase, Tfi DNA ligase, Tth DNA ligase, wBm-LigA |
| Comments |
The enzyme, typically found in bacteria, catalyses the ligation of DNA strands with 3′-hydroxyl and 5′-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in duplex DNA. Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by NAD+, forming a phosphoramide bond between adenylate and a lysine residue. The adenylate group is then transferred to the 5′-phosphate terminus of the substrate, forming the capped structure 5′-(5′-diphosphoadenosine)-[DNA]. Finally, the enzyme catalyses a nucleophilic attack of the 3′-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the adenylate. RNA can also act as substrate, to some extent.?cf. EC?6.5.1.1, DNA ligase (ATP), EC?6.5.1.6, DNA ligase (ATP or NAD+), and EC?6.5.1.7, DNA ligase (ATP, ADP or GTP). |
