| 别名 |
ATP-dependent RNA ligase, b1-10t, bacteriophage RNA ligase, band IV protein, class I ligase, class I RNA ligase ribozyme, DraRnI, DraRnl, DREL, gp24.1, P52, phage Rnl2, Polynucleotide synthetase, Polyribonucleotide ligase, Polyribonucleotide synthase (ATP), REL1, Ribonucleic ligase, ribonucleprotein editing complex, RM378 RNA ligase, RNA editing ligase 1, RNA ligase, RNA ligase (ATP), RNA ligase 1, RNA ligase 2, RNA ligase ribozyme, RNA-editing ligase 1, RNL, Rnl1, Rnl2, Rnl5, RnlA, RtcA, rtcB, Synthetase, polyribonucleotide, T4 RNA ligase, T4 RNA ligase 1, T4 RNA ligase 2, T4Rnl2, TbMP52, TbREL1, thermostable RNA ligase 1, Trl1 |
| Comments |
The enzyme catalyses the ligation of RNA strands with 3′-hydroxyl and 5′-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in RNA. Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by ATP, 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)-[RNA]. 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. |
