EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
6.5.1.3 | more |
the enzyme is unreactive with a 5'-32P-labeled single-strand 18-mer pDNA substrate |
Naegleria gruberi |
? |
- |
? |
6.5.1.3 | more |
the enzyme seals nicked 3'-OH/5'-PO4 duplexes in which the 3'-OH strand is RNA. The enzyme entails reaction with ATP to form a covalent enzyme-AMP intermediate, transfer of AMP to the nick 5'-PO4, and attack of the RNA 3'-OH on the adenylylated nick to form a 3'-5' phosphodiester |
Naegleria gruberi |
? |
- |
? |
6.5.1.3 | more |
the group I intron from cyanobacterium Anabaena sp. catalyzes phosphodiester bond formation using a triphosphate on the 5'-terminal nucleotide, much like protein polymerases and engineered ribozymes. In the process, this ribozyme forms a unique circular RNA that incorporates the exogenous guanosine cofactor added during self-splicing |
Anabaena sp. |
? |
- |
? |
6.5.1.3 | ATP + (ribonucleotide)n + (ribonucleotide)m |
the kinetic mechanism of single-turnover nick sealing by T4 Rnl2-AMP is explored by using a rapid mix-quench method and the effects of 3'-OH mispairs and base damage lesions on the rates of nick 5'-adenylylation and phosphodiester synthesis is determined. With respect to the sealing of perfectly paired nicks the rates of step 2 catalysis are rapid (9.5-17.9/sec) and similar in magnitude to the step 3 rates (7.9-32/sec). Rnl2 is kinetically sensitive to all 3'-OH base mispairs |
Tequatrovirus T4 |
AMP + diphosphate + (ribonucleotide)n+m |
- |
? |
6.5.1.3 | ATP + (ribonucleotide)n + (ribonucleotide)m |
the L1 ligase is regioselective for formation of the biologically relevant 5' to 3' phosphodiester bond rather than a 5' to 2' bond |
Enterobacteria phage L1 |
AMP + diphosphate + (ribonucleotide)n+m |
- |
? |
6.5.1.3 | more |
the RNA ligase has a a strict requirement for RNA substrates with a 2'-phosphate terminus for the ligation of RNAs with 5'-phosphate and 3'-hydroxyl ends. RNA ligase forms a 2'-phosphomonoester-3',5'-phosphodiester junction |
Branchiostoma floridae |
? |
- |
? |
6.5.1.3 | ATP + (ribonucleotide)n + (ribonucleotide)m |
the TS2126 RNA ligase catalyzes both inter- and intra-molecular single-stranded DNA ligation to more than 50% completion in not more than a few hours at an elevated temperature, although favoring intramolecular ligation on RNA and single-stranded DNA substrates |
Phage TS2126 |
AMP + diphosphate + (ribonucleotide)n+m |
- |
? |
6.5.1.3 | ATP + (ribonucleotide)n + (ribonucleotide)m |
Trl1 executes the end-healing and end-sealing steps of tRNA splicing, requires a 2'-PO4 end for tRNA splicing in vivo |
Saccharomyces cerevisiae |
AMP + diphosphate + (ribonucleotide)n+m |
- |
? |
6.5.1.3 | ATP + etidronate |
weak activity |
Tequatrovirus T4 |
? |
- |
? |
6.5.1.3 | more |
wheat RNA ligase can be dissected into three isolated domain enzymes that are responsible for its core ligase, 5'-kinase, and 2',3'-cyclic phosphate 3'-phosphodiesterase activities, respectively. A side reaction on 5'-tri/diphosphate RNAs is dependent on ATP, a 2'-phosphate-3'-hydroxyl end, and the ligase domain. Two RNA molecules having 5'-hydroxyl and 2',3'-cyclic monophosphate groups are ligated almost stoichiometrically after separate conversion of respective terminal phosphate states into reactive ones |
Triticum aestivum |
? |
- |
? |