EC Number   |
Substrates |
Organism |
Products  |
Reversibility |
|---|
   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 | more |
enzyme does not discriminate between RNA and DNA for phosphodiester bond formation |
Methanothermobacter thermautotrophicus |
? |
- |
? |
| 6.5.1.3 | more |
intramolecular ligation of 5'-PO4 single-strand RNA to form a covalently closed circular RNA molecule through ligase-adenylylate and RNA-adenylylate intermediates AppRNA. At the optimal temperature of 65°C, AppRNA is predominantly ligated to a circular product. At 35°C, phosphodiester bond formation is suppressed and the majority of the AppRNA is deadenylylated |
Methanothermobacter thermautotrophicus |
? |
- |
? |
| 6.5.1.3 | more |
T4 RNA ligase possesses nick-joining activity in RNA/DNA hybrids against junctional matches/mismatches complementary to the RNA strand as a ligation template. When a junctional mismatch is present at the 30-terminal of RNA probe, the nick-joining activity of T4Rnl2 is inhibited |
Tequatrovirus T4 |
? |
- |
? |
| 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 | 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 |
? |
- |
? |
| 6.5.1.3 | more |
wheat RNA ligase contains 5'-hydroxyl kinase, 2',3'-cyclic phosphate 3'-phosphodiesterase, and 5'-phosphate 2'-phosphate-3'-hydroxyl RNA ligase activities |
Triticum aestivum |
? |
- |
? |
| 6.5.1.3 | more |
RtcA is able of cyclizing a 2'-phosphate RNA end in high yield. The rate of 2'-phosphate cyclization by RtcA is five orders of magnitude slower than 3'-phosphate cyclization, notwithstanding that RtcA binds with similar affinity to RNA3'p and RNA2'p substrates |
Escherichia coli |
? |
- |
? |
| 6.5.1.3 | more |
the enzyme catalyzes an adenylation reaction that is specific for ATP and either ssDNA or RNA. It does not require synthesis of a template strand for adenylation. To achieve quantitative DNA adenylation, single turnover reaction condition with substrate to enzyme ratio 1:1 should be used |
Methanothermobacter thermautotrophicus |
? |
- |
? |
| 6.5.1.3 | more |
the enzyme catalyzes formation of phosphodiester bonds between the 5'-phosphate and 3'-hydroxyl termini of single-stranded RNAs. It can also react with RNA with a 3'-phosphate end to generate a 2',3'-cyclic phosphate. The enzyme can additionally remove adenosine from the 3'-terminus of the RNA to produce 3'-deadenylated RNA |
Methanothermobacter thermautotrophicus |
? |
- |
? |
