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<< < Results 91 - 100 of 103 > >>
EC Number
Substrates
Commentary Substrates
Organism
Products
Commentary (Products)
Reversibility
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no activity with alendronate nor pamidronate
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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
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enzyme does not discriminate between RNA and DNA for phosphodiester bond formation
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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
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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
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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
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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
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wheat RNA ligase contains 5'-hydroxyl kinase, 2',3'-cyclic phosphate 3'-phosphodiesterase, and 5'-phosphate 2'-phosphate-3'-hydroxyl RNA ligase activities
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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
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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
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<< < Results 91 - 100 of 103 > >>