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Your query returned 1 entry. Printable version
EC | 6.5.1.3 | ||||||||||||
Accepted name: | RNA ligase (ATP) | ||||||||||||
Reaction: | ATP + (ribonucleotide)n-3′-hydroxyl + 5′-phospho-(ribonucleotide)m = (ribonucleotide)n+m + AMP + diphosphate (overall reaction) (1a) ATP + [RNA ligase]-L-lysine = [RNA ligase]-N6-(5′-adenylyl)-L-lysine + diphosphate (1b) [RNA ligase]-N6-(5′-adenylyl)-L-lysine + 5′-phospho-(ribonucleotide)m = 5′-(5′-diphosphoadenosine)-(ribonucleotide)m + [RNA ligase]-L-lysine (1c) (ribonucleotide)n-3′-hydroxyl + 5′-(5′-diphosphoadenosine)-(ribonucleotide)m = (ribonucleotide)n+m + AMP |
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Other name(s): | polyribonucleotide synthase (ATP); RNA ligase; polyribonucleotide ligase; ribonucleic ligase; poly(ribonucleotide):poly(ribonucleotide) ligase (AMP-forming) | ||||||||||||
Systematic name: | poly(ribonucleotide)-3′-hydroxyl:5′-phospho-poly(ribonucleotide) ligase (ATP) | ||||||||||||
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. | ||||||||||||
Links to other databases: | BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 37353-39-2 | ||||||||||||
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