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Information on EC 6.5.1.3 - RNA ligase (ATP) and Organism(s) Trypanosoma brucei brucei and UniProt Accession P86927

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EC Tree
IUBMB 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.
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Trypanosoma brucei brucei
UNIPROT: P86927
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The taxonomic range for the selected organisms is: Trypanosoma brucei brucei
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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ATP
+
(deoxyribonucleotide)n-3'-hydroxyl
+
5'-phospho-(deoxyribonucleotide)m
=
(deoxyribonucleotide)n+m
+
AMP
+
beta-nicotinamide D-nucleotide
+
+
5'-phospho-(deoxyribonucleotide)m
=
+
+
beta-nicotinamide D-nucleotide
Synonyms
rna ligase, t4 rna ligase, t4 rna ligase 2, tbrel1, drarnl, t4 rna ligase 1, rna ligase ribozyme, class i ligase, rna editing ligase 1, atp-dependent rna ligase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Polynucleotide synthetase
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Polyribonucleotide ligase
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Polyribonucleotide synthase (ATP)
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Ribonucleic ligase
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RNA ligase
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Synthetase, polyribonucleotide
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SYSTEMATIC NAME
IUBMB Comments
poly(ribonucleotide)-3'-hydroxyl:5'-phospho-poly(ribonucleotide) ligase (ATP)
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.
CAS REGISTRY NUMBER
COMMENTARY hide
37353-39-2
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