Entry |
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Name |
RNA ligase (ATP);
polyribonucleotide synthase (ATP);
RNA ligase;
polyribonucleotide ligase;
ribonucleic ligase;
poly(ribonucleotide):poly(ribonucleotide) ligase (AMP-forming)
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Class |
Ligases;
Forming phosphoric-ester bonds;
Ligases that form phosphoric-ester bonds (only sub-subclass identified to date)
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Sysname |
poly(ribonucleotide)-3'-hydroxyl:5'-phospho-poly(ribonucleotide) ligase (ATP)
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Reaction(IUBMB) |
ATP + (ribonucleotide)n-3'-hydroxyl + 5'-phospho-(ribonucleotide)m = (ribonucleotide)n+m + AMP + diphosphate (overall reaction) [RN: R07640];
(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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Reaction(KEGG) |
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Substrate |
ATP [CPD: C00002];
(ribonucleotide)n-3'-hydroxyl;
5'-phospho-(ribonucleotide)m;
[RNA ligase]-L-lysine;
[RNA ligase]-N6-(5'-adenylyl)-L-lysine;
5'-(5'-diphosphoadenosine)-(ribonucleotide)m
|
Product |
(ribonucleotide)n+m [CPD: C00046];
AMP [CPD: C00020];
diphosphate [CPD: C00013];
[RNA ligase]-N6-(5'-adenylyl)-L-lysine;
5'-(5'-diphosphoadenosine)-(ribonucleotide)m;
[RNA ligase]-L-lysine
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Comment |
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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History |
EC 6.5.1.3 created 1976, modified 2016
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Orthology |
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Genes |
» show all
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Reference |
|
Authors |
Silber R, Malathi VG, Hurwitz J. |
Title |
Purification and properties of bacteriophage T4-induced RNA ligase. |
Journal |
|
Reference |
|
Authors |
Cranston JW, Silber R, Malathi VG, Hurwitz J |
Title |
Studies on ribonucleic acid ligase. Characterization of an adenosine triphosphate-inorganic pyrophosphate exchange reaction and demonstration of an enzyme-adenylate complex with T4 bacteriophage-induced enzyme. |
Journal |
J Biol Chem 249:7447-56 (1974) |
Reference |
|
Authors |
Sugino A, Snoper TJ, Cozzarelli NR |
Title |
Bacteriophage T4 RNA ligase. Reaction intermediates and interaction of substrates. |
Journal |
J Biol Chem 252:1732-8 (1977) |
Reference |
|
Authors |
Romaniuk PJ, Uhlenbeck OC |
Title |
Joining of RNA molecules with RNA ligase. |
Journal |
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Reference |
|
Authors |
Ho CK, Wang LK, Lima CD, Shuman S |
Title |
Structure and mechanism of RNA ligase. |
Journal |
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Reference |
|
Authors |
Nandakumar J, Shuman S, Lima CD |
Title |
RNA ligase structures reveal the basis for RNA specificity and conformational changes that drive ligation forward. |
Journal |
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Other DBs |
ExplorEnz - The Enzyme Database: | 6.5.1.3 |
ExPASy - ENZYME nomenclature database: | 6.5.1.3 |
BRENDA, the Enzyme Database: | 6.5.1.3 |
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LinkDB |
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