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Literature summary for 6.5.1.8 extracted from

  • Tanaka, N.; Chakravarty, A.K.; Maughan, B.; Shuman, S.
    Novel mechanism of RNA repair by RtcB via sequential 2',3'-cyclic phosphodiesterase and 3'-phosphate/5'-hydroxyl ligation reactions (2011), J. Biol. Chem., 286, 43134-43143.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.5.1.8

Organism

Organism UniProt Comment Textmining
Escherichia coli P46850
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(ribonucleotide)n-2',3'-cyclophosphate + H2O
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 Escherichia coli (ribonucleotide)n-3'-phosphate
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 ?
(ribonucleotide)n-3'-(5'-diphosphoguanosine) + 5'-hydroxy-(ribonucleotide)m
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 Escherichia coli (ribonucleotide)n+m + GMP
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 ?
5'-guanosyl [RNA ligase]-Ntau-phosphono-L-histidine + (ribonucleotide)n-3'-phosphate
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 Escherichia coli (ribonucleotide)n-3'-(5'-diphosphoguanosine) + [RNA ligase]-L-histidine
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 ?
GTP + [RNA ligase]-L-histidine
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 Escherichia coli 5'-guanosyl [RNA ligase]-Ntau-phosphono-L-histidine + diphosphate
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 ?

General Information

General Information Comment Organism
physiological function RtcB ligates 3'-monophosphate and 5'-OH ends and has an intrinsic 2',3'-cyclic phosphodiesterase activity. The 2',3'-cyclic phosphodiesterase and ligase reactions both require manganese and are abolished by mutation of the RtcB active site. RtcB executes a unique two-step pathway of strand joining whereby the 2',3'-cyclic phosphodiester end is hydrolyzed to a 3'-monophosphate, which is then linked to the 5'-OH end to form the splice junction. The energy for the 3'-phosphate ligase activity is provided by GTP Escherichia coli