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Literature summary for 3.1.4.58 extracted from

  • Makino, S.; Sawasaki, T.; Endo, Y.; Takai, K.
    In vitro dissection revealed that the kinase domain of wheat RNA ligase is physically isolatable from the flanking domains as a non-overlapping domain enzyme (2010), Biochem. Biophys. Res. Commun., 397, 762-766 .
    View publication on PubMed
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Organism

Organism UniProt Comment Textmining
Triticum aestivum
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information RNA ligase contains 5'-hydroxyl kinase, 2',3'-cyclic phosphate 3'-phosphodiesterase, and 5'-phosphate 2'-phosphate-3'-hydroxyl RNA ligase activities Triticum aestivum ?
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Subunits

Subunits Comment Organism
More RNA ligase contains 5'-hydroxyl kinase, 2',3'-cyclic phosphate 3'-phosphodiesterase, and 5'-phosphate 2'-phosphate-3'-hydroxyl RNA ligase activities. Each of the three activities can be assigned to a non-overlapping domain that does not require the presence of the other part(s) of the enzyme for its activity. The CPD activity is located on the residues 886-1042 fragment Triticum aestivum

General Information

General Information Comment Organism
physiological function RNA ligase contains 5'-hydroxyl kinase, 2',3'-cyclic phosphate 3'-phosphodiesterase, and 5'-phosphate 2'-phosphate-3'-hydroxyl RNA ligase activities. Each of the three activities can be assigned to a non-overlapping domain that does not require the presence of the other part(s) of the enzyme for its activity. The CPD activity is located on the residues 886-1042 fragment Triticum aestivum