EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
  6.5.1.B1 | 3'-half-tRNA molecule with a 5'-OH end + 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end |
the reaction occurs possible through a one-step reaction involving hydrolysis of the 2',3'-cyclic phosphodiester bond and the simultaneous formation of a 2'-5'-phosphodiester bond. The reaction proceeds without added ATP or NAD+ |
Escherichia coli |
mature tRNA molecule containing a 2'-5'-phosphodiester bond |
- |
? |
| 6.5.1.B1 | 3'-half-tRNA molecule with a 5'-OH end + 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end |
the reaction occurs possible through a one-step reaction involving hydrolysis of the 2',3'-cyclic phosphodiester bond and the simultaneous formation of a 2'-5'-phosphodiester bond. The reaction proceeds without added ATP or NAD+. The enzyme from Escherichia coli specifically ligates tRNA half-molecules (from Saccharomyces cerevisiae) containing nucleoside base modifications forming a 2'-5' phosphodiester bond at the ligated junction and shows a preference among different tRNA species, reversible in vitro. Yeast extract-modified pre-tRNATyr are the most active substrates tested for ligation by the Escherichia coli RNA ligase. tRNAPhe half-molecules produced by digestion of T7-transcribed pre-tRNAPhe with Saccharomyces cerevisiae tRNA splicing endonuclease are poorly ligated in Escherichia coli extracts |
Escherichia coli |
mature tRNA molecule containing a 2'-5'-phosphodiester bond |
- |
r |
| 6.5.1.B1 | more |
the apparent requirement of Escherichia coli 2'-5' ligase for nucleoside modifications and the preference shown by this enzyme for a subset of Saccharomyces cerevisiae tRNA splicing substrates suggest that the Escherichia coli ligase is likely to act upon a tRNA or tRNA-like molecule in vivo. The tight binding of the RNA ligase to immobilized prokaryotic and eukaryotic tRNA provides evidence that the ligase recognizes a tRNA or tRNA-like substrate in vivo |
Escherichia coli |
? |
- |
? |
