Slight sequence variations of a common fold explain the substrate specificities of tRNA-guanine transglycosylases from the three kingdoms.

@article{Romier1997SlightSV,
  title={Slight sequence variations of a common fold explain the substrate specificities of tRNA-guanine transglycosylases from the three kingdoms.},
  author={Christophe Romier and Joachim E. W. Meyer and Dietrich Suck},
  journal={FEBS letters},
  year={1997},
  volume={416 1},
  pages={93-8}
}
tRNA-guanine transglycosylases (TGTs) are the enzymes catalyzing the base exchange required for the synthesis of the modified bases derived from 7-deazaguanine in prokaryotic, archaebacterial, and eukaryotic tRNAs. Unlike the eukaryotic and archaebacterial enzymes, the prokaryotic TGTs have been clearly identified and highly characterized both biochemically and structurally. The recent occurrence in sequence databases of archaebacterial and eukaryotic proteins homologous to the prokaryotic TGTs… CONTINUE READING

From This Paper

Figures, tables, results, connections, and topics extracted from this paper.
11 Extracted Citations
0 Extracted References
Similar Papers

Citing Papers

Publications influenced by this paper.
Showing 1-10 of 11 extracted citations

Similar Papers

Loading similar papers…