Peculiar inhibition of human mitochondrial aspartyl-tRNA synthetase by adenylate analogs.

@article{Messmer2009PeculiarIO,
  title={Peculiar inhibition of human mitochondrial aspartyl-tRNA synthetase by adenylate analogs.},
  author={Marie Messmer and S{\'e}bastien P. Blais and Christian Balg and Robert Ch{\^e}nevert and Luc Grenier and Patrick Lag{\"u}e and Claude Sauter and Marie Sissler and Richard Gieg{\'e} and Jacques Lapointe and Catherine Florentz},
  journal={Biochimie},
  year={2009},
  volume={91 5},
  pages={596-603}
}
Human mitochondrial aminoacyl-tRNA synthetases (mt-aaRSs), the enzymes which esterify tRNAs with the cognate specific amino acid, form mainly a different set of proteins than those involved in the cytosolic translation machinery. Many of the mt-aaRSs are of bacterial-type in regard of sequence and modular structural organization. However, the few enzymes investigated so far do have peculiar biochemical and enzymological properties such as decreased solubility, decreased specific activity and… CONTINUE READING

Similar Papers

Loading similar papers…