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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

PARS2  -  prolyl-tRNA synthetase 2, mitochondrial...

Homo sapiens

Synonyms: DKFZp727A071, ProRS, Prolyl-tRNA synthetase
 
 
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Disease relevance of PARS2

  • Previously, we showed that class II Escherichia coli proline-tRNA synthetase (ProRS) is capable of (1) weakly misactivating Ala, (2) hydrolyzing the misactivated Ala-AMP in a reaction known as pretransfer editing, and (3) deacylating a mischarged Ala-tRNA(Pro) variant via a post-transfer editing pathway [1].
 

High impact information on PARS2

  • We also demonstrate that M. jannaschii ProRS is a homodimeric enzyme that is functionally asymmetric; only one of the two active sites at a time is able to form prolyl-adenylate, and only one tRNA molecule binds per dimer [2].
  • The most potent analogue, 2-(4-bromo-phenyl)-6-chloro-8-methyl-4-quinolinecarboxylic acid, showed IC50 = 5 nM (Ca. ProRS) with high selectivity over the human enzyme [3].

References

  1. Functional role of the prokaryotic proline-tRNA synthetase insertion domain in amino acid editing. Wong, F.C., Beuning, P.J., Nagan, M., Shiba, K., Musier-Forsyth, K. Biochemistry (2002) [Pubmed]
  2. Asymmetric behavior of archaeal prolyl-tRNA synthetase. Ambrogelly, A., Kamtekar, S., Stathopoulos, C., Kennedy, D., Söll, D. FEBS Lett. (2005) [Pubmed]
  3. A series of quinoline analogues as potent inhibitors of C. albicans prolyl tRNA synthetase. Yu, X.Y., Hill, J.M., Yu, G., Yang, Y., Kluge, A.F., Keith, D., Finn, J., Gallant, P., Silverman, J., Lim, A. Bioorg. Med. Chem. Lett. (2001) [Pubmed]
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