The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

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

Homo sapiens

Synonyms: DKFZp727A071, ProRS, Prolyl-tRNA synthetase
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

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].


  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]
WikiGenes - Universities