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

Trx-2  -  thioredoxin-2

Drosophila melanogaster

Synonyms: 31884, CG31884, CG3864, DTrx-2, DmTrx-2, ...
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.

Psychiatry related information on Trx-2

  • Among these we emphasize the identification of proteins with molecular chaperone properties (heat shock proteins and PPIases) and protein spots involved in defense responses such as antioxidant and immunological defense mechanisms (thioredoxin, prophenoloxidase, and serine proteases), as well as in signal transduction pathways [1].

High impact information on Trx-2

  • Recombinant thioredoxin peroxidase-1 (subunit molecular mass = 23 kDa) was found to be a decameric protein that can efficiently use Trx-2 but not Trx-1 as a reducing substrate [2].
  • In its disulfide form, the 13-kDa protein thioredoxin-2 is a substrate of thioredoxin reductase-1 (K(m) = 5.2 microm, k(cat) = 14.5 s(-1)) and in its dithiol form, an electron donor for TPx-1 (K(m) = 9 microm, k(cat) = 5.4 s(-1)) [2].
  • DmTrx-2 is capable of reducing glutathione disulfide with a second order rate constant of 170 m(-1) s(-1) at pH 7.4 and 25 degrees C. Western blot analysis indicated that this thioredoxin represents up to 1% of the extractable protein of D. melanogaster Schneider cells or whole fruit flies [2].
  • Molecular modeling and homology considerations based on 450 GPxs suggest peculiar features to determine Trx specificity: (i) a non-aligned second Cys within the fourth helix that acts as C(R); (ii) deletions of the subunit interfaces typical of tetrameric GPxs leading to flexibility of the C(R)-containing loop [3].
  • Among the five ICs in Ciona, three are orthologs of those in sea urchin dynein: two are WD-repeat proteins and the third one, unique to metazoan sperm flagella, contains both thioredoxin and nucleoside diphosphate kinase modules [4].

Associations of Trx-2 with chemical compounds

  • The purified recombinant GoPrx was shown to reduce H(2)O(2) in the presence of electrons donated by dithiothreitol, but did not show the activity in the presence of thioredoxin as electron donor [5].

Analytical, diagnostic and therapeutic context of Trx-2


  1. Drosophila melanogaster larval hemolymph protein mapping. Guedes, S.d.e. .M., Vitorino, R., Tomer, K., Domingues, M.R., Correia, A.J., Amado, F., Domingues, P. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  2. Thioredoxin-2 but not thioredoxin-1 is a substrate of thioredoxin peroxidase-1 from Drosophila melanogaster: isolation and characterization of a second thioredoxin in D. Melanogaster and evidence for distinct biological functions of Trx-1 and Trx-2. Bauer, H., Kanzok, S.M., Schirmer, R.H. J. Biol. Chem. (2002) [Pubmed]
  3. The Thioredoxin Specificity of Drosophila GPx: A Paradigm for a Peroxiredoxin-like Mechanism of many Glutathione Peroxidases. Maiorino, M., Ursini, F., Bosello, V., Toppo, S., Tosatto, S.C., Mauri, P., Becker, K., Roveri, A., Bulato, C., Benazzi, L., De Palma, A., Floh??, L. J. Mol. Biol. (2007) [Pubmed]
  4. Molecular characterization of Ciona sperm outer arm dynein reveals multiple components related to outer arm docking complex protein 2. Hozumi, A., Satouh, Y., Makino, Y., Toda, T., Ide, H., Ogawa, K., King, S.M., Inaba, K. Cell Motil. Cytoskeleton (2006) [Pubmed]
  5. Molecular cloning and characterization of a peroxiredoxin gene from the mole cricket, Gryllotalpa orientalis. Kim, I., Lee, K.S., Hwang, J.S., Ahn, M.Y., Li, J., Sohn, H.D., Jin, B.R. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. (2005) [Pubmed]
WikiGenes - Universities