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Gene Review

ECs3448  -  thioredoxin 2

Escherichia coli O157:H7 str. Sakai

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Disease relevance of ECs3448


High impact information on ECs3448


Chemical compound and disease context of ECs3448


Biological context of ECs3448

  • Trx2 contains two distinct domains: an N-terminal domain of 32 amino acids including two CXXC motifs and a C-terminal domain, with the conserved active site, Trp-Cys-Gly-Pro-Cys, showing high homology to the prokaryotic thioredoxins [7].
  • This suggests that Trx2 may play a role in the cellular defense against oxidative stress [1].
  • Thus when E. coli TrxA is combined in a recombinant fusion protein with P. haemolytica A1 Gcp, productive folding of the glycoprotease can occur as a result of the chaperone action of the protein disulfide reductase coupled with its ability to retain the fusion gene product in the E. coli cytoplasm [9].

Anatomical context of ECs3448


Associations of ECs3448 with chemical compounds

  • A truncated form of the protein, lacking the N-terminal domain, is insensitive to the presence of dithiothreitol, further confirming the involvement of the additional cysteine residues in modulating Trx2 activity [7].
  • Thus, under aerobic conditions selenite catalyzed, NADPH-dependent redox cycling with oxygen, a large oxygen-dependent consumption of NADPH and oxidation of reduced thioredoxin inhibiting its disulfide-reductase activity [11].

Other interactions of ECs3448


Analytical, diagnostic and therapeutic context of ECs3448


  1. Thioredoxin 2, an oxidative stress-induced protein, contains a high affinity zinc binding site. Collet, J.F., D'Souza, J.C., Jakob, U., Bardwell, J.C. J. Biol. Chem. (2003) [Pubmed]
  2. The N-terminal domain of PILB from Neisseria meningitidis is a disulfide reductase that can recycle methionine sulfoxide reductases. Wu, J., Neiers, F., Boschi-Muller, S., Branlant, G. J. Biol. Chem. (2005) [Pubmed]
  3. The primary structure of thioredoxin from the filamentous cyanobacterium Anabaena sp. 7119. Gleason, F.K., Whittaker, M.M., Holmgren, A., Jörnvall, H. J. Biol. Chem. (1985) [Pubmed]
  4. Characterization of Mycobacterium tuberculosis WhiB1/Rv3219 as a protein disulfide reductase. Garg, S.K., Suhail Alam, M., Soni, V., Radha Kishan, K.V., Agrawal, P. Protein Expr. Purif. (2007) [Pubmed]
  5. Conversion of a peroxiredoxin into a disulfide reductase by a triplet repeat expansion. Ritz, D., Lim, J., Reynolds, C.M., Poole, L.B., Beckwith, J. Science (2001) [Pubmed]
  6. Protein levels of Escherichia coli thioredoxins and glutaredoxins and their relation to null mutants, growth phase, and function. Potamitou, A., Holmgren, A., Vlamis-Gardikas, A. J. Biol. Chem. (2002) [Pubmed]
  7. Cloning, expression, and characterization of a novel Escherichia coli thioredoxin. Miranda-Vizuete, A., Damdimopoulos, A.E., Gustafsson, J., Spyrou, G. J. Biol. Chem. (1997) [Pubmed]
  8. Identification of a coenzyme A--glutathione disulfide (DSI), a modified coenzyme A disulfide (DSII), and a NADPH-dependent coenzyme A--glutathione disulfide reductase in E. coli. Loewen, P.C. Can. J. Biochem. (1977) [Pubmed]
  9. Refolding of recombinant Pasteurella haemolytica A1 glycoprotease expressed in an Escherichia coli thioredoxin gene fusion system. Watt, M.A., Lo, R.Y., Mellors, A. Cell Stress Chaperones (1997) [Pubmed]
  10. Mutations of the membrane-bound disulfide reductase DsbD that block electron transfer steps from cytoplasm to periplasm in Escherichia coli. Cho, S.H., Beckwith, J. J. Bacteriol. (2006) [Pubmed]
  11. Selenite is a substrate for calf thymus thioredoxin reductase and thioredoxin and elicits a large non-stoichiometric oxidation of NADPH in the presence of oxygen. Kumar, S., Björnstedt, M., Holmgren, A. Eur. J. Biochem. (1992) [Pubmed]
  12. Bacterial defenses against oxidants: mechanistic features of cysteine-based peroxidases and their flavoprotein reductases. Poole, L.B. Arch. Biochem. Biophys. (2005) [Pubmed]
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