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Gene Review

SRXN1  -  sulfiredoxin 1

Homo sapiens

Synonyms: C20orf139, Npn3, SRX, SRX1, Sulfiredoxin-1, ...
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Disease relevance of SRXN1

  • Srx also has a role in the reduction of glutathionylation a post-translational, oxidative modification that occurs on numerous proteins and has been implicated in a wide variety of pathologies, including Parkinson's disease [1].

High impact information on SRXN1


Biological context of SRXN1


Associations of SRXN1 with chemical compounds

  • All Srx enzymes contain a conserved cysteine residue [3].
  • Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins [7].
  • Both glutathione and thioredoxin are potential physiological electron donors for the Srx reaction, given that their Km values (1.8 mM and 1.2 microM, respectively) are in the range of their intracellular concentrations, and the Vmax values obtained with the two reductants were similar [5].
  • We observed the exclusive formation of a thiosulfinate linkage between Prx and Srx (k = 1.4 min(-1)) that collapses to the disulfide-bonded Srx-Prx species (k = 0.14 min(-1)) [8].

Other interactions of SRXN1

  • This review discusses Srx as a novel antioxidant, and focuses on its potential role in the regulation of glutathionylation/deglutathionylation pathways, that have been implicated in a growing number of disease states [1].
  • Unlike, the reduction of Prx over-oxidation, Srx-dependent deglutathionylation appears to be non-specific [1].
  • Although Srx reduces sulfinic Prx III in vitro, it remains unclear whether the reduction of Prx III in cells is actually mediated by Srx [9].

Analytical, diagnostic and therapeutic context of SRXN1


  1. Sulfiredoxin: a potential therapeutic agent? Findlay, V.J., Tapiero, H., Townsend, D.M. Biomed. Pharmacother. (2005) [Pubmed]
  2. A novel role for human sulfiredoxin in the reversal of glutathionylation. Findlay, V.J., Townsend, D.M., Morris, T.E., Fraser, J.P., He, L., Tew, K.D. Cancer Res. (2006) [Pubmed]
  3. Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin. Jeong, W., Park, S.J., Chang, T.S., Lee, D.Y., Rhee, S.G. J. Biol. Chem. (2006) [Pubmed]
  4. The structure of the mammalian signal recognition particle (SRP) receptor as prototype for the interaction of small GTPases with Longin domains. Schlenker, O., Hendricks, A., Sinning, I., Wild, K. J. Biol. Chem. (2006) [Pubmed]
  5. Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine. Chang, T.S., Jeong, W., Woo, H.A., Lee, S.M., Park, S., Rhee, S.G. J. Biol. Chem. (2004) [Pubmed]
  6. Evolution of eukaryotic cysteine sulfinic acid reductase, sulfiredoxin (Srx), from bacterial chromosome partitioning protein ParB. Basu, M.K., Koonin, E.V. Cell Cycle (2005) [Pubmed]
  7. Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins. Woo, H.A., Jeong, W., Chang, T.S., Park, K.J., Park, S.J., Yang, J.S., Rhee, S.G. J. Biol. Chem. (2005) [Pubmed]
  8. Identification of intact protein thiosulfinate intermediate in the reduction of cysteine sulfinic acid in peroxiredoxin by human sulfiredoxin. Jönsson, T.J., Tsang, A.W., Lowther, W.T., Furdui, C.M. J. Biol. Chem. (2008) [Pubmed]
  9. Sulfiredoxin Translocation into Mitochondria Plays a Crucial Role in Reducing Hyperoxidized Peroxiredoxin III. Noh, Y.H., Baek, J.Y., Jeong, W., Rhee, S.G., Chang, T.S. J. Biol. Chem. (2009) [Pubmed]
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