Cu/Zn superoxide dismutase (SOD-1)

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Function

  • destroys O2- radicals which are normally produced within the cells & which are toxic to biological systems
  • operates at diffusion-limited rate
  • Zn+2 binding promotes dimerization
2 O2- + 2 H+ <--> O2 + H2O2

Cofactor:

  • binds 1 copper ion per subunit
  • binds 1 Zn+2 per subunit

Structure

homodimer

Compartment

cytoplasm

Pathology

Laboratory

More general terms

Additional terms

References

  1. Berry MJ et al Type I iodothyronine deiodinase is a selenocysteine-containing enzyme. Nature 349:438 1991 PMID: https://www.ncbi.nlm.nih.gov/pubmed/1825132
  2. Marklund SL Expression of extracellular superoxide dismutase by human cell lines. Biochem J 1990 Feb 15;266(1):213-9 PMID: https://www.ncbi.nlm.nih.gov/pubmed/2106874
  3. Rosen DR et al Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362:59 1993 PMID: https://www.ncbi.nlm.nih.gov/pubmed/8446170
  4. Alsod; Note: ALS genetic mutations db http://alsod.iop.kcl.ac.uk/Als/
  5. GeneReviews https://www.genecards.org/cgi-bin/carddisp.pl?gene=SOD1
  6. Wikipedia; superoxide dismutase entry http://en.wikipedia.org/wiki/superoxide_dismutase
  7. UniProt http://www.uniprot.org/uniprot/P00441.html

Database