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
Pathology
- point mutation in SOD1 gene are the cause of amyotrophic lateral sclerosis type 1
Laboratory
More general terms
Additional terms
References
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ Alsod; Note: ALS genetic mutations db http://alsod.iop.kcl.ac.uk/Als/
- ↑ GeneReviews https://www.genecards.org/cgi-bin/carddisp.pl?gene=SOD1
- ↑ Wikipedia; superoxide dismutase entry http://en.wikipedia.org/wiki/superoxide_dismutase
- ↑ UniProt http://www.uniprot.org/uniprot/P00441.html