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Cu/Zn superoxide dismutase (SOD-1)
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:
- point mutation in SOD1 gene are the cause of amyotrophic lateral sclerosis type 1
Laboratory:
- SOD1 gene mutation
Related
copper chaperone for superoxide dismutase; superoxide dismutase copper chaperone (CCS)
superoxide dismutase-1 gene; Cu/Zn superoxide dismutase gene (SOD1)
General
oligomerizing protein
superoxide dismutase
Properties
SIZE: entity length = 154 aa
MW = 16 kD
COMPARTMENT: cytoplasm
MOTIF: copper [Cu]-binding site
SITE: 47-47
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 49-49
MOTIF: histidine residue (3)
cysteine residue {C58}
MODIFICATION: cysteine residue {C147}
copper [Cu]-binding site
SITE: 64-64
MOTIF: histidine residue (3)
Zn+2-binding site
SITE: 64-64
Zn+2-binding site
SITE: 72-72
Zn+2-binding site
SITE: 81-81
Zn+2-binding site
SITE: 84-84
copper [Cu]-binding site
SITE: 121-121
MOTIF: histidine residue (3)
cysteine residue {C147}
MODIFICATION: cysteine residue {C58}
Database Correlations
OMIM correlations
MORBIDMAP 147450
UniProt P00441
Pfam PF00080
Kegg hsa:6647
ENZYME 1.15.1.1
References
- Berry MJ et al
Type I iodothyronine deiodinase is a selenocysteine-containing
enzyme.
Nature 349:438 1991
PMID: 1825132
- Marklund SL
Expression of extracellular superoxide dismutase by human
cell lines.
Biochem J 1990 Feb 15;266(1):213-9
PMID: 2106874
- Rosen DR et al
Mutations in Cu/Zn superoxide dismutase gene are associated
with familial amyotrophic lateral sclerosis.
Nature 362:59 1993
PMID: 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 :accession P00441