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Study Progress of Cu,Zn Superoxide Dismutas——From Gene to Function / 现代生物医学进展
Progress in Modern Biomedicine ; (24): 940-943, 2008.
Article in Chinese | WPRIM | ID: wpr-737079
ABSTRACT
Superoxide Dismutase (SOD)(EC 1.15.1.1)is a metalloenzyme that is found in almost all organisms and catalyzes the dismutation of superoxide anion radical to hydrogen peroxide and molecular oxygen. Three unique and highly compartmentalized mammalian SOD have been biochemically and molecularly characterized to date Cu, Zn superoxide dismutase (CuZnSOD, SOD1), MnSOD (Manganese Superoxide Dismutase, SOD2)and EC-SOD (Extracellular Superoxide Dismutase, SOD3). Cu, Zn superoxide dismutase (CuZnSOD, SOD1)is a copper and zinc-containing homodimer that is found almost exclusively in intracellular cytoplasmic spaces. CuZnSOD is widely distributed and comprises about 90% of the total SOD. Cytoplasmic and periplasmic SOD exists as dimers,whereas chloroplastic and extracellular enzymes exist as tetramers. Structure supports independent functional evolution in prokaryotes and eukaryotes. CuZnSOD are thought to protect the brain, lungs, and other tissues from oxidative stress. This paper reviewed the gene, molecular and chemical structure and biological function of CuZnSOD.

Full text: Available Index: WPRIM (Western Pacific) Language: Chinese Journal: Progress in Modern Biomedicine Year: 2008 Type: Article

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Full text: Available Index: WPRIM (Western Pacific) Language: Chinese Journal: Progress in Modern Biomedicine Year: 2008 Type: Article