Comparison of genetic structure of the Cu,Zn superoxide dismutase (SOD1) from Cordyceps militaris, Paecillomyces tenuipes and P.sinensis

  • Park, Nam-Sook (College of Natural Resources and Life Science, Dong-A University) ;
  • Lee, Sang-Mong (Department of Sericultural and Entomological Biology, Miryang National University) ;
  • Sohn, Hung-Dae (College of Natural Resources and Life Science, Dong-A University) ;
  • Jin, Byung-Rae (College of Natural Resources and Life Science, Dong-A University)
  • Published : 2003.10.01

Abstract

Superoxide dismutase (SOD), one of the essential element of the antioxidant defense system, mainly removes $O^{-10}$ $_2$ and also prevents $O^{-10}$ $_2$ mediated reduction of iron and subsequent OH$^{-10}$ generation, which is highly toxic to the organism. Of these SOD enzymes, Cu, Zn-containing SOD (SODI) is an important component of the antioxidant defense system in eucaryotic cells. The SODI enzyme binds one copper and one zinc ion and displays the Greek Key $\beta$-barrel fuld. (omitted)

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