Human MnSOD and Cancer Research: Difference between revisions

Human Superoxide Dismutase (MnSOD) is a 22kD homotetrameric protein that is characterized by each subunit containing an N-terminus helical hairpin and alpha/beta domain that contribute to the catalytic site, the enzyme has four manganese active sites (Borgstahl et al). MnSOD alpha and beta C-terminus domains contain a “...three stranded antiparallel beta-sheet and five alpha-helices” (Borgstahl et al). The N-terminus helical hairpins are composed of “...two long antiparallel alpha-helices separated by a tight turn to form a helical hairpin” (Borgstahl et al). The active sites themselves are positioned between the helical and beta-sheet areas, while also joining the two domains (Borgstahl et al). A couple of amino acid residues from both domains and a water molecule are responsible for the ligation of Manganese (Borgstahl et al). The four active sites associate in pairs on either side of the enzyme.