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ABSTRACT:
SUBMITTER: Furukawa Y
PROVIDER: S-EPMC1150991 | biostudies-literature | 2004 Jul
REPOSITORIES: biostudies-literature
Furukawa Yoshiaki Y Torres Andrew S AS O'Halloran Thomas V TV
The EMBO journal 20040624 14
The antioxidant enzyme Cu,Zn-superoxide dismutase (SOD1) has the distinction of being one of the most abundant disulfide-containing protein known in the eukaryotic cytosol; however, neither catalytic nor physiological roles for the conserved disulfide are known. Here we show that the disulfide status of Saccharomyces cerevisiae SOD1 significantly affects the monomer-dimer equilibrium, the interaction with the copper chaperone CCS, and the activity of the enzyme itself. Disulfide formation in SOD ...[more]