Table 3.
SOD1 redox-modified sites. Summary of SOD1 redox-modified sites described in this paper, including oxidation, glutathionylation, and cysteinylation.
| Species | Residue | Modification | Modifying Enzyme (if known); Potential Location of PTM | Significance | Reference |
|---|---|---|---|---|---|
| human | Trp32 | oxidation | increases aggregation of SOD1 | Zhang, 2003 | |
| human | Cys111 | oxidation | increases SOD1 propensity to misfold and inhibit kinesin-based fast axonal transport | Bosco, 2010 | |
| yeast | Cys146, His71, His120 | oxidation | speculated that oxidation leads to SOD1 misfolding and aggregation | Martins, 2014 | |
| human | Cys111 | glutathion-ylation | destabilizes SOD1 and promotes monomer formation which is the initiating step for SOD1 aggregation | Wilcox, 2009 | |
| human | Cys111 | cysteinylation | protects SOD1 from oxidation; slight conformational change at the dimer interface and electrostatic loop | Auclair, 2013a; Auclair, 2013b |