Structural highlights
Function
[SODM2_CAEEL] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Publication Abstract from PubMed
We have generated a site-directed mutant of the manganese superoxide dismutase SOD-3 of C.elegans (MnSOD-3) which modifies the metal specificity of the enzyme. While wild-type MnSOD-3 functions with manganese in the active site (3600 U.mg protein-1) it has little or no activity when iron is incorporated. However, when histidine replaces glutamine 142 in the active site, the enzyme retains 50% of its activity and becomes cambialistic for its metal cofactor exhibiting very similar specific activity with either manganese or iron.
A single mutation is sufficient to modify the metal selectivity and specificity of a eukaryotic manganese superoxide dismutase to encompass iron.,Hunter GJ, Hunter T, Trinh C, Bonetta R, Sacco A, Vella M, Sultana PM, Borowski T, Garcia-Fandino R, Stockner T, Fadia H Chemistry. 2017 Nov 26. doi: 10.1002/chem.201704655. PMID:29178484[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hunter GJ, Hunter T, Trinh C, Bonetta R, Sacco A, Vella M, Sultana PM, Borowski T, Garcia-Fandino R, Stockner T, Fadia H. A single mutation is sufficient to modify the metal selectivity and specificity of a eukaryotic manganese superoxide dismutase to encompass iron. Chemistry. 2017 Nov 26. doi: 10.1002/chem.201704655. PMID:29178484 doi:http://dx.doi.org/10.1002/chem.201704655
