{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hunter T"],"funding":["University of Malta","Biotechnology and Biological Sciences Research Council"],"pagination":["5303-5308"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5969255"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["24(20)"],"pubmed_abstract":["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<sup>-1</sup> of protein) 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."],"journal":["Chemistry (Weinheim an der Bergstrasse, Germany)"],"pubmed_title":["A Single Mutation is Sufficient to Modify the Metal Selectivity and Specificity of a Eukaryotic Manganese Superoxide Dismutase to Encompass Iron."],"pmcid":["PMC5969255"],"funding_grant_id":["PHBIN02-1","PHBRP03-17","PHBRP03-05","BB/L015056/1"],"pubmed_authors":["Hunter T","Trinh CH","Fadia HBR","Borowski T","Stockner T","Hunter GJ","Bonetta R","Vella M","Sultana PM","Garcia-Fandino R","Sacco A"],"additional_accession":[]},"is_claimable":false,"name":"A Single Mutation is Sufficient to Modify the Metal Selectivity and Specificity of a Eukaryotic Manganese Superoxide Dismutase to Encompass Iron.","description":"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<sup>-1</sup> of protein) 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.","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Apr","modification":"2026-05-03T02:14:30.405Z","creation":"2026-04-07T18:44:06.018Z"},"accession":"S-EPMC5969255","cross_references":{"pubmed":["29178484"],"doi":["10.1002/chem.201704655"]}}