Genomes and Genes
Gene Symbol: sodC
Description: superoxide dismutase, Cu, Zn, periplasmic
Alias: ECK1642, JW1638
Species: Escherichia coli str. K-12 substr. MG1655
- Benov L, Fridovich I. Escherichia coli expresses a copper- and zinc-containing superoxide dismutase. J Biol Chem. 1994;269:25310-4 pubmed..It will now be interesting to explore the phenotypic consequences imposed by the absence of this SOD. ..
- Battistoni A, Folcarelli S, Gabbianelli R, Capo C, Rotilio G. The Cu,Zn superoxide dismutase from Escherichia coli retains monomeric structure at high protein concentration. Evidence for altered subunit interaction in all the bacteriocupreins. Biochem J. 1996;320 ( Pt 3):713-6 pubmed..The substitution of hydrophobic residues with charged ones at positions located at the dimer interface of all known Cu,Zn superoxide dismutases could be specifically responsible for the monomeric structure of the E. coli enzyme. ..
- Korshunov S, Imlay J. Detection and quantification of superoxide formed within the periplasm of Escherichia coli. J Bacteriol. 2006;188:6326-34 pubmed..coli. This endogenous superoxide may create oxidative stress in that compartment and be a primary substrate of CuZnSOD. ..
- Sevcenco A, Krijger G, Pinkse M, Verhaert P, Hagen W, Hagedoorn P. Development of a generic approach to native metalloproteomics: application to the quantitative identification of soluble copper proteins in Escherichia coli. J Biol Inorg Chem. 2009;14:631-40 pubmed publisher..coli strengthens the view that the bacterial periplasm contains only a few periplasmic copper proteins, and that the cytosol is devoid of copper proteins. ..
- Pesce A, Capasso C, Battistoni A, Folcarelli S, Rotilio G, Desideri A, et al. Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography. J Mol Biol. 1997;274:408-20 pubmed..The molecular surface region involved in subunit dimerization in eukaryotic superoxide dismutases is structurally altered in E_SOD and displays a net polar nature. ..
- Puget K, Michelson A. Isolation of a new copper-containing superoxide dismutase bacteriocuprein. Biochem Biophys Res Commun. 1974;58:830-8 pubmed
- Imlay K, Imlay J. Cloning and analysis of sodC, encoding the copper-zinc superoxide dismutase of Escherichia coli. J Bacteriol. 1996;178:2564-71 pubmed..We have used the N-terminal protein sequence to isolate the gene encoding this enzyme. The gene, denoted sodC, is located at 37.1 min on the chromosome, adjacent to lhr and sodB...
- Lacour S, Landini P. SigmaS-dependent gene expression at the onset of stationary phase in Escherichia coli: function of sigmaS-dependent genes and identification of their promoter sequences. J Bacteriol. 2004;186:7186-95 pubmed..Only seven genes (dps, osmE, osmY, sodC, rpsV, wrbA, and yahO) had previously been recognized as rpoS dependent...
- Benov L, Fridovich I. Superoxide dismutase protects against aerobic heat shock in Escherichia coli. J Bacteriol. 1995;177:3344-6 pubmed..This effect is not seen at 53 degrees C, presumably because, at this higher temperature, direct thermolability of vital cell components overrides the effect of superoxide radicals. ..
- Benov L, Sage H, Fridovich I. The copper- and zinc-containing superoxide dismutase from Escherichia coli: molecular weight and stability. Arch Biochem Biophys. 1997;340:305-10 pubmed..A parallel was drawn between the E. coli Cu,ZnSOD and FALS varients of human Cu,ZnSOD, which are also relatively unstable and exhibit low affinity for Cu(II). ..
- Benov L, Beyer W, Stevens R, Fridovich I. Purification and characterization of the Cu,Zn SOD from Escherichia coli. Free Radic Biol Med. 1996;21:117-21 pubmed..0 Cu/subunit and the specific activity would have been 4800 U/mg. It now appears likely that gram negative bacteria will commonly be found to contain a periplasmic Cu,Zn SOD. ..