A metalloprotein; also known as erythrocuprein, hemocuprein or cytocuprein. Enzymes from most eukaryotes contain both copper and zinc; those from mitochondria and most prokaryotes contain manganese or iron.
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SYSTEMATIC NAME
IUBMB Comments
superoxide:superoxide oxidoreductase
A metalloprotein; also known as erythrocuprein, hemocuprein or cytocuprein. Enzymes from most eukaryotes contain both copper and zinc; those from mitochondria and most prokaryotes contain manganese or iron.
native and recombinant enzyme ossess a covalent modification of the conserved Tyr41 in the active site, Tyr41 plays an important role in the enzyme activity and the maintenance of the structural architecture of SOD, overview
native and recombinant enzyme ossess a covalent modification of the conserved Tyr41 in the active site, Tyr41 plays an important role in the enzyme activity and the maintenance of the structural architecture of SOD, overview
covalent modification of the conserved Tyr41 in the active site, Tyr41 and His155 are involved in catalysis, hydrogen bond network including three solvent molecules connecting the iron-ligating hydroxide ion via H155 with F41 and H37, Y41 and H155 are important for the structural and functional properties of SOD, overview
Fe-type SOD, helices alpha1 and alpha2 contribute one metal ligand each, i.e. His33 and His84, binding structure, the iron is ligated by Nepsilon2 of His33, His84 and His174, by Odelta1 of Asp170, and a solvent molecule forming a distorted trigonal bipyramidal coordination sphere, overview
irreversible inactivation by attachment of a molecule phenylmethanesulfonyl fluoride to the active site Tyr41 reinforcing the heat stability of the enzyme, overview
recombinant Fe-reconstituted SOD is not inhibited by azide, steric hindrance in the substrate funnel of the enzyme prevents the access of N3- but allows O2- and F- access to the active site
recombinant Fe-reconstituted SOD is not inhibited by azide, steric hindrance in the substrate funnel of the enzyme prevents the access of N3- but allows O2- and F- access to the active site
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified mutant enzyme Y41F, hanging drop vapor diffusion method, 21°C, 1:1 mix of the reservoir solution containing 8% PEG 8000, 0.1 M Tris-HCl, pH 8.5, and the protein solution containing 1.45 mg/mL Y41F, 20 mM Tris-HCl, pH 7.8, and 1% glycerol, X-ray diffraction structure determination and analysis
site-directed mutagenesis, the mutant shows a a slightly lower iron content, reduced heat stability, and a 2fold reduced activity compared to the wild-type enzyme
site-directed mutagenesis, the mutant shows a a slightly lower iron content and a 17fold reduced activity compared to the wild-type enzyme, the mutant shows an uninterrupted hydrogen bond network
construction of a fusion protein with the N-terminal domain of superoxide dismutase from Geobacillus thermodenitrificans NG80-2. The recombinant protein exhibits improved thermophilicity, higher working temperature, improved thermostability, broader pH stability, and enhanced tolerance to inhibitors and organic media without any alterations in its oligomerization state
construction of a fusion protein with the N-terminal domain of superoxide dismutase from Geobacillus thermodenitrificans NG80-2. The recombinant protein exhibits improved thermophilicity, higher working temperature, improved thermostability, broader pH stability, and enhanced tolerance to inhibitors and organic media without any alterations in its oligomerization state
5 h, 40% loss of activity for wild-type, 13% loss of activity for fusion protein with the N-terminal domain of superoxide dismutase from Geobacillus thermodenitrificans NG80-2
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
DNA binding protein-like protein, superoxide dismutase, and peroxiredoxin interact and likely form a supramolecular complex for mitigating oxidative damage
native enzyme from post-ribosomal supernatant by anion exchange, hydrophobic interaction, and hydroxyapatite chromatography, followed by gel filtration, to homogeneity
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of Fe-SOD from purified recombinant apo-enzyme, apo-enzyme preparation: purified recombinant enzyme is denatured in buffer containing 50 mM acetate buffer, pH 3.8, 6 M guanidine hydrochloride, and 10 mM EDTA for 16 h at 50°C, followed by dialysis against the same buffer containing MnSO4 instead of EDTA, and removal of guanidine hydrochloride in a second dialysis step, followed by gel filtration, overview
Cannio, R.; D'Angelo, A.; Rossi, M.; Bartolucci, S.
A superoxide dismutase from the archaeon Sulfolobus solfataricus is an extracellular enzyme and prevents the deactivation by superoxide of cell-bound proteins
Dello Russo, A.; Rullo, R.; Nitti, G.; Masullo, M.; Bocchini, V.
Iron superoxide dismutase from the archaeon Sulfolobus solfataricus: average hydrophobicity and amino acid weight are involved in the adaptation of proteins to extreme environments
De Vendittis, E.; Ursby, T.; Rullo, R.; Gogliettino, M.A.; Masullo, M.; Bocchini, V.
Phenylmethanesulfonyl fluoride inactivates an archaeal superoxide dismutase by chemical modification of a specific tyrosine residue. Cloning, sequencing and expression of the gene coding for Sulfolobus solfataricus superoxide dismutase