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2 superoxide + 2 H+ = O2 + H2O2
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
2 superoxide + 2 H+ = O2 + H2O2
three-dimensional structure
-
2 superoxide + 2 H+ = O2 + H2O2
Cu2+-binding
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
Megalodesulfovibrio gigas
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
2 superoxide + 2 H+ = O2 + H2O2
A metalloprotein. Enzymes from most eukaryotes contain both copper and zinc, those from mitochondria and most prokaryotes contain manganese or iron. ligand binding site and structure
-
2 superoxide + 2 H+ = O2 + H2O2
A metalloprotein. Enzymes from most eukaryotes contain both copper and zinc, those from mitochondria and most prokaryotes contain manganese or iron. ligand binding site and structure
-
2 superoxide + 2 H+ = O2 + H2O2
A metalloprotein. Enzymes from most eukaryotes contain both copper and zinc, those from mitochondria and most prokaryotes contain manganese or iron. ligand binding site and structure
2 superoxide + 2 H+ = O2 + H2O2
active site, manganese-binding site and contact site between monomers
-
2 superoxide + 2 H+ = O2 + H2O2
active site, manganese-binding site and contact site between monomers
-
2 superoxide + 2 H+ = O2 + H2O2
active site, manganese-binding site and contact site between monomers
-
2 superoxide + 2 H+ = O2 + H2O2
active site is not conserved, differing from others of Mn-SOD and Fe-SOD
-
2 superoxide + 2 H+ = O2 + H2O2
presence of a general acid and a general base in catalysis. Catalytic model requires histidine residues, metal-bound water molecules and two hydrated metal ions to operate in concert
-
2 superoxide + 2 H+ = O2 + H2O2
the amino acid residues His46, His48, His63, His71, His80, and His120, and Asp83 in the active site are conserved as in other Cu/ZnSODs
-
2 superoxide + 2 H+ = O2 + H2O2
electrostatic guidance of anionic substrate to the active site, detailed overview. Generation of a model for electrostatic-mediated diffusion, and efficient binding of superoxide for catalysis
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
A metalloprotein. Enzymes from most eukaryotes contain both copper and zinc, those from mitochondria and most prokaryotes contain manganese or iron. ligand binding site and structure
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
active site, manganese-binding site and contact site between monomers
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
-
2 superoxide + 2 H+ = O2 + H2O2
three-dimensional structure
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
-
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
active site, manganese-binding site and contact site between monomers
-
-
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
active site, manganese-binding site and contact site between monomers
-
-
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
Megalodesulfovibrio gigas Fe-SOD
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
A metalloprotein. Enzymes from most eukaryotes contain both copper and zinc, those from mitochondria and most prokaryotes contain manganese or iron. ligand binding site and structure
-
-
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
the amino acid residues His46, His48, His63, His71, His80, and His120, and Asp83 in the active site are conserved as in other Cu/ZnSODs
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
active site, manganese-binding site and contact site between monomers
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
Anas platyrhynchos domestica CuZn-SOD
-
-
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
mechanism
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
A metalloprotein. Enzymes from most eukaryotes contain both copper and zinc, those from mitochondria and most prokaryotes contain manganese or iron. ligand binding site and structure
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
-
-
-
-
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2 O2.- + 2 H+ +
O2 + H2O2
2 superoxide + 2 H+
O2 + H2O2
nitro blue tetrazolium + ?
?
Nitroblue Tetrazolium + ?
?
O2.- + 4-[3-(4-iodophenyl)-2-(4-nitrophenyl)-2H-5-tetrazolio]-1,3-benzene disulfonate
?
i.e. WST-1, activity assay detection method
-
-
?
additional information
?
-
2 O2.- + 2 H+
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
activity determination by the epinephrine assay: at alkaline pH, superoxide anion O2- causes the oxidation of epinephrine to adrenochrome, SOD competes with this reaction by decreasing the adrenochrome formation
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
-
ir
2 O2.- + 2 H+
O2 + H2O2
-
enzyme activity determination by xanthine-xanthine oxidase-nitro blue tetrazolium assay
-
-
ir
2 O2.- + 2 H+
O2 + H2O2
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
enzyme activity assay by measurement of inhibition of reduction of cytochrome c by O2- produced by the xanthine oxidase/xanthine reaction
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
superoxide dismutase is a key enzyme for the protection of aerobic organisms against toxic radicals produced during oxidative processes
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
dismutation of superoxide in a two-step reaction: 1. O2.- + Fe3+-SOD = O2 + Fe2+-SOD, 2. O2.- + Fe2+-SOD + 2 H+ = H2O2 + Fe3+-SOD
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
Thermochaetoides thermophila
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
-
-
-
-
?
2 O2.- + 2 H+ +
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+ +
O2 + H2O2
the SOD-catalyzed reaction proceeds through a redox cycle of metal ions, active site geometry, overview
-
-
?
2 O2.- + 2 H+ +
O2 + H2O2
-
-
-
-
?
2 O2.- + 2 H+ +
O2 + H2O2
-
-
-
?
2 O2.- + 2 H+ +
O2 + H2O2
-
-
-
-
?
2 O2.- + 2 H+ +
O2 + H2O2
-
-
-
-
?
2 O2.- + 2 H+ +
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
detoxification of superoxide
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
Photobacterium sepia
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
-
-
-
-
?
nitro blue tetrazolium + ?
?
-
-
-
-
?
nitro blue tetrazolium + ?
?
-
-
-
-
?
Nitroblue Tetrazolium + ?
?
-
enzyme inhibits superoxide-induced reduction of colorless Nitroblue Tetrazolium dye to its oxidized blue formazan form
-
-
?
Nitroblue Tetrazolium + ?
?
-
enzyme inhibits superoxide-induced reduction of colorless Nitroblue Tetrazolium dye to its oxidized blue formazan form
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
Anas platyrhynchos domestica CuZn-SOD
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
r
O2- + H+
O2 + H2O2
-
-
-
r
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
Mn-SOD, expression is strongly stimulated during stationary phase in cell culture, enzyme is atypical and plays an important role in cell protection against reactive oxygen in the cytosol in the stationary phase
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
defense against oxidants
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
defense against oxidants
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Mn-SOD is unaffected by H2O2
?
O2- + H+
O2 + H2O2
-
-
Mn-SOD is unaffected by H2O2
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Mn-SOD is unaffected by H2O2
?
O2- + H+
O2 + H2O2
-
-
Mn-SOD is unaffected by H2O2
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
r
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
r
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
Megalodesulfovibrio gigas
-
-
-
?
O2- + H+
O2 + H2O2
Megalodesulfovibrio gigas Fe-SOD
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
Radix lethospermi
-
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
defense against oxidants
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
defense against oxidants
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2- + H+
O2 + H2O2
-
-
-
?
O2- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
isozyme MnSOD1, the product of sodA-1 gene, is expressed at lower level compared to MnSOD2, overview
-
-
?
O2.- + H+
O2 + H2O2
isozyme MnSOD2, encoded by sodA-2, plays a more important role in antioxidative stress compared to MnSOD1, overview
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
isozyme MnSOD2, encoded by sodA-2, plays a more important role in antioxidative stress compared to MnSOD1, overview
-
-
?
O2.- + H+
O2 + H2O2
isozyme MnSOD1, the product of sodA-1 gene, is expressed at lower level compared to MnSOD2, overview
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
SOD is a regulatory enzyme involved in the degradation of superoxide anions in living organisms
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
the enzyme catalyzes the disproportionation of superoxide via its Cu ion redox cycle [Cu-(II)/Cu(I)], protecting the organism from oxidative stress, while the neighboring Zn ion plays a structural role
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
periplasmic Cu,ZnSOD protects the bacterium from exogenously generated O2.- and contributes to intracellular survival of the bacterium in macrophages
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
periplasmic Cu,ZnSOD protects the bacterium from exogenously generated O2.- and contributes to intracellular survival of the bacterium in macrophages
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
a metalloenzyme that eliminates superoxide radicals by dismutation into hydrogen peroxide and molecular oxygen
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
Deinococcus radiodurans Mn-SOD is most effective at high superoxide fluxes found under conditions of high radioactivity compared to te enzyme of Escherichia coli and Homo sapiens
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
a key enzyme for fighting oxidative stress
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
-
EC-SOD plays an important role in regulating inflammatory responses to pulmonary injury, EC-SOD binds directly to hyaluronic acid and may inhibit pulmonary inflammation in part by preventing superoxide-mediated fragmentation of hyaluronan to low molecular mass fragments, thereby preventing activation of polymorphic neutrophil chemotaxis by fragmented hyaluronic acid, overview
-
-
?
O2.- + H+
O2 + H2O2
-
the enzyme mutation E93A leads to a decrease in muscle cdk5 activity accompanied by a significant reduction in MyoD and cyclin D1 levels causing amyotrophic lateral sclerosis, a primarily a motor neuron disorder with early muscle denervation preceding motor neuron loss, the progressive deterioration of muscle function is potentiated by altered muscle biochemistry in these mice at a very young, presymptomatic age, overview
-
-
?
O2.- + H+
O2 + H2O2
the conserved, active-site residue Tyr34 mediates product inhibition
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
SOD is a regulatory enzyme involved in the degradation of superoxide anions in living organisms
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
EC-SOD plays an important role in regulating inflammatory responses to pulmonary injury, EC-SOD binds directly to hyaluronic acid via its matrix-binding domain and may inhibit pulmonary inflammation in part by preventing superoxide-mediated fragmentation of hyaluronan to low molecular mass fragments
-
-
?
O2.- + H+
O2 + H2O2
-
enzyme inhibition by tetrathiomolybdate leads to antiangiogenic and antitumour effects in mice
-
-
?
O2.- + H+
O2 + H2O2
-
rosuvastatin induces the enzyme in aortic extracts and restores the enzyme expression in mice with combined leptin and LDL-receptor deficiency, and in THP-1 macrophages and foam cells in vitro, thus, SOD1 is a potentially important mediator of the prevention of oxLDL accumulation within atherosclerotic plaques, overview
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
extracellular superoxide dismutase accelerates endothelial recovery and inhibits in-stent restenosis in stented atherosclerotic Watanabe heritable hyperlipidemic rabbit aorta. Extracellular superoxide dismutase, EC-SOD, is a major component of antioxidative defense in blood vessels, and exogenously delivered EC-SOD protects against balloon-induced neointima formation and constrictive remodeling and has powerful cardioprotective properties, overview
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
the enzyme is important in defense of cells against oxidative stress
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
Cu,ZnSOD is a urinary marker of hepatic necrosis, but not hepatic fibrosis, overview
-
-
?
O2.- + H+
O2 + H2O2
-
SOD1 induces Ca2+ in the cell and inhibits ERK phosphorylation in the P-ERK1/2 pathway by muscarinic receptor M1 modulation in rat pituitary GH3 cells, the effect is enhanced by oxotremorine and partially reverted by pyrenzepine, and independent from increased intracellular calcium concentration, overview
-
-
?
O2.- + H+
O2 + H2O2
-
the enzyme is involved in hypoxic pulmonary vasoconstriction, HPV, an important physiological mechanism, which is regulated by changes in the production of and interactions among reactive oxygen species, mechanism, overview, the superoxide dismutase mimetic tempol inhibits HPV, overview
-
-
?
O2.- + H+
O2 + H2O2
-
the enzyme prevents the inhibition of human CYP3A4, UGT1A6, and P-glycoprotein with halogenated xanthene food dyes, overview
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
the enzyme contributes to the virulence of many human-pathogenic fungi through its ability to neutralize toxic levels of reactive oxygen species generated by the host
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
?
O2.- + H+
O2 + H2O2
-
-
-
-
?
pyrogallol + ?
?
-
-
-
?
pyrogallol + ?
?
enzyme inhibits the autooxidation of pyrogallol
-
-
?
pyrogallol + ?
?
-
enzyme inhibits the autooxidation of pyrogallol
-
-
?
riboflavin + ?
?
-
-
-
-
?
riboflavin + ?
?
-
-
-
-
?
additional information
?
-
SOD activity is determined by a modified method of inhibition of cytochrome c reduction in a xanthine/xanthine oxidase system generating superoxide ions
-
-
?
additional information
?
-
-
SOD activity is determined by a modified method of inhibition of cytochrome c reduction in a xanthine/xanthine oxidase system generating superoxide ions
-
-
?
additional information
?
-
-
SOD enzyme activity is determined by measuring enzyme ability to inhibit the photochemical reduction of nitrobluetetrazolium
-
-
?
additional information
?
-
-
the enzyme is involved in activation and modulation of phospho-extracellular signal-regulated kinases proteins and in the control of several biological processes including cell proliferation
-
-
?
additional information
?
-
-
SOD activity measurement using the nitroblue tetrazolium
-
-
?
additional information
?
-
-
SOD activity measurement using the nitroblue tetrazolium
-
-
?
additional information
?
-
-
enzyme activity measurement by determination of inhibition through the enzyme of pyrogallol autoxidation to purpurogallin
-
-
?
additional information
?
-
-
enzyme can reduce ferrocyanide to ferricyanide at pH 5.0-8.7
-
-
?
additional information
?
-
-
addition of hexacyanoferrate results in reduction of Cu(II) to Cu(I)
-
-
?
additional information
?
-
-
SOD inhibits the autoxidation of pyrogallol
-
-
?
additional information
?
-
-
coupled assay method using inhibition of the autooxidation of pyrogallol
-
-
?
additional information
?
-
-
superoxide dismutase inhibits pyrogallol autoxidation in alkaline medium characterized by increases in oxygen consumption. The primary products of pyrogallol autoxidation are H2O2 by reduction of O2 and pyrogallol-orthoquinone by oxidation of pyrogallol. SOD is catalyzing a reaction that annuls the forward electron transfer step that produces superoxide and pyrogallol-semiquinone, both oxygen radicals. By dismutating these oxygen radicals, SOD can reverse autoxidation. Analysis of reaction parameters, overview
-
-
?
additional information
?
-
-
enzyme can reduce ferrocyanide to ferricyanide at pH 5.0-8.7
-
-
?
additional information
?
-
-
addition of hexacyanoferrate results in reduction of Cu(II) to Cu(I)
-
-
?
additional information
?
-
enzyme activity assay method using riboflavin and nitroblue tetrazolium (NBT) reduction
-
-
?
additional information
?
-
SOD activity is assayed based on its ability to compete with nitroblue-tetrazolium for superoxide anions generated by the xanthine-xanthine oxidase system, which in turn results in the inhibition of reduction of nitroblue-tetrazolium
-
-
?
additional information
?
-
-
SOD activity is assayed based on its ability to compete with nitroblue-tetrazolium for superoxide anions generated by the xanthine-xanthine oxidase system, which in turn results in the inhibition of reduction of nitroblue-tetrazolium
-
-
?
additional information
?
-
-
Cu,Zn-dependent enzyme protects photoheterotrophic cells from periplasmic superoxide generated by exposure to low O2 under illuminated conditions
-
-
?
additional information
?
-
SOD activity measurement by the ferricytochrome c method, using xanthine/xanthine oxidase as the source of superoxide radicals
-
-
?
additional information
?
-
-
the extracellular enzyme appears to bind lipopolysaccharides, recognition mechanisms can be provided by several actors which can interplay such as plasma LBP-binding protein (LBP), membrane bound or soluble forms of CD14 and integrins
-
-
?
additional information
?
-
-
enzyme Sod2 is a major component of the antioxidant defense system, and adaptation to elevated growth temperatures is also dependent on enzyme activity
-
-
?
additional information
?
-
the enzyme activity assay uses the p-nitro blue tetrazolium chloride (NBT) solution method
-
-
?
additional information
?
-
-
the enzyme activity assay uses the p-nitro blue tetrazolium chloride (NBT) solution method
-
-
?
additional information
?
-
-
equilibrium binding of Escherichia coli MnSOD to poly(U), poly(A), poly(C), poly(dU) and double-stranded (ds) DNA, overview. The polynucleotides bind to MnSOD in the following affinity hierarchy, poly(dU) N poly(U) N dsDNA N poly(A) N poly(C). The differences in the hierarchy are not large in magnitude as the poly(dU) bound with less than a 100fold higher affinity than poly(C). For each polynucleotide, Kobs decreases only slightly with increasing [K+], surprising for a relatively non-specific nucleic acid protein. There is either only one binding site shared by these polynucleotides or the larger site size occluded by poly(C) overlaps that of poly(U) and poly(A), but extends further on the protein
-
-
?
additional information
?
-
-
enzyme activity assay using nitroblue tetrazolium and riboflavin
-
-
?
additional information
?
-
-
determination of superoxide dismutase is performed using the method of inhibition of epinephrine auto-oxidation in alkaline medium and the measurement of the absorbance of the resulting product at 340 nm
-
-
?
additional information
?
-
-
EC-SOD protects the lung in both bleomycin- and asbestos-induced models of pulmonary fibrosis
-
-
?
additional information
?
-
-
pharmacokinetics of single and multiple doses of recombinant human superoxide dismutase covalently linked to lecithin in healthy Japanese and Caucasian volunteers are nonlinear with dose, showing a relatively long half-life of PC-SOD of over 24 hours, overview
-
-
?
additional information
?
-
-
pharmacokinetics, safety and tolerability of single rising doses up to 80 mg of recombinant human superoxide dismutase covalently linked to lecithin in healthy white volunteers, overview
-
-
?
additional information
?
-
enzyme activity detection by water-soluble tetrazolium (WST-1) assay. This assay is based on the detection of a water-soluble formazan dye that is formed upon reduction of water-soluble tetrazolium salt, WST-1, by the superoxide anion
-
-
?
additional information
?
-
-
enzyme activity detection by water-soluble tetrazolium (WST-1) assay. This assay is based on the detection of a water-soluble formazan dye that is formed upon reduction of water-soluble tetrazolium salt, WST-1, by the superoxide anion
-
-
?
additional information
?
-
the enzyme activity is detected by its ability to inhibit the autoxidation of epinephrine at pH 10.2
-
-
?
additional information
?
-
-
the enzyme activity is detected by its ability to inhibit the autoxidation of epinephrine at pH 10.2
-
-
?
additional information
?
-
SOD activity is one major defense line against oxidative stress for all of the aerobic organisms
-
-
?
additional information
?
-
-
SOD activity is one major defense line against oxidative stress for all of the aerobic organisms
-
-
?
additional information
?
-
SOD activity is one major defense line against oxidative stress for all of the aerobic organisms
-
-
?
additional information
?
-
-
SOD activity is one major defense line against oxidative stress for all of the aerobic organisms
-
-
?
additional information
?
-
the enzyme assay measures the enzyme's ability to inhibit the oxidation of hydroxylamine catalyzed by the xanthine-xanthine oxidase system
-
-
?
additional information
?
-
-
the enzyme assay measures the enzyme's ability to inhibit the oxidation of hydroxylamine catalyzed by the xanthine-xanthine oxidase system
-
-
?
additional information
?
-
enzyme activity of recombinant MgMnSOD1 is assayed by using 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-(2,4-disulfophenyl)-2H-tetrazolium, i.e. WST-1. The method shows high sensitivity due to the lower reaction rate of WST-1 and superoxide anion
-
-
?
additional information
?
-
enzyme activity of recombinant MgMnSOD1 is assayed by using 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-(2,4-disulfophenyl)-2H-tetrazolium, i.e. WST-1. The method shows high sensitivity due to the lower reaction rate of WST-1 and superoxide anion
-
-
?
additional information
?
-
-
inverse relationship between SOD1 expression and ox-LDL in plaque plays a role in oxidative stress contributes to post-ischaemic injury in the heart, increasing SOD1 protects against this increased oxidative stress
-
-
?
additional information
?
-
-
enzyme is involved in pathogenesis of the parasite by protecting it from oxidative killing
-
-
?
additional information
?
-
-
higher levels of oxidative stress may induce changes in photochemicla efficiency of photosystem II
-
-
?
additional information
?
-
enzyme PschSOD exhibits superoxide dismutase and peroxidase activities. The enzyme utilizes its own dismutation product, the H2O2 in presence of bicarbonate
-
-
?
additional information
?
-
-
enzyme PschSOD exhibits superoxide dismutase and peroxidase activities. The enzyme utilizes its own dismutation product, the H2O2 in presence of bicarbonate
-
-
?
additional information
?
-
-
the enzyme is required for virulence of the organism, e.g. in silkworm Bombyx mori, with iron-SOD being more important, overview
-
-
?
additional information
?
-
-
superoxide dismutase activity in Pseudomonas putida affects utilization of sugars and growth on root surfaces, role of SOD in root colonization and oxidative stress, overview
-
-
?
additional information
?
-
-
dismutation of superoxide anions is promoted by reduction of Cu2+ to Cu+
-
-
?
additional information
?
-
-
MnSOD may have a specific role in the steroidogenic function of the fasciulata/reticularis of the rat adrenal, but not on that of the glomerulosa
-
-
?
additional information
?
-
-
dismutation of superoxide anions is promoted by reduction of Cu2+ to Cu+
-
-
?
additional information
?
-
enzyme activity measurement by reduction of NBT
-
-
?
additional information
?
-
-
enzyme activity measurement by reduction of NBT
-
-
?
additional information
?
-
enzyme activity measurement by reduction of NBT
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
unusual covalent modification of the conserved Tyr41 in the active site, interactions Tyr41-His155, overview
-
-
?
additional information
?
-
-
SOD activity is measured using a method employing xanthine and xanthine oxidase to generate superoxide radicals which react with 2-(4-iodophenyl)-3-(4-nitrophenol)-5-phenyltetrazolium chloride (INT) to form a red formazan dye. The SOD activity is then measured spectrophotometrically by the degree of inhibition of this reaction by means of the decrease in absorbance at 505 nm, 37°C
-
-
?
additional information
?
-
-
enzyme activity is measured byy the enzyme caused inhibition of the xanthine oxidase coupling reaction
-
-
?
additional information
?
-
-
enzyme activity determination with riboflavin and nitroblue tetrazolium (NBT), kinetics
-
-
?
additional information
?
-
-
Fe2+-containing active site structure, overview
-
-
?
additional information
?
-
-
Fe2+-containing active site structure, overview
-
-
?
additional information
?
-
-
SOD enzyme activity measurement is based on the inhibition of nitroblue tetrazolium reduction by superoxide radical generated by xanthine/xanthine oxidase
-
-
?
additional information
?
-
-
superoxide dismutase activity is measured by the inhibition of nitro blue tetrazolium reduction in the presence of the superoxide anion generated by the xanthine and xanthine oxidase system
-
-
?
additional information
?
-
-
enzyme activity determination by NBT reduction
-
-
?
additional information
?
-
-
the enzyme activity is determined by measuring by inhibition of autooxidation of pyrogallol
-
-
?
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Al3+
-
activates by 10% at 10 mM
Fe3+
activates the enzyme at 1 mM
Ca2+
-
study on affinity for enzyme-DNA complex and binding parameters. Enzyme-DNA complex shows at least two binding sites for divalent metal ions
Ca2+
-
activates the enzyme
Ca2+
-
activates slightly by 10% at 5 mM
Co2+
-
Co(II) can substitute for zinc in erythrocytes
Co2+
-
the Co ion can stably substitute the native cofactor Mn ion
Co2+
-
Co2+ binds at zinc site
Co2+
-
27% stimulation of activity
copper
-
-
copper
-
peculiar axial geometry of copper active sitewith low accessibility to external chelating agents
copper
0.68 mol per mol of subunit
copper
recombinant enzyme, 0.9 mol per mol of subunit, native enzyme, 0.86 mol per mol of subunit
copper
-
coexpression with yeast copper chaperone, copper supplement of medium, about 1 atom per subunit
copper
-
wild-type, 0.98 atoms per subunit, mutant H43R, 1.42, mutant A4V, 1.06 atoms per subunit
copper
-
2 CuZn-type constitutively expressed enzymes plus one induced by exposure of animals to copper
copper
-
1 atom per subunit
copper
Radix lethospermi
-
-
Cu
extracellular CuZnSOD
Cu
-
a Cu-Zn SOD, activates
Cu
-
a Cu/Zn superoxide dismutase
Cu
-
a Cu,Zn superoxide dismutase
Cu2+
a Cu/ZnSOD, highly conserved amino acid residues are involved in Cu/Zn binding
Cu2+
7 isozymes of CuZnSOD
Cu2+
a CuZn-superoxide dismutase
Cu2+
-
2 mol of Cu per mol of enzyme
Cu2+
-
heart: 1.64 mol of Cu per mol of enzyme, erythrocyte: 1.84 mol of Cu per mol of enzyme
Cu2+
-
the concentration of enzyme bound Cu2+ is 1.63 mg/l, the enzyme catalyzes the disproportionation of superoxide via its Cu ion redox cycle [Cu-(II)/Cu(I)], replacement of natural cofactor Cu2+ by isotopically enriched 65Cu, method, overview
Cu2+
-
1.1 mol per mol of Cu,Zn-SOD
Cu2+
a CuZnSOD, Cherax quadricarinatus ecCuZnSOD contains a Cu signature from 59 to 69 (GFHVHEKGDLG), and four Cu binding sites (His 61,63, 78, and 137)
Cu2+
-
1 gatom per mol of enzyme
Cu2+
a CuZn-superoxide dismutase
Cu2+
-
an intracellular Cu-Zn superoxide dismutase. The enzyme amino acid sequence contains several highly conserved motifs including Cu/Zn ions binding sites, i.e. His46, His48, His63, and His120 for Cu2+ binding
Cu2+
-
2 mol of Cu per mol of enzyme
Cu2+
-
1 gatom per mol of enzyme
Cu2+
-
a CuZn-superoxide dismutase
Cu2+
-
a Cu,Zn-superoxide dismutase
Cu2+
-
2 mol of Cu per mol of enzyme
Cu2+
-
1.7 mol per mol of enzyme
Cu2+
-
extracellular EC-SOD with Cu,Zn-SOD activity
Cu2+
-
Cu,Zn-SOD mutant H63C
Cu2+
a Cu,ZnSOD with 1.07 Cu2+ per enzyme subunit, binding structure, position of Cu2+ in the Zn2+-deficient enzyme A chain active site, overview, physiologic function in Cu,Zn-SOD, overview
Cu2+
a CuZn-superoxide dismutase
Cu2+
required, enzyme-bound
Cu2+
a Cu/Zn-SOD, the enzyme contains 1.54 mg/l copper atoms, and 0.239 mol Cu2+ per mol of enzyme
Cu2+
isozyme Cu/Zn-SOD, the highly conserved histidine residues H47, H49, H64, H72, H81, and H121 are involved in the interaction with the metallic cofactors, which are essential for activity and folding in all the Sod1 enzymes, D84 is also involve in Cu2+ binding
Cu2+
-
2 mol of Cu per mol of enzyme
Cu2+
a Cu,Zn-superoxide dismutase
Cu2+
a Cu,Zn-superoxide dismutase
Cu2+
a Cu,Zn-superoxide dismutase, residues H46, H48, H63, and H119 are involved in Cu2+ binding
Cu2+
-
mitochondrial cyanide-sensitive enzyme
Cu2+
-
2 mol of Cu per mol of enzyme
Cu2+
a Cu/ZnSOD, the enzyme sequence harbors two Cu/ZnSOD signatures and seven metal liganding residues
Cu2+
a Cu/Zn-superoxide dismutase
Cu2+
-
a Cu/Zn-SOD, conserved amino acids required for binding copper and zinc
Cu2+
-
2 mol of Cu per mol of enzyme
Cu2+
a CuZn-superoxide dismutase, the prosthetic copper and zinc are essential component of CuZn-SODs, 1.80-1.84 Cu2+ per enzyme dimer
Cu2+
-
a Cu/Zn-SOD. The isolated enzyme has 30% of its copper in the reduced state
Cu2+
-
a CuZn-superoxide dismutase
Cu2+
activates the enzyme at 1 mM
Cu2+
-
2 mol of Cu per mol of enzyme
Cu2+
-
1.63-1.78 mol per mol of isoenzyme I
Cu2+
-
1.86-1.97 mol per mol of isoenzyme II
Cu2+
a CuZn-superoxide dismutase
Cu2+
-
activates slightly at 0.5-1.0 mM
Cu2+
-
a CuZn-superoxide dismutase
Cu2+
the residues His47, His49, His64, His72, His81, and Asp121 are involved in metal binding
Cu2+
Thermochaetoides thermophila
a CuZn-superoxide dismutase
Cu2+
-
activates by 16% at 10 mM
Cu2+
a Cu/Zn SOD, 0.83 ng atom Cu per mg protein
Cu2+
-
SOD-1, SOD-2 and SOD-4
Fe
-
cognate metal ions Mn, Fe, and Co can effectively occupy the metal site of superoxide dismutase, respectively. MnSOD exhibits the highest SOD activity of 8600 U/mg, while Fe-sub-MnSOD shows only 800 U/mg, and Co-sub-MnSOD does not have any detectable activity. Thermodynamic stability decreases in the order Co-sub-MnSOD, MnSOD, Fe-sub-MnSOD
Fe
-
the recombinant SOD binds either Fe or Mn as a metal co-factor, with a consistent preference for Fe accommodation. But differently from the significant preference for Fe displays by the enzyme in the binding reaction, its Mn-form is 71fold more active compared to the Fe-form
Fe2+
a Fe-SOD, the enzyme is able to bind various bivalent metals in the active site
Fe2+
presence of 0.25 Fe atom and 0.01 Mn atom per monomer of protein
Fe2+
the SOD is active with Fe2+ and Mn2+, Fe2+ activates 6fold, binding structure, overview
Fe2+
the enzyme contains both Mn and Fe. It is cambialistic, i.e. active with either Fe2+ or Mn2+. The specific activities were 906 U/mg with Mn2+ and 175 U/mg with Fe2+
Fe2+
the enzyme is active with either Fe(II) or Mn(II) as a cofactor. The recombinant enzyme is produced in Escherichia coli expressed as an apoprotein. This apoprotein shows no SOD activity. The recombinant is activated with Fe(NH4)2(SO4)2 and MnSO4 salts at elevated temperature. The Fe-reconstituted enzyme contains 0.79 atom of iron per subunit
Fe2+
-
the Fe ion can stably substitute the native cofactor Mn ion
Fe2+
all isozymes in the organism are FeSODs
Fe2+
-
Fe-SOD contains 1 Fe2+ per subunit
Fe2+
Fe-SOD, 0.41 atom of Fe per SOD subunit
Fe2+
-
a Fe,Mn-SOD, the purified enzyme contains 1.1 g-atom of Fe per mol enzyme
Fe2+
a cambialistic Fe/Mn-superoxide dismutase, 0.56 g-atom per mol of enzyme
Fe2+
-
the enzyme is an iron SOD with 0.9 Fe/subunit
Fe2+
-
a Fe-SOD, the dimeric enzyme contains one iron atom/subunit
Fe2+
the purified apoprotein can be reconstituted with either Mn2+ or Fe2+ by heating the protein with the appropriate metal salt at 95°C. Both Mn- and Fe-reconstituted enzyme exhibits superoxide dismutase activity, with the Mn-containing enzyme having the higher activity
Fe2+
native enzyme from aerobically-grown cells grown in standard medium contains 0.55 mol Fe2+ per mol of subunit. Native enzyme from aerobically-grown cells grown in medium supplemented with manganese contains less than 0.01 mol Fe2+ per mol of subunit. Native enzyme from aerobically-grown cells grown in medium supplemented with iron contains 0.01 mol Fe2+ per mol of subunit. Native enzyme from anaerobically-grown cells grown in standard medium contains 0.43 mol Fe2+ per mol of subunit. Recombinant apo-enzyme contains less than 0.01 mol Fe2+ per mol of subunit. Mn2+-reconstituted recombinant enzyme contains less than 0.01 mol Fe2+ per mol of subunit. Fe2+-reconstituted recombinant enzyme contains 0.76 mol Mn2+ per mol of subunit. The recombinant protein has little activity due to the lack of metal incorporation. Reconstitution of the enzyme by heat treatment with either Mn2+ or Fe2+ yields a highly active protein
Fe2+
-
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
Fe2+
-
the homodimeric enzyme contains 0.7 atom of iron per subunit
Fe2+
-
a Fe-SOD, all iron-binding sites (His 27, His 80, Asp 164 and His 168) of SaFe-SOD are conserved
Fe2+
-
activates the enzyme
Fe2+
-
activates slightly by 10% at 5 mM
Fe2+
-
bound by His33, His84, His174, and Asp170, coordination in the active site, overview
Fe2+
Fe/Mn-type SOD, the Fe-type enzyme contains Gln85
Fe2+
a cambialistic Mn/Fe-SOD
Fe2+
recombinant mutant H29A and H171A specificity
Iron
the enzyme is a tetramer with 4 iron centers, one iron per monomer
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
-
1.8-1.9 mol (gatoms) per mol of enzyme
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
-
1.6 mol per mol of enzyme
Iron
0.4 mol per mol of mn-SOD
Iron
30% of the activity with manganese
Iron
0.5-1.0 atom Fe2+ per subunit
Iron
0.3 atoms of iron/manganese in ratio 2:1 per subunit
Iron
-
2.7-2.8 mol per mol of enzyme
Iron
-
1.8-1.9 mol (gatoms) per mol of enzyme
Iron
-
1.8-1.9 mol (gatoms) per mol of enzyme
Iron
-
each Fe3+ ion has 2 coordination positions available for interaction with solute molecules but only 1 is necessary for catalysis
Iron
-
1.8-1.9 mol (gatoms) per mol of enzyme
Iron
spectroscopic analysis of reduced and oxidized state of iron. In oxidized state, formation of a six-coordinate complex occurs. Two substrate analogues F- can bind to the oxidized enzymes active site
Iron
-
1.8-1.9 mol (gatoms) per mol of enzyme
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
-
0.9 mol per mol of enzyme
Iron
-
1.8-1.9 mol (gatoms) per mol of enzyme
Iron
-
contains 0.95 atoms of Fe per monomer
Iron
-
2.7-2.8 mol per mol of enzyme
Iron
-
2.0 mol per mol of enzyme
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
Megalodesulfovibrio gigas
-
-
Iron
-
1.1 mol per mol of subunit
Iron
contains 1 mol iron per mol of enzyme, but no manganese
Iron
-
1.8-1.9 mol (gatoms) per mol of enzyme
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
-
1.8-1.9 mol (gatoms) per mol of enzyme
Iron
-
2.0 mol per mol of enzyme
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
-
1 atom per subunit
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
-
1.8-1.9 mol (gatoms) per mol of enzyme
Iron
-
accepts iron and/or manganese as cofactor
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
0.75 atoms per subunit
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
-
iron-superoxide dismutase, FeSOD, encoded by gene sodB
Iron
-
when mitochondrial iron homeostasis is disrupted, iron accumulates in a reactive form and competes with manganese, inactivating the enzyme. The ability to control the iron pool within mitochondria is critical to maintaining enzyme activity
Iron
-
0.24 mol Fe2+ per mol of subunit
Iron
-
1.0-1.45 mol per mol of enzyme
Iron
contains one iron atom per dimer, the protein contains a mononuclear iron center
Iron
-
1.8-1.9 mol (gatoms) per mol of enzyme
Iron
-
2.0 mol per mol of enzyme
Iron
Thermosynechococcus vestitus
-
no change in the geometry of the FeII site occurs over a wide pH range
Iron
-
2.7-2.8 mol per mol of enzyme
Iron
-
2.7-2.8 mol per mol of enzyme
Iron
-
0.35 mol per mol of subunit, required both for activity and stability of enzyme tetramer
Manganese
most effcient metal ion
Manganese
0.3 atoms of iron/manganese in ratio 2:1 per subunit
Manganese
-
when the Deinococcus radiodurans Mn2+SOD reacts with a substoichiometric amount of superoxide, Deinococcus radiodurans Mn3+SOD is produced
Manganese
analysis of manganese(II) high-field electron paramagnetic resonance spectrum. In the -248°C to -73°C range, the zero-field interaction steadily decreases with increasing temperature. Above -33°C, a distinct six-line component is detected derived from a hexacoordinate Mn(II) center resulting from coordination of normally five-coordinate Mn(II) by a water molecule. comparison with Mn(II) centers in concanavalin A and R. spheroides photosynthetic center
Manganese
-
kinetic study on metal binding mechanism. Apo-enzyme metallation kinetics are gated, zero order in metal ion for both native Mn2+ and nonnative Co2+. Cobalt-binding reveals two exponential kinetic processes. Sensitivity of metallated protein to exogenously added chelator decreases with time, consistent with annealing of an initially formed metalloprotein complex
Manganese
-
less than 0.1 mol per mol of subunit
Manganese
-
manganese-superoxide dismutase, MnSOD, encoded by gene sodA
Manganese
-
mitochondrial localization is essential for insertion of manganese to protein. Insertion is only possible with a newly synthesized polypeptide and seems to be driven by the protein unfolding process associated with mitochondrial import
Manganese
putatively coordinated by H27, H81, D167, H171
Mg2+
-
study on affinity for enzyme-DNA complex and binding parameters. Enzyme-DNA complex shows at least two binding sites for divalent metal ions
Mg2+
-
up to 48% activation
Mg2+
-
73% stimulation of activity
Mn
manganese superoxide dismutase
Mn
-
cognate metal ions Mn, Fe, and Co can effectively occupy the metal site of superoxide dismutase, respectively. MnSOD exhibits the highest SOD activity of 8600 U/mg, while Fe-sub-MnSOD shows only 800 U/mg, and Co-sub-MnSOD does not have any detectable activity. Thermodynamic stability decreases in the order Co-sub-MnSOD, MnSOD, Fe-sub-MnSOD
Mn
manganese superoxide dismutase
Mn
cytosolic MnSOD isozymes, Mn binding sequence is DVWHHAYY
Mn
mitochondrial MnSOD isozymes, Mn binding sequence is DVWHHAYY
Mn
manganese superoxide dismutase
Mn
-
the recombinant SOD binds either Fe or Mn as a metal co-factor, with a consistent preference for Fe accommodation. But differently from the significant preference for Fe displays by the enzyme in the binding reaction, its Mn-form is 71fold more active compared to the Fe-form
Mn
a manganese superoxide dismutase, contains 0.00246 mg Mn/mg protein, binding involves conserved residues H88, H136, D222, and H226
Mn2+
-
0.5 mol per mol of subunit
Mn2+
presence of 0.25 Fe atom and 0.01 Mn atom per monomer of protein
Mn2+
the SOD is active with Fe2+ and Mn2+, Mn2+ activates 20fold, binding structure, overview
Mn2+
the enzyme contains both Mn and Fe. It is cambialistic, i.e. active with either Fe2+ or Mn2+. The specific activities were 906 U/mg with Mn2+ and 175 U/mg with Fe2+
Mn2+
the enzyme is active with either Fe(II) or Mn(II) as a cofactor. The recombinant enzyme is produced in Escherichia coli expressed as an apoprotein. This apoprotein shows no SOD activity. The recombinant is activated with Fe(NH4)2(SO4)2 and MnSO4 salts at elevated temperature. The Mn-reconstituted enzyme contains 0.82 atom of manganese per subunit
Mn2+
isozyme MnSOD2, encoded by gene sodA-2
Mn2+
Mn-SOD isozyme MnSOD1, encoded by gene sodA-1, MnSOD1 is expressed at lower level compared to MnSOD2
Mn2+
a Mn-superoxide dismutase, conserved manganese-binding site residues are H28, H83, D165, and H169
Mn2+
-
1.1 mol per mol of enzyme
Mn2+
-
0.05 mol per mol of enzyme
Mn2+
-
contains no manganese
Mn2+
-
study on affinity for enzyme-DNA complex and binding parameters. Enzyme-DNA complex shows at least two binding sites for divalent metal ions
Mn2+
0.9 Mn per mol of enzyme
Mn2+
-
0.89 mol per mol of liver Mn-SOD
Mn2+
-
1 atom per subunit
Mn2+
a MnSOD, Cherax quadricarinatus mtMnSOD contains a manganese superoxide dismutase domain (DVWEHAYY) from 180-187, and four conserved amino acids responsible for binding manganese (His48, His96, Asp180, and His184)
Mn2+
-
contains no manganese
Mn2+
-
the enzyme selectively chooses the Mn ion as its native cofactor, although Co and Fe ions can stably substitute the Mn ion
Mn2+
-
1.3 gatoms per mol of enzyme
Mn2+
-
1.3 gatoms per mol of enzyme
Mn2+
-
1.2-1.8 mol per mol of Mn-SOD
Mn2+
-
MnSOD, the Mn ion is the only metal cofactor, 0.57 atom per polypeptide chain
Mn2+
-
1.3 gatoms per mol of enzyme
Mn2+
a Mn-SOD, Mn2+ activates, the manganese-binding site is formed by conserved residues His260, His308, Asp392, and His396
Mn2+
a Mn-SOD, Mn2+ activate the enzyme at 1 mM, the manganese-binding sites are conserved in the sequence involving residues His260, His308, Asp392, and His396
Mn2+
-
0.22 mol per mol of enzyme
Mn2+
-
2.2 mol per mol of enzyme
Mn2+
-
1.5 mol per mol of enzyme
Mn2+
-
1.3 gatoms per mol of enzyme
Mn2+
a MnSOD, activates, binding sequence is DVWEHAYY
Mn2+
-
1 atom per subunit
Mn2+
-
less than 0.2 mol per mol of enzyme
Mn2+
-
a Fe,Mn-SOD, the purified enzyme contains 0.7 g-atom of Mn per mol enzyme
Mn2+
-
1.3 gatoms per mol of enzyme
Mn2+
a cambialistic Fe/Mn-superoxide dismutase, 1.12 g-atom per mol of enzyme
Mn2+
-
1.7 mol per mol of enzyme
Mn2+
-
1.3 gatoms per mol of enzyme
Mn2+
-
0.5 mol per mol of subunit
Mn2+
-
1.22 mol per mol of enzyme
Mn2+
a manganese-containing superoxide dismutase
Mn2+
-
1.3 gatoms per mol of enzyme
Mn2+
-
a Mn-SOD, Mn2+ constitutes 0.13% of the enzyme, equivalent to one manganese atom per molecule of enzyme
Mn2+
-
accepts iron and/or manganese as cofactor
Mn2+
-
manganese-SOD variant
Mn2+
-
1.1 mol per mol of enzyme
Mn2+
the purified apoprotein can be reconstituted with either Mn2+ or Fe2+ by heating the protein with the appropriate metal salt at 95°C. Both Mn- and Fe-reconstituted enzyme exhibits superoxide dismutase activity, with the Mn-containing enzyme having the higher activity
Mn2+
native enzyme from aerobically-grown cells grown in standard medium contains 0.55 mol Mn2+ per mol of subunit. Native enzyme from aerobically-grown cells grown in medium supplemented with manganese contains 0.86 mol Mn2+ per mol of subunit. Native enzyme from aerobically-grown cells grown in medium supplemented with iron contains 0.68 mol Mn2+ per mol of subunit. Native enzyme from anaerobically-grown cells grown in standard medium contains 0.08 mol Mn2+ per mol of subunit. Recombinant apoenzyme contains less than 0.01 mol Mn2+ per m,ol of subunit. Mn2+-reconstituted recombinant enzyme contains 0.86 mol Mn2+ per mol of subunit. Fe2+-reconstituted recombinant enzyme contains less than 0.01 mol Mn2+ per mol of subunit.The recombinant protein has little activity due to the lack of metal incorporation. Reconstitution of the enzyme by heat treatment with either Mn2+ or Fe2+ yields a highly active protein
Mn2+
-
1.2-1.8 mol per mol of Mn-SOD
Mn2+
-
3.69 mol per mol of enzyme
Mn2+
activates the enzyme at 1 mM
Mn2+
-
1 atom per subunit
Mn2+
-
4 mol per mol of enzyme
Mn2+
-
0.75 mol per mol of subunit
Mn2+
-
accepts iron and/or manganese as cofactor
Mn2+
-
isoform I, 1.85 atoms manganese per mol of enzyme
Mn2+
Fe/Mn-type SOD, the Mn-type enzyme contains Gly85
Mn2+
-
1.3 gatoms per mol of enzyme
Mn2+
Thermochaetoides thermophila
-
0.00205 mg/mg of protein
Mn2+
Thermochaetoides thermophila
manganese superoxide dismutase
Mn2+
-
2 atoms of manganese per molecule
Mn2+
a cambialistic Mn/Fe-SOD
Mn2+
-
2 atoms of manganese per molecule
Mn2+
-
activates by 12% at 10 mM, Mn-containing superoxide dismutase
Mn2+
a Mn-SOD, wild-type specificity, and mutant H84A
Mn2+
-
isozyme SODI is a Mn-SOD
Mn2+
-
1.22 mol per mol of enzyme
Zinc
-
-
Zinc
1.02 mol per mol of subunit
Zinc
recombinant enzyme, 0.51 mol per mol of subunit, native enzyme, 1.01 mol per mol of subunit
Zinc
-
wild-type, 1.08 atoms per subunit, mutant H43R, 1.11, mutant A4V, 1.43 atoms per subunit
Zinc
-
2 CuZn-type constitutively expressed enzymes plus one induced by exposure of animals to copper
Zinc
-
0.5 atoms per subunit
Zinc
Radix lethospermi
-
-
Zn
extracellular CuZnSOD
Zn
-
in solution, 1 mol per mol of protein. In crystal, a second Zn is bound at the interface between the two enzyme molecules leading to the formation of covalently bound enzyme dimers
Zn
-
a Cu/Zn superoxide dismutase
Zn
-
a Cu,Zn superoxide dismutase
Zn2+
a Cu/ZnSOD, highly conserved amino acid residues are involved in Cu/Zn binding
Zn2+
-
0.2 mol of Cu per mol of enzyme
Zn2+
-
0.6-0.7 mol per mol of enzyme
Zn2+
7 isozymes of CuZnSOD
Zn2+
a CuZn-superoxide dismutase
Zn2+
-
2 mol of Zn2+ per mol of enzyme
Zn2+
-
1.8 mol of Zn per mol of enzyme
Zn2+
-
the concentration of enzyme bound Zn2+ is 1.68 mg/l, the Zn ion plays a structural role, replacement of natural cofactor Zn2+ by isotopically enriched 68Zn, method, overview
Zn2+
-
1.3 mol per mol of Cu,Zn-SOD
Zn2+
a CuZnSOD, Cherax quadricarinatus ecCuZnSOD contains a Zn signature from 155 to 166 (GNAGQRSGCGII) and four Zn binding sites (His 78, 86, and 95, and Asp 98)
Zn2+
-
1.0 gatom per mol of enzyme
Zn2+
a CuZn-superoxide dismutase
Zn2+
-
an intracellular Cu-Zn superoxide dismutase. The enzyme amino acid sequence contains several highly conserved motifs including Cu/Zn ions binding sites, i.e. His63, His71, His80, and Asp83 for Zn2+ binding
Zn2+
-
2 mol of Zn2+ per mol of enzyme
Zn2+
-
0.85 mol per mol of enzyme
Zn2+
-
a CuZn-superoxide dismutase
Zn2+
-
a Cu,Zn-superoxide dismutase
Zn2+
-
2.2 mol per mol of enzyme
Zn2+
-
2 mol of Zn2+ per mol of enzyme
Zn2+
-
1.5 mol per mol of enzyme
Zn2+
-
0.5 mol per mol of enzyme
Zn2+
-
1.6 mol per mol of enzyme
Zn2+
-
extracellular EC-SOD with Cu,Zn-SOD activity
Zn2+
a Cu,ZnSOD with 1.18 Zn2+ per enzyme subunit, binding structure, overview
Zn2+
a CuZn-superoxide dismutase
Zn2+
a Cu/Zn-SOD, the enzyme contains 1.71 mg/l zinc atoms, 0.258 mol Zn2+ per mol of enzyme
Zn2+
isozyme Cu/Zn-SOD, the highly conserved histidine residues H47, H49, H64, H72, H81, and H121 are involved in the interaction with the metallic cofactors, which are essential for activity and folding in all the Sod1 enzymes
Zn2+
-
2 mol of Zn2+ per mol of enzyme
Zn2+
-
0.2 mol of Cu per mol of enzyme
Zn2+
a Cu,Zn-superoxide dismutase
Zn2+
a Cu,Zn-superoxide dismutase
Zn2+
a Cu,Zn-superoxide dismutase, residues H63, H71, H80, and D83 are involved in Zn2+ binding
Zn2+
-
1.8 mol of Zn per mol of enzyme
Zn2+
-
0.6-0.7 mol per mol of enzyme
Zn2+
-
mitochondrial cyanide-sensitive enzyme
Zn2+
-
2 mol of Zn2+ per mol of enzyme
Zn2+
-
1.2 mol per mol of enzyme
Zn2+
a Cu/ZnSOD, the enzyme sequence harbors two Cu/ZnSOD signatures and seven metal liganding residues
Zn2+
a Cu/Zn-superoxide dismutase
Zn2+
-
a Cu/Zn-SOD, conserved amino acids required for binding copper and zinc
Zn2+
-
2 mol of Zn2+ per mol of enzyme
Zn2+
a CuZn-superoxide dismutase, the prosthetic copper and zinc are essential component of CuZn-SODs, 1.6 Zn2+ per enzyme dimer
Zn2+
-
a CuZn-superoxide dismutase
Zn2+
activates the enzyme at 1 mM
Zn2+
-
2 mol of Zn2+ per mol of enzyme
Zn2+
-
1.8 mol of Zn per mol of enzyme
Zn2+
-
1.34-1.81 mol per mol of isoenzyme I
Zn2+
-
1.9-20.0 mol per mol of isoenzyme II
Zn2+
-
2 mol of Zn2+ per mol of enzyme
Zn2+
a CuZn-superoxide dismutase
Zn2+
-
activates slightly at 0.5-1.0 mM
Zn2+
-
a CuZn-superoxide dismutase
Zn2+
the residues His47, His49, His64, His72, His81, and Asp121 are involved in metal binding
Zn2+
Thermochaetoides thermophila
a CuZn-superoxide dismutase
Zn2+
-
1.0 gatom per mol of enzyme
Zn2+
-
activates by 48% at 10 mM
Zn2+
a Cu/Zn SOD, 0.41 ng atom Zn per mg protein
Zn2+
-
SOD-1, SOD-2 and SOD-4
additional information
-
the native forms of SODAp and NTD-fused N-terminal domain ntdSODAp prefer binding Fe2+ over Mn2+ (about 10fold) but contain low ion amounts in each monomer, respectively
additional information
enzyme affinities for copper, zinc, and nickel, overview
additional information
-
enzyme affinities for copper, zinc, and nickel, overview
additional information
-
presence of Cu and Zn is confirmed by inductively coupled plasma mass spectrometry, metal content analysis reveals a 1/1 molar ratio (metal/protein) for Cu and Zn, without significant amounts of Fe, Mn or Ni
additional information
presence of Cu and Zn is confirmed by inductively coupled plasma mass spectrometry, metal content analysis reveals a 1/1 molar ratio (metal/protein) for Cu and Zn, without significant amounts of Fe, Mn or Ni
additional information
-
presence of Cu and Zn is confirmed by inductively coupled plasma mass spectrometry, metal content analysis reveals for SODI molar ratios (metal/protein) for Cu = 0.7 and Zn = 0.4, and for Mn = 0.16
additional information
presence of Cu and Zn is confirmed by inductively coupled plasma mass spectrometry, metal content analysis reveals for SODI molar ratios (metal/protein) for Cu = 0.7 and Zn = 0.4, and for Mn = 0.16
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
-
overview: metal content
additional information
-
the enzyme contains 7 metal binding sites
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
-
relevance of the zinc imidazolate bond to the redox properties
additional information
-
overview: metal content
additional information
-
role of copper and zinc in protein conformation and activity
additional information
-
Cu2+ and Zn2+ binding sites are very close to each other
additional information
-
Cu2+-binding site
additional information
-
quantitative determination of an isotopically enriched metalloenzyme containing two different metal isotopes, method development, overview
additional information
Mn-SOD contains as well Fe3+, but is only active with manganese
additional information
-
Mn-SOD contains as well Fe3+, but is only active with manganese
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
-
overview: metal content
additional information
-
overview: metal content
additional information
-
Co-sub-MnSOD does not have any detectable activity. Thermodynamic stability decreases in the order Co-sub-MnSOD, MnSOD, Fe-sub-MnSOD
additional information
-
the enzyme selectively chooses the Mn ion as its native cofactor, although Co and Fe ions can stably substitute the Mn ion. Molecular mechanism and structural basis of the metal specificity, preparation of Mn-superoxide dismutase, Fe-Mn-superoxide dismutase, and Co-Mn-superoxide dismutase, the cognate metal characters tuned by the metal microenvironment dominate the metal specificity of the enzyme, overview. The H-bond between Gln178 and Tyr64 in Mn-superoxide dismutase is stronger than that in Fe-Mn-superoxide dismutase, while the coupling between Gln178 and the coordinated solvent of Mn-superoxide dismutase is weaker than that of Fe-Mn-superoxide dismutase. In the oxidized Fe-Mn-superoxide dismutase, tight coupling between Gln178 and the coordination hydroxyl may reduce its redox potential and thus impact its catalytic activity
additional information
no MnSOD and Cu/ZnSOD in Crypthecodinium cohnii
additional information
no MnSOD and Cu/ZnSOD in Crypthecodinium cohnii
additional information
no MnSOD and Cu/ZnSOD in Crypthecodinium cohnii
additional information
-
no MnSOD and Cu/ZnSOD in Crypthecodinium cohnii
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
-
overview: metal content
additional information
-
overview: metal content
additional information
no enzyme activity with Fe2+-reconstituted enzyme
additional information
the Fe2+-reconstituted SOD is inactive
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
-
overview: metal content
additional information
-
overview: metal content
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
-
overview: metal content
additional information
-
Cu2+ is not necessarily required
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
-
overview: metal content
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
-
overview: metal content
additional information
-
the enzyme contains no iron
additional information
added Zn2+ and Cu2+ do not affect the enzyme activity or structure
additional information
-
added Zn2+ and Cu2+ do not affect the enzyme activity or structure
additional information
the enzyme contains 6 metal binding sites
additional information
the enzyme contains no copper, zinc, or manganese
additional information
-
the enzyme contains no copper, zinc, or manganese
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
-
overview: metal content
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
-
overview: metal content
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
-
overview: metal content
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
-
overview: metal content
additional information
-
overview: metal content
additional information
-
no evidence for the presence of either iron or copper/zinc SODs in Phytophthora cinnamomi
additional information
measurement of Cu and Zn content of PschSOD by ICP-MS, zincon, and bathocuproeine protocols
additional information
-
measurement of Cu and Zn content of PschSOD by ICP-MS, zincon, and bathocuproeine protocols
additional information
-
exposure to a pH of 3.8 in the presence of 8.0 M urea labilizes the manganese and allows the preparation of a colorless and inactive apoenzyme, that can be reconstituted by subsequent treatment with MnCl2
additional information
-
metal content of the enzyme depends on the growth condition: anaerobic culture condition promote a higher Fe-content, aerobic conditions promote a higher Mn-content
additional information
protein contains no manganese
additional information
-
protein contains no manganese
additional information
-
no effect: Cu2+, Co2+, Ca2+
additional information
metal content analysis of the recombinant enzyme
additional information
-
metal content analysis of the recombinant enzyme
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
-
overview: metal content
additional information
-
no effect: Cu2+, Ca2+
additional information
-
no effect on enzyme activity by Cu2+ at 0.1-5 mM
additional information
-
different values of the Mn/Fe ratio in the active site prove that the type of metal is crucial for the regulation of the activity of recombinant SmSOD
additional information
Thermochaetoides thermophila
-
the purified enzyme contains no Fe
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
-
overview: metal content
additional information
Zn, Ni, and Fe contents of the His29Ala enzyme mutant are 180, 76, and 300 ng/mg, respectively, and the amount of Fe is almost twice that of Zn and fourtimes that of Ni, suggesting that His29Ala mainly is a Fe-SOD. Metal binding trutcure involving residues His29 and His171, overview
additional information
iron, manganese, and nickel contents are below the detection level
additional information
-
iron, manganese, and nickel contents are below the detection level
additional information
binding ligands: His27, His74, Asp157 and His161 in SodB
additional information
binding ligands: His27, His74, Asp157 and His161 in SodB
additional information
binding ligands: His27, His74, Asp157 and His161 in SodB
additional information
-
binding ligands: His27, His74, Asp157 and His161 in SodB
additional information
binding ligands: His27, His82, Asp169 and His173 in SodA
additional information
binding ligands: His27, His82, Asp169 and His173 in SodA
additional information
binding ligands: His27, His82, Asp169 and His173 in SodA
additional information
-
binding ligands: His27, His82, Asp169 and His173 in SodA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,4,6-Trinitrobenzenesulfonate
-
0.5 M, pH 9.0, 25°C, native wild-type enzyme: half-life 3.5 min, recombinant wild-type enzyme: half-life: 5.1 min, recombinant mutant H30A: half-life 5.5 min, recombinant mutant K170R half-life 101 min
4-chloromercuribenzoate
-
26.6% inhibition at 1 mM
5,5'-dithiobis(2-nitrobenzoate)
-
Mn-SOD
5-(((2,4-dichlorobenzyl)(propyl)amino)methyl)-1H-pyrazol-3(2H)-one
5-(((3,5-dichlorobenzyl)(ethyl)amino)methyl)-1H-pyrazol-3(2H)-one
5-(((3,5-dichlorobenzyl)(isopropyl)amino)methyl)-1H-pyrazol-3(2H)-one
5-(((3,5-dichlorobenzyl)(methyl)amino)methyl)-1H-pyrazol-3(2H)-one
5-(((3,5-dichlorobenzyl)(propyl)amino)methyl)-1H-pyrazol-3(2H)-one
5-(((3,5-dichlorophenethyl)(methyl)amino)methyl)-1H-pyrazol-3(2H)-one
5-(((3-(3,5-dichlorophenyl)propyl)(methyl)amino)methyl)-1H-pyrazol-3(2H)-one
5-((benzyl(3,5-dichlorobenzyl)amino)methyl)-1H-pyrazol-3(2H)-one
5-((cyclopropyl(3,5-dichlorobenzyl)amino)methyl)-1H-pyrazol-3(2H)-one
5-[(3,5-dichlorophenoxy)methyl]-1,2-dihydro-3H-pyrazol-3-one
5-[[(3,5-dichlorophenyl)(methyl)amino]methyl]-1,2-dihydro-3H-pyrazol-3-one
beta-naphthoquinone-4-sulfonic acid
-
-
chloroform:ethanol solution
the Mn- and Fe-SODs of Yérsinia enterocolitica are inhibited by chloroform:ethanol solution; the Mn- and Fe-SODs of Yérsinia enterocolitica are inhibited by chloroform:ethanol solution; the Mn- and Fe-SODs of Yérsinia enterocolitica are inhibited by chloroform:ethanol solution
concanavalin A
-
inhibition in vivo and in vitro, essentially dependent on calcium chloride
-
di-N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium sulfate
diethyl dicarbonate
-
at 2.5 mM
Dithiocarbamate
strongly inhibits the activity of the rOf-cCu/ZnSOD
DTPA
-
i.e. diethylenetriamine-N,N,N,N,N-pentaacetic acid, inhibits the reductive decomposition of S-nitroso-L-glutathione catalyzed by superoxide dismutase by binding to the solvent-exposed active-site copper of one subunit without removing it. The resulting conformational change at the second active site inhibits the S-nitroso-L-glutathione reductase but not superoxide dismutase activity
DTT
13% inhibition at 2.5 mM
guanidine hydrochloride
-
Guanidinium chloride
-
Mn-SOD, 70% inhibition at 1 mM
guanidinium hydrochloride
HgCl2
-
1 mM, inhibition of isozyme SODI
HS-
substrate analogue, formation of a green complex upon binding
iodoacetic acid
-
23.5% inhibition at 1 mM
Mn(Me-Phimp)2(ClO4)
-
i.e. Mn(2-(1-(2-phenyl-2-(pyridine-2-yl)hydrazono)ethyl)phenol)chlorate, active as cofactor in superoxide dismutation reaction
Mn(N-Phimp)2
-
i.e. Mn-(2-((2-phenyl-2-(pyridin-2-yl)hydrazono)methyl)naphthalen-1-ol), active as cofactor in superoxide dismutation reaction
Mn(N-Phimp)2(ClO4)
-
i.e. Mn(2-((2-phenyl-2-(pyridin-2-yl)hydrazono)methyl)naphthalen-1-ol)chlorate, active as cofactor in superoxide dismutation reaction
Mn(Phimp)2
-
i.e. Mn(2-((2-phenyl-2-(pyridin-2-yl)hydazono)methyl)phenol), active as cofactor in superoxide dismutation reaction
Mn(Phimp)2(ClO4)
-
i.e. Mn(2-((2-phenyl-2-(pyridin-2-yl)hydazono)methyl)phenol)chlorate, active as cofactor in superoxide dismutation reaction
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium chloride
-
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium citrate
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium dibasic phosphate
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium L-tartrate
N-ethyl-5-phenylisoxazolium 3'-sulfonate
-
i.e. Woodwards reagent, Kat 50 mM
O2-
-
substrate inhibition for mutant C140S/Q143A
OH-
-
Cu,Zn-SOD, competitively
para-diazobenzene sulfonic acid
-
-
Pectin
-
from avocado root or cell wall
Penicillamine
-
copper-chelator, wild-type and mutant Cu,Zn-SOD
perchlorate
-
competitive
phenyl mercuric acetate
-
Cu,Zn-SOD
Phenylglyoxal
-
25% activity remaining after 3 h for native and recombinant wild-type and recombinant mutant H30A, complete inactivation of recombinant mutant K179R after 7 min
phenylmethanesulfonyl fluoride
irreversible inactivation by attachment of a molecule phenylmethanesulfonyl fluoride to the active site Tyr41 reinforcing the heat stability of the enzyme, overview
phenylmethylsulfonyl fluoride
phosphate
-
100 mM, 50% inhibition
polygalacturonase
-
from avocado root or cell wall
-
Sodium diethyldithiocarbamate
-
complete inhibition above 0.1 mM
Sodium fluoride
inhibits both the Mn- and Fe-reconstituted enzyme. The concentrations of sodium fluoride causing 50% inhibition of the Mn- and Fe reconstituted enzymes are 89 and 13 mM, respectively
tetrathiomolybdate
-
i.e. ATN-224, choline salt, inhibition leads to antiangiogenic and antitumour effects
-
trichloromethane-ethanol
-
-
2-mercaptoethanol
-
25% inhibition of Mn-reconstituted wild-type enzyme at 10 mM, no inhibition at 1 mM
2-mercaptoethanol
17% inhibition at 3 mM
2-mercaptoethanol
gradual inhibition by increasing concentration of 2-mercaptoethanol, 20% inhibition at 2 mM, 36% at 16 mM
2-mercaptoethanol
8 mM, slight inhibition
2-mercaptoethanol
-
15% inhibition
5-(((2,4-dichlorobenzyl)(propyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 630 nM
5-(((2,4-dichlorobenzyl)(propyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 630 nM
5-(((3,5-dichlorobenzyl)(ethyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 420 nM
5-(((3,5-dichlorobenzyl)(ethyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 420 nM
5-(((3,5-dichlorobenzyl)(isopropyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 0.00108 mM
5-(((3,5-dichlorobenzyl)(isopropyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 0.00108 mM
5-(((3,5-dichlorobenzyl)(methyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 480 nM
5-(((3,5-dichlorobenzyl)(methyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 480 nM
5-(((3,5-dichlorobenzyl)(propyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 470 nM
5-(((3,5-dichlorobenzyl)(propyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 470 nM
5-(((3,5-dichlorophenethyl)(methyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 0.00164 mM
5-(((3,5-dichlorophenethyl)(methyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 0.00164 mM
5-(((3-(3,5-dichlorophenyl)propyl)(methyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 0.00332 mM
5-(((3-(3,5-dichlorophenyl)propyl)(methyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 0.00332 mM
5-((benzyl(3,5-dichlorobenzyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 0.00245 mM
5-((benzyl(3,5-dichlorobenzyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 0.00245 mM
5-((cyclopropyl(3,5-dichlorobenzyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 0.00134 mM
5-((cyclopropyl(3,5-dichlorobenzyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 0.00134 mM
5-[(3,5-dichlorophenoxy)methyl]-1,2-dihydro-3H-pyrazol-3-one
-
EC50 value is 400 nM
5-[(3,5-dichlorophenoxy)methyl]-1,2-dihydro-3H-pyrazol-3-one
-
EC50 value is 400 nM
5-[[(3,5-dichlorophenyl)(methyl)amino]methyl]-1,2-dihydro-3H-pyrazol-3-one
-
EC50 value is 570 nM
5-[[(3,5-dichlorophenyl)(methyl)amino]methyl]-1,2-dihydro-3H-pyrazol-3-one
-
EC50 value is 570 nM
azide
the azide ion acts as a strong competitive inhibitor for SOD by binding directly to the active site metal. Azide is bound end-on at the sixth coordinate position of the manganese ion. Tetrameric electrostatic surfaces are calculated incorporating accurate partial charges for the active site in three states, including a state with superoxide coordinated to the metal using the position of azide as a model
azide
-
causes 50% inhibition at 20 mM
azide
Mn2+-reconstituted recombinant enzyme and Fe2+-reconstututed recombinant enzyme displays relatively strong resistance against azide. Mn2+- and Fe2+-reconstituted activity decreases 50% with 380 and 340 mM azide, respectively
Ba2+
inhibitory at 1 mM
Ca2+
inhibitory at 1 mM
chloride
-
-
chloride
-
100 mM, 50% inhibition
chloroform
-
Mn-SOD
chloroform
recombinant PsSOD is sensitive to a mixture of chloroform and ethanol in the ratio 3:5. Mixing the recombinant PsSOD enzyme and the solvent mixture by 2:1 and 1:1, the relative activity is 36.4 and 13.6%, respectively. In addition, no enzymatic activity remains after incubation at 1:2 mixture
CN-
-
-
CN-
slight inhibition, Mn-SOD
CN-
-
no inhibition Mn-SOD
CN-
-
at 1-3 mM, complete inhibition; Cu,Zn-SOD
CN-
-
slight inhibition, Mn-SOD
CN-
-
extracellular enzyme
CN-
Megalodesulfovibrio gigas
-
no inhibition: Fe-SOD
CN-
-
contains a cyanide-sensitive enzyme in cytosol and mitochondrial intermembrane space and one cyanide-insensitive enzyme in mitochondrial matrix; Cu,Zn-SOD; no inhibition Mn-SOD
CN-
-
no inhibition Mn-SOD
CN-
-
no inhibition Mn-SOD
CN-
-
Cu,Zn-SOD; no inhibition Mn-SOD
CN-
-
SOD-2 and SOD-4 inhibited, SOD-3 not inhibited
Co2+
inhibitory at 1 mM
Co2+
-
inhibits by 25% at 10 mM
Cu2+
50% inhibition at 1 mM
Cu2+
-
slight inhibition at 1.0-5.0 mM
cyanide
-
the isoenzyme Cu/Zn-SOD is cyanide-sensitive, while the Mn-SOD is not
cyanide
Radix lethospermi
-
-
di-N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium sulfate
-
EC50 value is 480 nM
di-N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium sulfate
-
EC50 value is 480 nM
diethyldithiocarbamate
-
-
diethyldithiocarbamate
complete inhibition, Cu,Zn-SOD
diethyldithiocarbamate
-
-
diethyldithiocarbamate
-
-
diethyldithiocarbamate
-
-
diethyldithiocarbamate
-
Mn-SOD; slightly
diethyldithiocarbamate
a specific inhibitor for CuZn-SODs
diethyldithiocarbamate
-
strong inhibition
diethyldithiocarbamate
-
strong inhibition, extracellular enzyme
diethyldithiocarbamate
-
copper-chelator, wild-type and mutant Cu,Zn-SOD
diethyldithiocarbamate
-
inhibits recombinant Cu,Zn-SOD, at 0.05-0.1 mM inactivation occurs gradually within 1 h
diethyldithiocarbamate
-
slightly
diethyldithiocarbamate
complete inhibition at 1.4 mM, a specific inhibitor for CuZn-SODs
diethyldithiocarbamate
-
causes decline of the enzyme in various tissues after intraperitoneal injection, alpha-tocopherol feeding prior to application of diethyldithiocarbamate leads to reduced inhibition of the enzyme
diethyldithiocarbamate
-
Cu,Zn-SOD
diethyldithiocarbamate
-
40% inhibition
diethyldithiocarbamate
inhibits SodC specifically
EDTA
-
60% inhibition of Mn-reconstituted wild-type enzyme at 10 mM, 20% at 1 mM
EDTA
-
i.e. diethylenediamine-N,N,N,N-tetraacetic acid, inhibits the reductive decomposition of S-nitroso-L-glutathione catalyzed by superoxide dismutase by binding to the solvent-exposed active-site copper of one subunit without removing it. The resulting conformational change at the second active site inhibits the S-nitroso-L-glutathione reductase but not superoxide dismutase activity
EDTA
15% inhibition at 0.5 mM
EDTA
-
inhibition is reversible by Cu and Zn
EDTA
strong inhibition at 10 mM
EDTA
gradual inhibition by increasing concentration of EDTA
EDTA
-
66% inhibition at 1 mM
EDTA
Radix lethospermi
-
2 mM, 18% inhibition
ethanol
-
Mn-SOD
ethanol
recombinant PsSOD is sensitive to a mixture of chloroform and ethanol in the ratio 3:5. Mixing the recombinant PsSOD enzyme and the solvent mixture by 2:1 and 1:1, the relative activity is 36.4 and 13.6%, respectively. In addition, no enzymatic activity remains after incubation at 1:2 mixture
Fe2+
inhibitory at 1 mM
Fe2+
-
inhibits by 44% at 10 mM
fluoride
-
Fe-SOD
fluoride
recombinant Fe-reconstituted SOD
guanidinium hydrochloride
-
25% inhibition of Mn-reconstituted wild-type enzyme at 10 mM
guanidinium hydrochloride
40% inhibition at 2 M, 85% at 5 M
guanidinium hydrochloride
69% inhibition at 6 M
guanidinium hydrochloride
6 M, slight inhibition
guanidinium hydrochloride
-
up to 50% inhibition
H2O2
-
no inhibition: Mn-SOD
H2O2
inactivates the Fe-reconstituted SOD in a time-dependent manner, but not the Mn-reconstituted enzyme. The incubation time for 50% inactivation of the Fe-reconstituted enzyme in the presence of 0.24 mM H2O2 is 50 min
H2O2
complete inhibition; Cu,Zn-SOD
H2O2
-
Cu,Zn-SOD; no inhibition: Mn-SOD
H2O2
no inhibition: Mn-SOD
H2O2
-
Cu,Zn-SOD; no inhibition: Mn-SOD
H2O2
50% inhibition at 4.3 mM
H2O2
-
no inhibition: Mn-SOD
H2O2
-
no inhibition: Mn-SOD
H2O2
2.5 mM, 20% residual activity
H2O2
inactivation of FeSOD; inactivation of FeSOD; inactivation of FeSOD
H2O2
58% inhibition at 2 mM
H2O2
-
partial sensitivity
H2O2
-
Cu,Zn-SOD; no inhibition: Mn-SOD
H2O2
-
Cu,Zn-SOD; no inhibition: Mn-SOD
H2O2
-
no inhibition: Mn-SOD
H2O2
-
Cu,Zn-SOD; no inhibition: Mn-SOD
H2O2
-
Cu,Zn-SOD; no inhibition: Mn-SOD
H2O2
-
Cu,Zn-SOD; no inhibition: Mn-SOD
H2O2
-
extracellular enzyme, rapidly
H2O2
gradual inhibition by increasing concentration of H2O2, 36% inhibition at 2 mM, 81% at 16 mM
H2O2
-
10 mM, complete inhibition
H2O2
Megalodesulfovibrio gigas
-
-
H2O2
-
Cu,Zn-SOD; no inhibition: Mn-SOD
H2O2
-
no inhibition: Fe-SOD
H2O2
-
H2O2 does not show significant inhibition of the SOD activity in cell-free extracts prepared from cells grown in Mn-rich medium, but inhibits 30% of the enzyme activity in cell extracts from cells grown in Fe-rich medium
H2O2
-
Cu,Zn-SOD; no inhibition: Mn-SOD
H2O2
-
no inhibition: Mn-SOD
H2O2
-
Cu,Zn-SOD; no inhibition: Mn-SOD
H2O2
-
50 mM, 100% inhibition
H2O2
-
Cu,Zn-SOD; no inhibition: Mn-SOD
H2O2
-
no inhibition: Mn-SOD
H2O2
addition of 5 mM of hydrogen peroxide (H2O2) completely inhibits of the enzyme
H2O2
-
no inhibition: Mn-SOD
H2O2
half-life of 22 min both in absence or presence of 2-mercaptoethanol
H2O2
preincubation in 5 mM H2O2 for 30 min results in a loss of 91% activity
H2O2
-
no inhibition: Mn-SOD
H2O2
Radix lethospermi
-
-
H2O2
-
inhibition at 10 mM, the Fe-SOD is less sensitive
H2O2
distinguishes Fe-SOD from Mn-SOD, since it inactivates only Fe-SOD
H2O2
-
90% inhibition at 5 mM
H2O2
-
no inhibition: Fe-SOD; no inhibition: Mn-SOD
H2O2
-
no inhibition: Mn-SOD
H2O2
-
inactivation kinetics of rSmSOD by hydrogen peroxide, overview
H2O2
Thermochaetoides thermophila
-
H2O2
-
Cu,Zn-SOD; no inhibition: Mn-SOD
H2O2
5 mM, partial inhibition
H2O2
-
no inhibition: Mn-SOD
H2O2
-
SOD-2 and SOD-4 inhibited, SOD-3 not
Hg2+
-
strong inhibition
Hg2+
-
35% inhibition at 0.1 mM, complete inhibition at 5 mM
Hg2+
-
inhibits by 35% at 10 mM
hydrogen peroxide
-
hydrogen peroxide
-
up to 80% inhibition
imidazole
above 1.6 mM
imidazole
1 mM, slight inhibition
Iodine
-
-
Iodine
-
completely inhibits the cell wall SOD, the inhibition is partly, up to 70%, reversed by 2-mercaptoethanol
iodoacetamide
-
Cu,Zn-SOD
iodoacetamide
-
2 mM, 15% inhibition
K+
-
inhibits by 14% at 10 mM
KCN
-
KCN
5 mM, 40% residual activity
KCN
-
30% inhibition at 2 mM
KCN
3 mM, 65% loss of activity
KCN
strongly inhibits the activity of the rOf-cCu/ZnSOD
KCN
complete inhibition at 0.16 mM, a specific inhibitor for CuZn-SODs
KCN
-
inhibition at 10 mM, the Fe-SOD is less sensitive
KCN
-
complete inhibition at 5 mM
KCN
Thermochaetoides thermophila
-
KCN
2 mM, complete inhibition
Mg2+
inhibitory at 1 mM
Mg2+
30% inhibition at 1 mM
Mg2+
-
25% inhibition at 5 mM
Mg2+
-
inhibits by 64% at 10 mM
Mn2+
-
55% inhibition
Mn2+
-
35% inhibition at 5 mM
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium chloride
-
EC50 value is 510 nM
-
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium chloride
-
EC50 value is 510 nM
-
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium citrate
-
EC50 value is 480 nM
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium citrate
-
EC50 value is 480 nM
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium dibasic phosphate
-
EC50 value is 480 nM
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium dibasic phosphate
-
EC50 value is 480 nM
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium L-tartrate
-
EC50 value is 480 nM
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium L-tartrate
-
EC50 value is 480 nM
N3-
-
-
N3-
-
Mn-SOD is inhibited by 50%, enzyme reconstituted by Fe3+ shows increased inhibition
N3-
-
extracellular enzyme; Mn-SOD
N3-
-
binds to Fe3+, but has no effect on activity
N3-
-
no inhibition, Fe-SOD
N3-
-
extracellular enzyme
N3-
Megalodesulfovibrio gigas
-
-
N3-
-
no inhibition, Fe-SOD
N3-
-
no inhibition: Zn,Cu-SOD
N3-
-
SOD-2 and SOD-4 inhibited, SOD-3 not inhibited
NaCl
-
slight inhibition at 1 mM
NaCl
60% activity remains at 2.5 M NaCl
NaCl
activity of SaCSD1 decreases with the increase of salt concentration
NaN3
-
13.5 mM, inhibition
NaN3
-
inactivates 15% and 24% of the SODs present in cell extracts prepared from cells grown in the Mn- and Fe-rich media, respectively
NaN3
low inhibition by sodium azide, 40% inhibition at 50 mM
NaN3
50% inhibition at 6.9 mM in absence, at 9.0 mM in presence of 2-mercaptoethanol
NaN3
-
inhibition at 5 mM, the Fe-SOD is less sensitive
NaN3
-
inhibits the enzyme mutants Y41F and H155Q, but not the wild-type enzyme
NaN3
Thermochaetoides thermophila
-
-
Ni2+
inhibitory at 1 mM
Ni2+
inhibits slightly at 1 mM
Ni2+
-
inhibits by 57% at 10 mM
o-phenanthroline
-
-
o-phenanthroline
-
Mn-SOD
o-phenanthroline
-
slightly
o-phenanthroline
-
depending on assay method; Fe-SOD
p-hydroxymercuribenzoate
-
completely inhibited at 1 mM; Mn-SOD
p-hydroxymercuribenzoate
-
completely inhibited at 1 mM; Mn-SOD
peroxynitrite
almost complete inhibition via nitration of active-site residue Y34, no significant change in conformation upon nitration. Inhibition occurs either through a steric effect of 3-nitrotyrosine 34 that impedes substrate binding or through an electrostatic effect of the nitro group
peroxynitrite
50% inhibition at 0.032 mM in absence, at 0.153 mM in presence of 2-mercaptoethanol
phenylmethylsulfonyl fluoride
-
phenylmethylsulfonyl fluoride
-
2 mM, 15% inhibition
PMSF
-
PMSF
-
irreversible inhibition by binding to active site Tyr41
potassium cyanide
-
2 mM, complete inhibition
potassium cyanide
-
up to 90% inhibition
SDS
-
60% inhibition of Mn-reconstituted wild-type enzyme at 1%, and 40% inhibition of the Mn-reconstituted N-terminal domain
SDS
-
recombinant Cp-icCuZnSOD is active and retains more than 80% activity under treatment with 1-6% SDS. It retains 70% activity after treatment with 8% SDS but activity is rapidly lowered to 52% after treatment with 10% SDS
SDS
-
0.5 mM, complete inhibition
SDS
-
19% inhibition at 0.1 mM, complete inhibition at 0.5 mM
SDS
-
1 mM, inhibition of isozyme SODI
Sodium azide
50% inhibition of the Fe-reconstituted enzyme at 41 mM. Sodium azide does not inhibit the Mn-reconstituted superoxide dismutase even at concentrations up to 400 mM
Sodium azide
-
33% inhibition
Sodium azide
-
32% inhibition
Sodium cyanide
-
-
Sodium cyanide
-
36% inhibition
Sodium dodecyl sulfate
-
1%, complete inhibition
Sodium dodecyl sulfate
-
2% w/v, Cu,Zn-SOD and EC-SOD
Sodium dodecyl sulfate
-
-
sodium dodecylsulfate
-
up to 67% inhibition
sodium dodecylsulfate
Radix lethospermi
-
2 mM, 34% inhibition
Triton X-100
-
Triton X-100
70% inhibition
Urea
-
Mn-SOD, 90% inhibition at 6 M
Urea
8 M, slight inhibition
Zn2+
inhibitory at 1 mM
Zn2+
-
strong inhibition at 1.0-5.0 mM
Zn2+
-
12% inhibition at 5 mM
ZnCl2
-
slight inhibition at 1 mM
additional information
no inhibition by hydrogen peroxide or potassium cyanide
-
additional information
-
no inhibition by hydrogen peroxide or potassium cyanide
-
additional information
no inhibition by KCN of MnSOD
-
additional information
no inhibition by KCN of MnSOD
-
additional information
-
enzyme is not inhibited by H2O2 and unusually resistant to KCN; SodC is resistant to inhibition by H2O2 and is unusually resistant to KCN for a Cu,Zn-SOD
-
additional information
no inhibition by sodium azide or potassium cyanide
-
additional information
-
no inhibition by sodium azide or potassium cyanide
-
additional information
the enzyme is resistant to denaturation by sodium dodecyl sulfate (SDS) and urea
-
additional information
no inhibition by 10 mM NaN3
-
additional information
-
no inhibition by 10 mM NaN3
-
additional information
not inhibitory
H2O2 up to 80 mM
-
additional information
-
not inhibitory
H2O2 up to 80 mM
-
additional information
-
not inhibitory: NaN3
-
additional information
not inhibitory: NaN3
-
additional information
not inhibitory: sodium dodecylsulfate
-
additional information
imidazole up to 0.8 M and sodium dodecylsulfate up to 4% are not inhibitory
-
additional information
no inhibition by CN; no inhibition by CN; no inhibition by CN
-
additional information
no inhibition by CN; no inhibition by CN; no inhibition by CN
-
additional information
no inhibition by CN; no inhibition by CN; no inhibition by CN
-
additional information
-
no inhibition by CN; no inhibition by CN; no inhibition by CN
-
additional information
no inhibition by NaN3 and KCN
-
additional information
-
no inhibition by NaN3 and KCN
-
additional information
-
UV-B radiation decreases the SOD activity
-
additional information
-
not inhibitory: sodium dodecyl sulfate up to 4%
-
additional information
-
not inhibitory: cyanide
-
additional information
not inhibitory: sodium dodecylsulfate up to 2.5%
-
additional information
-
not inhibitory: sodium dodecylsulfate up to 2.5%
-
additional information
-
no inhibition by dithiothreitol and beta-mercaptoethanol
-
additional information
insensitivity of the recombinant enzyme to both KCN and H2O2
-
additional information
the enzyme shows good tolerance to some inhibitors, detergents, and denaturants
-
additional information
insensitivity of the recombinant enzyme to both KCN and H2O2. The enzyme shows a relatively good tolerance to some inhibitors, detergents, and denaturants, such as 2-mercaptoethanol, dithiothreitol, phenylmethylsulfonyl fluoride, Chaps, Triton X-100, urea, and guanidine hydrochloride
-
additional information
tributyltin chloride does not affect enzyme expression
-
additional information
-
tributyltin chloride does not affect enzyme expression
-
additional information
the conserved, active-site residue Tyr34 mediates product inhibition
-
additional information
-
the conserved, active-site residue Tyr34 mediates product inhibition
-
additional information
-
ligand complex synthesis, electrochemical properties, and structure determination, overview
-
additional information
NO-induced damage in eSOD causes alteration in hydrophobic or aromatic amino acids and protein carbonyl contents
-
additional information
-
NO-induced damage in eSOD causes alteration in hydrophobic or aromatic amino acids and protein carbonyl contents
-
additional information
-
pyrazolone derivatives are inhibitors of Cu/Zn superoxide dismutase 1 (SOD1)-dependent protein aggregation and are useful as drugs in treatment of amyotrophic lateral sclerosis (ALS). Design and synthesis of a series of tertiary amine-containing pyrazolones and their structure-activity relationships, conjugate salts greatly improved their solubility, overview
-
additional information
-
insensitive to fluoride
-
additional information
-
no inhibition of Cu/ZnSOD by 10 mM H2O2, 1 mM CaCl2, and 1 mM NaN3
-
additional information
-
not inhibitory: cyanide
-
additional information
-
not inhibitory: cyanide
-
additional information
-
not inhibitory: KCN
-
additional information
the enzyme is not inhibited by cyanide (10 mM)
-
additional information
-
the enzyme is not inhibited by cyanide (10 mM)
-
additional information
-
compound 2-[(3-iodophenyl)methylsulfanyl]-5-pyridin-4-yl-1,3,4-oxadiazole, a known protein kinase inhibitor, decreases enzyme mutant G93A-SOD1 expression in vitro and in the brain and spinal cord in vivo, but this compound has a biphasic dose response curve and a likely toxophore which limit its therapeutic window for chronic disease such as amyotrophic lateral sclerosis (ALS). Therefore, a focused library of analogues are tested for the ability to decrease SOD1 expression in vitro. This exercise results in the identification of a lead compound with improved drug-like characteristics and activity. Development of small molecules that reduce the expression of etiologically relevant toxic proteins, structureactivity relationships, overview. Compounds 3-[1-(3-hydroxypropyl)-1H-pyrrolo[2,3-b]pyridin-3-yl]-4-(pyrazin-2-yl)-1H-pyrrole-2,5-dione, 2-chloro-1-(4,5-dibromothiophen-2-yl)ethan-1-one, 2-bromo-1-(4-bromophenyl)ethan-1-one, 4-(5-[[(3-iodophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(3-methoxyphenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(3-fluorophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-[5-([[4-(trifluoromethyl)phenyl]methyl]sulfanyl)-1,3,4-oxadiazol-2-yl]pyridine, 4-(5-[[(3-chlorophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(3-nitrophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(3-bromophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(4-methoxyphenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(4-chlorophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(4-bromophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(4-iodophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(4-fluorophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(4-methylphenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(4-nitrophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(4-nitrophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine suppress the enzyme expression
-
additional information
-
pyrazolone derivatives are inhibitors of Cu/Zn superoxide dismutase 1 (SOD1)-dependent protein aggregation and toxicity, and are useful as drugs in treatment of amyotrophic lateral sclerosis (ALS). Design and synthesis of a series of tertiary amine-containing pyrazolones and their structure-activity relationships, conjugate salts greatly improve their solubility, overview. Identification of several neuron-protection scaffolds based on mitigating protein aggregation and toxicity. A tertiary amine fragment is incorporated into the linker between the pyrazolone and the aryl group on the basis of principles of optimal brain exposure in CNS drug molecule design, the tertiary amine pyrazolone scaffolds exhibited superior properties for potential neuronal activity and in metabolic studies, such as microsomal stability, plasma stability, and Caco-2 permeability
-
additional information
poor inhibition by KCN, no inhibition by EDTA and cuprizone
-
additional information
-
poor inhibition by KCN, no inhibition by EDTA and cuprizone
-
additional information
-
not inhibitory: sodium azide, potassium cyanide
-
additional information
-
not inhibitory: EDTA
-
additional information
no inhibition by EDTA and poor inhibition by NaN3
-
additional information
-
no inhibition by EDTA and poor inhibition by NaN3
-
additional information
-
not inhibitory: cyanide, hydrogen peroxide, ditiothreitol, sodium azide, Triton X-100, and 2-mercaptoethanol
-
additional information
-
not inhibitory: cyanide
-
additional information
-
no inhibition by KCN or H2O2. Level of activity of the MnSOD polypeptides decreases in the presence of avocado root or cell wall components, addition of avocado root, pectin, or polygalacturonase to the incubation medium results in a significant increase in the accumulation of O2.-
-
additional information
not inhibitory: sodium dodecylsulfate
-
additional information
-
not inhibitory: sodium dodecylsulfate
-
additional information
-
cyanide at 5 mM and H2O2 at 3 mM have no effect on the activity of the enzyme
-
additional information
-
no inhibition by N-ethylmaleide
-
additional information
-
no effect: Cu2+, Co2+, Ca2+, sodium dodecylsulfate, 2-mercaptoethanol
-
additional information
Radix lethospermi
-
not inhibitory: dithiothreitol, sodium azide, 2-mercaptoethanol
-
additional information
-
no effect on the enzyme by alpha-tocopherol in absence of diethyldithiocarbamate
-
additional information
-
melatonin, testosterone, dihydrotestosterone, estradiol, and vitamin D induce activation of SOD1 in mitochondria. Enzyme activation is not affected by furafylline, a selective inhibitor of the P450 1A2 isoform, but is inhibited by omeprazole and ketoconazole, and by tiron, a superoxide radical specific scavenger
-
additional information
no inhibition by DTT. Ba2+, Ca2+, Ni2+, and Fe2+ have no obvious impact to enzyme activity at 1 mM
-
additional information
-
no inhibition by DTT. Ba2+, Ca2+, Ni2+, and Fe2+ have no obvious impact to enzyme activity at 1 mM
-
additional information
-
the enzyme is insensitive to cyanide inhibition
-
additional information
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
-
additional information
-
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
-
additional information
-
no inhibition of Cu,Zn-SOD by sodium azide and O-phenanthroline
-
additional information
-
no effect: Cu2+, Ca2+
-
additional information
the SaCSD1 protein is very susceptive to pepsin digestion
-
additional information
-
the SaCSD1 protein is very susceptive to pepsin digestion
-
additional information
the enzyme is insensitive to malondialdehyde (MDA) or 4-hydroxy-2-nonenal (HNE); the enzyme is insensitive to malondialdehyde (MDA) or 4-hydroxy-2-nonenal (HNE). Enzyme Mn-SOD is insensitive to cyanide
-
additional information
the enzyme is insensitive to malondialdehyde (MDA) or 4-hydroxy-2-nonenal (HNE); the enzyme is insensitive to malondialdehyde (MDA) or 4-hydroxy-2-nonenal (HNE). Enzyme Mn-SOD is insensitive to cyanide
-
additional information
no inhibition by NaN3
-
additional information
-
no inhibition by NaN3
-
additional information
-
no inhibition of the purified enzyme by 6 M guanidinium chloride or by proteases trypsin and Staphylococcus aureus V8 protease
-
additional information
no inhibition of the purified enzyme by 6 M guanidinium chloride or by proteases trypsin and Staphylococcus aureus V8 protease
-
additional information
-
the native enzyme is degraded by pepsin and trypsin, while the polysialylated SOD is resistant to pepsin and trypsin
-
additional information
-
urea and iodoacetamide do not affect the enzymatic activity
-
additional information
no inhibition by KCN and H2O2
-
additional information
-
no inhibition by KCN and H2O2
-
additional information
Thermochaetoides thermophila
-
no inhibition by KCN and H2O2
-
additional information
Thermochaetoides thermophila
no inhibition by NaN3
-
additional information
-
not inhibitory: potassium cyanide, H2O2
-
additional information
-
isoyzme SODI is insensitive to H2O2 and KCN
-
additional information
-
no inhiibtion by CN-
-
additional information
-
the enzyme is insensitive to potassium cyanide
-
additional information
the purified recombinant enzyme shows a high degree of resistance to detergent, ethanol and protease digestion
-
additional information
-
the purified recombinant enzyme shows a high degree of resistance to detergent, ethanol and protease digestion
-
additional information
no inhibition by diethyldithiocarbamate; no inhibition by diethyldithiocarbamate
-
additional information
no inhibition by diethyldithiocarbamate; no inhibition by diethyldithiocarbamate
-
additional information
no inhibition by diethyldithiocarbamate; no inhibition by diethyldithiocarbamate
-
additional information
-
no inhibition by diethyldithiocarbamate; no inhibition by diethyldithiocarbamate
-
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1.41
-
purified Cu,Zn-SOD
10500
-
purified native enzyme, pH 7.8, 25°C
113.8
-
purified isozyme SODII
115.8
Thermochaetoides thermophila
-
purified native enzyme
1250
purified recombinant His-tagged enzyme, pH 7.8, 37°C, substrate riboflavin
127.4
Thermochaetoides thermophila
purified recombinant enzyme, pH 6.5, 60°C
12800
purified recombinant SodA, 4°C, pH 6.0
1331
recombinant SOD1-Lys7 chimera, pH not specified in the publication, temperature not specified in the publication
1418
-
purified recombinant enzyme, one unit of SOD activity is defined as the amount of enzyme required to inhibit the autooxidation of pyrogallol to 50%. pH 8.2, 37°C
150
purified native enzyme
151.9
purified recombinant enzyme, pH and temperature not specified in the publication
1547
purified recombinant enzyme, 0°C, pH 7.8
160
Fe2+-bound enzyme, pH not specified in the publication, 37°C
17.3
-
purified extracellular enzyme, pyrogallol autoxidation inhibition assay method
1700
purified recombinant enzyme, pH 7.5, 25°C
17060
pH 7.8, native protein
178.7
recombinant wild-type SOD1, pH not specified in the publication, temperature not specified in the publication
179
-
purified isozyme SODI
1853
purified recombinant enzyme, in presence of Mn2+
1854.79
purified recombinant enzyme, pH and temperature not specified in the publication
1960
purified native enzyme, pH and temperature not specified in the publication
1970
recombinant Mn2+-reconstituted enzyme, pH and temperature not specified in the publication
2.585
-
purified recombinant Mn-reconstituted wild-type SOD, pH 7.8, 25°C
20.1
purified recombinant enzyme, in absence of Mn2+
2170
Thermochaetoides thermophila
purified recombinant enzyme, pH 6.5, 60°C
2200
purified recombinant His-tagged enzyme, pH 6.0, 25°C
228.19
-
purified native enzyme, pH 7.0, 37°C
230
Fe2+-bound enzyme, pH not specified in the publication, 70°C
2324
purified recombinant enzyme
24400
purified recombinant SodB, 4°C, pH 4.0
2524
purified native enzyme, pH 7.0, 25°C
27.12
purified recombinant His-tagged enzyme, pH 7.4, 25°C
27.5
apoenzyme, pH not specified in the publication, 37°C
2700
Mn2+-bound enzyme, pH not specified in the publication, 70°C
27270
pH 7.8, recombinant protein
289
pH 8.0, apoprotein reconstitued in presence of manganese and iron
2940
-
purified Cu,Zn-SOD
31.24
-
mitochondrial Mn-SOD
3538
pH 7.5, 37°C, recombinant enzyme
3788
recombinant SOD1 mutant P143S/P145L, pH not specified in the publication, temperature not specified in the publication
387
-
purified mutant Y41F
39.64
-
cytosolic Cu/Zn-SOD
3980
-
purified mutant H155Q
4.155
-
purified recombinant Mn-reconstituted N-terminal domain mutant SOD, pH 7.8, 25°C
4.3
reconstituted Mn-SOD mutant Y88F
40.21
-
mitochondrial Cu/Zn-SOD
4000
purified native isozyme SODII, pH and temperature not specified in the publication
4200
purified recombinant enzyme, pH and temperature not specified in the publication
421
pH 8.0, recombinant enzyme
434
recombinant Fe2+-reconstituted enzyme, pH and temperature not specified in the publication
480
purified Mn-SOD from peroxisomal membrane
4843
Radix lethospermi
-
-
500
purified native enzyme, pH not specified in the publication, temperature not specified in the publication
533.5
-
purified native enzyme, pH 8.2, 22°C
550
Mn2+-bound enzyme, pH not specified in the publication, 37°C
572
pH 8.0, apoprotein reconstitued in presence of manganese
5780
purified recombinant enzyme
5818
purified recombinant enzyme, pH 7.2, 25°C
615.65
-
purified enzyme, pH and temperature not specified in the publication
623
purified native isozyme SODI, pH and temperature not specified in the publication
63
pH 8.0, apoprotein reconstitued in presence of iron
63.4
purified recombinant His-tagged enzyme, pH 7.5, 25°C
630.61
-
purified enzyme, pH and temperature not specified in the publication
6720
-
purified wild-type enzyme
755
reconstituted Fe-SOD mutant Y88F
7980
-
purified recombinant enzyme
800
-
isoform FeSOD, pH not specified in the publication, temperature not specified in the publication
83.3
-
purified native enzyme, pH 7.2, 37°C
8600
-
isoform MnSOD, pH not specified in the publication, temperature not specified in the publication
9480
-
purified enzyme, pH 8.2, 20°C
996.2
-
purified native enzyme
1204
purified recombinant His-tagged enzyme, pH 7.8, 25°C
1204
purified recombinant His-tagged enzyme, pH 7.8, 25°C
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
overview: superoxide dismutase assays
additional information
-
activities of the native metalloenzyme and isotopically enriched metalloenzyme containing two different metal isotopes, measurement of SOD inhibition of the autoxidation of pyrogallol, method development, overview
additional information
-
activity of native enzyme and modified, fatty acid-conjugated enzyme, overview, coupled assay method using inhibition of the autooxidation of pyrogallol
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
enzyme activity in dogs with unilateral testicular tumor or unilateral cryptorchid testis, and with or without Sertoli cell tumor, seminoma and/or Leydig cell tumor, overview
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
dimeric form shows 65% higher activity than monomeric form
additional information
-
dimeric form shows 65% higher activity than monomeric form
additional information
-
value of SOD activity is 163.4 U/g total protein in wet tissues
additional information
-
Fe-SOD and Mn-SOD activity in Flavobacteria
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
Fe-SOD and Mn-SOD activity in Flavobacteria
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
Fe-SOD and Mn-SOD activity in Flavobacteria
additional information
-
-
additional information
-
activity in egg white and yolk during storage, overveiw
additional information
-
modeling of kinetics
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
Fe-SOD and Mn-SOD activity in Flavobacteria
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
recombinant EC-SOD
additional information
-
overview: superoxide dismutase assays
additional information
-
SOD activity profile after intravenous administration of Cu,Zn-SOD covalently linked to lecithin, measurement of serum and urinary PC-Cu,Zn-SOD concentrations after application of exogenous recombinant human isozyme to male and female humans, overview
additional information
-
-
additional information
Cu/Zn-SOD activity in overexpressing cells from different culture conditions, overview
additional information
-
Cu/Zn-SOD activity in overexpressing cells from different culture conditions, overview
additional information
-
-
additional information
-
-
additional information
-
-
additional information
Megalodesulfovibrio gigas
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
purified native enzyme
additional information
-
Fe-SOD and Mn-SOD activity in Flavobacteria
additional information
-
-
additional information
-
Fe-SOD and Mn-SOD activity in Flavobacteria
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
development of a 96-well-plate mircoassay for enzyme activity
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
Fe-SOD and Mn-SOD activity in Flavobacteria
additional information
-
-
additional information
-
-
additional information
-
-
additional information
specific activity is 14000 U per mg protein and mol Fe, and 10000 U per mg protein and mol Fe in presence of 2-mercaptoethanol. Specific activity shows little variation between 5°C and 25°C
additional information
-
specific activity is 14000 U per mg protein and mol Fe, and 10000 U per mg protein and mol Fe in presence of 2-mercaptoethanol. Specific activity shows little variation between 5°C and 25°C
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
Mn-SOD, native and recombinant wild-type and mutants
additional information
-
yeast Mn-SOD shows high activity compared to other species' enzymes
additional information
-
native and recombinant, wild-type and restored enzyme, with Fe2+ and Mn2+
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
Fe-SOD and Mn-SOD activity in Flavobacteria
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
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-
an ovarian carcinoma cell line
brenda
-
brenda
-
enzyme mRNA is only found in the inner zones of adrenal cortex, not the glomerulosa. Enzyme activity in the inner zone mitochondria is enhaced by corticotrophin and by a low-sodium diet, but suppressed by betamethasone
brenda
-
-
brenda
-
internal mammary arteries
brenda
-
developmental stage of organism
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harbors MnSOD with the ala16val polymorphism
brenda
-
-
brenda
accumulation of sodA mRNA in conidia, semi-quantitative expression analysis
brenda
-
brenda
-
germinated cyst, isoform MnSOD2 and low levels of isoform MnSOD1
brenda
-
very low activity
brenda
-
-
brenda
larval tissue
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
brenda
low expression level
brenda
-
isoform MnSOD1
brenda
-
TCAP-1-responsive, immortalized N38 cells
brenda
-
brenda
low expression level
brenda
-
brenda
-
brenda
-
brenda
-
brenda
-
brenda
larval tissue
brenda
-
-
brenda
-
TCAP-1-responsive hypothalamic cell line
brenda
-
nectarin I
brenda
-
sampled at altitudes of 1420, 1590 and 1920 m a.s.l. almost all superoxide dismutase activity represents Cu/Zn superoxide dismutase, about 4-6% represents Mn superoxide dismutase. In samples from 1590 and 1920 m a.s.l., enzyme activity is lower
brenda
very low expression level
brenda
-
cytoplasmic manganese SOD
brenda
-
brenda
-
-
brenda
-
cytoplasmic manganese SOD
brenda
-
brenda
-
brenda
low expression level
brenda
-
changes in SOD activity in boar sperm during preservation at 16°C, overview
brenda
-
-
brenda
low expression level
brenda
-
brenda
-
developmental stage of organism
brenda
-
-
brenda
-
dogs with unilateral testicular tumor or unilateral cryptorchid testis, and with or without Sertoli cell tumor, seminoma and/or Leydig cell tumor
brenda
-
-
brenda
-
in rats with hepatic necrosis after treatment with tetrachlorcarbon
brenda
-
the splice variant hipI-SODC1b is differentially expressed, being clearly expressed in cambial and xylem, but not phloem, regions
brenda
-
saphenous veins
brenda
-
-
brenda
-
brenda
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
isozyme profile, 4 constitutive isozymes, 3 cold-inducible isozymes, overview. The enzyme activity declines in the beginning of storage, that with cold treatment at 4°C rapidly increases. After 7 days, two Fe-Sod isozymes are still active, while the Mn-SOD are inactivated
brenda
-
-
brenda
-
-
-
brenda
the organism has a very high enzyme content
brenda
propagation of the fungus in the Mus musculus macrophage cell line derived from a reticulum sarcoma, J774.1, ATCC TIB-67, the enzyme expression is upregulated during macrophage infection
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
-
brenda
-
brenda
-
-
-
brenda
-
brenda
-
-
-
brenda
-
-
brenda
-
brenda
-
plasma, isozyme pattern, overview
brenda
-
Cu/Zn-superoxide dismutase isozymes
brenda
-
-
brenda
-
brenda
-
Cu,Zn-SOD
brenda
-
-
-
brenda
-
Cu,Zn-SOD
-
brenda
-
Cu,Zn-SOD
brenda
-
Cu,Zn-SOD
-
brenda
-
isozyme Cu/Zn SOD
brenda
-
-
brenda
-
brenda
-
Cu,Zn-SOD
brenda
-
EC-SOD
brenda
-
-
-
brenda
-
EC-SOD
-
brenda
-
Cu,Zn-SOD
-
brenda
-
EC-SOD
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
brenda
-
-
-
brenda
-
-
brenda
-
immature green fruit
brenda
-
-
brenda
-
-
brenda
-
brenda
-
high expression level
brenda
-
brenda
-
-
brenda
low expression level
brenda
-
brenda
-
cytoplasmic manganese SOD
brenda
-
-
brenda
-
brenda
-
-
brenda
-
Cu,Zn-SOD, in vessels, including endothelium
brenda
-
Mn-SOD, endothelium
brenda
-
Cu,Zn-SOD, in vessels, including endothelium
-
brenda
-
Mn-SOD, endothelium
-
brenda
-
brenda
-
brenda
-
cytoplasmic manganese SOD
brenda
-
brenda
-
brenda
-
Cg-EcSOD-expressing hemocytes were seen in blood circulation, in connective tissues, and closely associated to endothelium blood vessels. Cg-EcSOD presents in its amino acid sequence a LPS-binding motif found in the endotoxin receptor CD14, the protein displays an affinity to Escherichia coli bacteria and to LPS and lipid A
brenda
larval tissue
brenda
low expression rate
brenda
-
brenda
-
cytoplasmic manganese SOD
brenda
-
-
brenda
-
brenda
-
brenda
-
from hepatitis B virus-infected mice
brenda
-
brenda
real time quantitative PCR expression analysis of cytoplasmic Cu,Zn-SOD
brenda
high expression rate
brenda
-
brenda
-
brenda
-
cytoplasmic manganese SOD
brenda
-
brenda
low expression level
brenda
-
brenda
-
cytoplasmic manganese SOD
brenda
-
-
brenda
-
-
-
brenda
fourth-instar larva
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
during the early stretching of soybean leaves, removing cytokines or growth factors can induce Fe-SOD mRNA accumulation. In contrast, Fe-SOD mRNA accumulation is normal during any other stage by removing cytokines or growth factors. Fe-SOD expression is related to whether the development stage is leaf expansion or not
brenda
-
tissue extracts
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
-
-
-
brenda
-
brenda
-
high expression level
brenda
-
highest expression in leaf tissues
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
Cu,Zn-SOD
brenda
-
Cu,Zn-SOD
-
brenda
-
Mn-SOD
brenda
-
Mn-SOD
-
brenda
-
-
brenda
-
Cu,Zn-SOD
brenda
-
Cu,Zn-SOD
-
brenda
-
-
brenda
-
Mn-SOD
brenda
-
-
-
brenda
-
Mn-SOD
-
brenda
-
-
-
brenda
-
Mn-SOD
-
brenda
-
superoxide dismutase activity falls for the first 11 days after infection with smooth type Salmonella typhimurium, coinciding with the period of bacterial growth in the liver. Mild infection with Pseudomonas aeruginosa stimulates superoxide dismutase
brenda
-
brenda
-
-
brenda
-
Cu,Zn-SOD
brenda
-
Mn-SOD
brenda
-
Cu,Zn-SOD
-
brenda
-
-
-
brenda
-
Mn-SOD
-
brenda
-
-
-
brenda
-
-
brenda
-
-
brenda
-
high expression level of EC-SOD
brenda
-
-
-
brenda
-
-
-
brenda
-
high expression level of EC-SOD
brenda
-
-
brenda
-
-
brenda
-
peritoneal macrophages exposed to He-Ne laser radiation. Changes in the activity of superoxide dismutase as well as the formation of nitric oxide and peroxynitrite depend to a large extent on the laser radiation dose. Activation of enzyme at low radiation doses is accompanied by nitric oxide level increase without changes in peroxynitrite. Enhanced laser radiation doses inhibit the enzyme
brenda
-
brenda
-
brenda
-
brenda
-
aortic smooth muscle
brenda
-
-
brenda
-
adductor muscle
brenda
-
brenda
-
cytoplasmic manganese SOD
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-
brenda
submerged cultivation
brenda
-
submerged cultivation
-
brenda
-
-
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
-
isoform MnSOD2
brenda
-
-
brenda
-
-
brenda
semi-quantitative expression analysis, the expression is down regulates in the mycelium phase
brenda
-
brenda
-
-
brenda
of arousing hamster
brenda
-
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
-
-
-
brenda
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
low expression level
brenda
-
-
brenda
Fe-SOD
brenda
-
Fe-SOD
-
brenda
-
Cu,Zn-SOD
brenda
Radix lethospermi
-
-
brenda
-
brenda
-
-
brenda
-
brenda
-
etiolated, Mn-SOD and Cu,Zn-SOD
brenda
-
-
brenda
-
-
brenda
the higher SOD activity in the middle part of the shoots can scavenge the fast-producing reactive oxygen species because it is the most abundant cell-division region
brenda
the higher SOD activity in the middle part of the shoots can scavenge the fast-producing Rreactive oxygen species because it is the most abundant cell-division region
brenda
-
-
brenda
-
-
-
brenda
-
muscle-derived extracellular superoxide dismutase
brenda
-
muscle-derived extracellular superoxide dismutase
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
-
brenda
-
brenda
enzyme overexpression
brenda
-
brenda
additional information
optimal conditions for growth of this organism are 82-92°C, pH 3.0-4.0
brenda
additional information
-
optimal conditions for growth of this organism are 82-92°C, pH 3.0-4.0
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additional information
tissue specific expression of SOD, no activity in gonad and mantle
brenda
additional information
-
tissue specific expression of SOD, no activity in gonad and mantle
brenda
additional information
bamboo SODs show developmental and tissue-specific regulation, unique fast-growth phenotype of green bamboo
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additional information
bamboo SODs show developmental and tissue-specific regulation, unique fast-growth phenotype of green bamboo
brenda
additional information
-
quantitative determination of an isotopically enriched metalloenzyme containing two different metal isotopes, method development, overview
brenda
additional information
-
MnSOD-2 is constitutively expressed, while synthesis of MnSOD-3 is inducible
brenda
additional information
enzyme expression pattern, overview
brenda
additional information
enzyme expression pattern, overview
brenda
additional information
-
enzyme expression pattern, overview
brenda
additional information
MnSOD developmental expression, overview
brenda
additional information
-
MnSOD developmental expression, overview
brenda
additional information
-
MnSOD developmental expression, overview
-
brenda
additional information
-
growth temperature range of the strain OS-77 is between 5°C and 40°C with its optimum growth temperature of 20°C, the growth pH range of the strain OS-77 is between pH 6.0 and pH 10.0 with optimum growth at pH 8.0, strain OS-77 shows salinity tolerance up to 7.5% w/v NaCl solution
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additional information
-
growth temperature range of the strain OS-77 is between 5°C and 40°C with its optimum growth temperature of 20°C, the growth pH range of the strain OS-77 is between pH 6.0 and pH 10.0 with optimum growth at pH 8.0, strain OS-77 shows salinity tolerance up to 7.5% w/v NaCl solution
-
brenda
additional information
-
SOD activity during storage at 4°C for 9 days in egg yolk and egg white, overview, no activity change during 6 days storage but between 6th and 9th day, it decreased significantly in egg yolk while remained low but unchanged in egg white
brenda
additional information
-
measurement of serum and urinary PC-Cu,Zn-SOD concentrations after application of exogenous recombinant human isozyme to male and female humans, overview
brenda
additional information
-
measurement of serum and urinary PC-SOD concentrations after application of exogenous recombinant human isozyme to male and female humans, overview
brenda
additional information
not in venom
brenda
additional information
not in venom
brenda
additional information
-
not in venom
brenda
additional information
real-time PCR enzyme expression analysis
brenda
additional information
-
real-time PCR enzyme expression analysis
brenda
additional information
organs from eight-leaf growth stage, enzyme MgMnSOD1 expression pattern, overview
brenda
additional information
organs from eight-leaf growth stage, enzyme MgMnSOD1 expression pattern, overview
brenda
additional information
organs from eight-leaf growth stage, enzyme MgMnSOD2 expression pattern, overview
brenda
additional information
organs from eight-leaf growth stage, enzyme MgMnSOD2 expression pattern, overview
brenda
additional information
a constitutive mRNA expression of Of-cCu/ZnSOD with higher levels in blood, liver, heart, and brain is observed, no expresion in muscle
brenda
additional information
-
a constitutive mRNA expression of Of-cCu/ZnSOD with higher levels in blood, liver, heart, and brain is observed, no expresion in muscle
brenda
additional information
the enzyme contains no N-terminal signal peptide. Tissue-specific semiquantitative PCR enzyme expression analysis, Pinctada fucata superoxide dismutase mRNA is abundantly expressed in hemocytes and gill and scarcely expressed in other tissues tested
brenda
additional information
-
the enzyme contains no N-terminal signal peptide. Tissue-specific semiquantitative PCR enzyme expression analysis, Pinctada fucata superoxide dismutase mRNA is abundantly expressed in hemocytes and gill and scarcely expressed in other tissues tested
brenda
additional information
-
semi-quantitative enzyme expression analysis in adult tissues shows that the pfSOD mRNA is abundantly expressed in hemocytes and gill and scarcely expressed in other tissues tested
brenda
additional information
-
during different developmental stages of Pleurotus ostreatus, the highest expression levels of the Mn-SOD gene appears in the stage of mature fruit bodies, followed by young fruit bodies and vegetative mycelia. The expression of the Mn-SOD gene is developmentally regulated
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additional information
-
cell growth in the hemolymph of Bombyx mori
brenda
additional information
-
cultivation on bean seeds of Phaseolus vulgaris, root colonization and growth of wild-type and mutant strains, overview
brenda
additional information
gene sodB gene, encoding Fe-SOD, is expressed highly in logarithmic phase cells but is downregulated in stationaryphase cells, except when the medium is amended with FeCl3 suggesting that downregulation of Pseudomonas putida sodB in stationary phase cells is due to Fe2+ depletion in this phase of growth. Removal of Fe2+ by adding a Fe-chelator decreases the sodB transcript level, even in logarithmicphase cells
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additional information
-
overview: content of Cu,Zn-SOD and Mn-SOD in rat tissues
brenda
additional information
-
the enzyme is secreted by many cellular lines and it is also released trough a calcium-dependent depolarization mechanism involving SNARE protein SNAP 25
brenda
additional information
-
overview: content of Cu,Zn-SOD and Mn-SOD in rat tissues
-
brenda
additional information
-
overview: content of Cu,Zn-SOD and Mn-SOD in rat tissues
-
brenda
additional information
the Fe-SOD gene is expressed at low levels in Rhodobacter capsulatus cells grown under anaerobic or semiaerobic conditions, but expression is strongly induced upon exposure of the bacteria to air
brenda
additional information
Sulfolobus solfataricus grows between 50°C and 87°C with an optimum growing temperature of 87°C, but it neither grows nor survives at 90°C
brenda
additional information
-
Sulfolobus solfataricus grows between 50°C and 87°C with an optimum growing temperature of 87°C, but it neither grows nor survives at 90°C
brenda
additional information
-
quantitative real-time PCR enzyme expresion analysis
brenda
additional information
enzyme expression pattern analysis
brenda
additional information
-
enzyme expression pattern analysis
brenda
additional information
-
quantitative real-time PCR enzyme tissue expression analysis
brenda
additional information
constant expression in plerocercoid larvae and adult worms
brenda
additional information
-
constant expression in plerocercoid larvae and adult worms
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additional information
the enzyme expression is upregulated in the yeast phase
brenda
additional information
-
the enzyme expression is upregulated in the yeast phase
brenda
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evolution
Leptopilina SOD3 clusters with predicted extracellular insect Cu,Zn-SODs, phylogenetic analysis
evolution
Leptopilina SOD3 clusters with predicted extracellular insect Cu,Zn-superoxide dismutases, phylogenetic analysis
evolution
Leptopilina SOD3 clusters with predicted extracellular insect Cu,Zn-superoxide dismutases, phylogenetic analysis
evolution
two Cu/Zn superoxide dismutase family signature sequences exist in the deduced amino acid sequence of the superoxide dismutase: signature 1 consensus sequences [GA]-[IMFAT]-H-[LIVF]-H-{S}-x-[GP]-[SDG]-x-[STAGDE], and signature 2 consensus sequences G-[GNHD]-[SGA]-[GR]-x-R-x-[SGAWRV]-C-x(2)-[IV]
evolution
-
phylogenetic analysis clusters cMn-SODs and mitochondrial Mn-SODs in two separate groups
evolution
sequence analysis and expression patterns of MgMnSOD1 and MgMnSOD2 suggest that they are orthologous genes which are inherited from the two parents, Miscanthus sacchariflora and Miscanthus sinensis, respectively
evolution
the N-terminal amino acid sequence of Cu/Zn-SODII reveals a high degree of structural homology with Cu/Zn-SOD from other fungi, including Aspergillus species
evolution
-
the two different allelic forms of a Mn-SOD involved in ROS detoxification, ApMn-SOD1 and ApMn-SOD2, differ only by two substitutions, M110L and A138G, identified in an Alvinella pompejana cDNA library
evolution
-
the two different allelic forms of a Mn-SOD involved in ROS detoxification, ApMn-SOD1 and ApMn-SOD2, differ only by two substitutions, M110L and A138G, identified in an Alvinella pompejana cDNA library. ApMn-SOD2 is rare (2%) and only found in the heterozygous state
evolution
while invertebrate Cu/ZnSOD members mainly demonstrate a tetraexonic structure, the vertebrate members have acquired an additional intron in the third exon resulting in a quinquepartite arrangement with class-specific exon lengths. Although, teleost Cu/ZnSOD members resemble the mammalian orthologues in their genomic organization, they share a proximal position with molluscan members in the phylogeny
evolution
-
the N-terminal amino acid sequence of Cu/Zn-SODII reveals a high degree of structural homology with Cu/Zn-SOD from other fungi, including Aspergillus species
-
malfunction
MnSOD ala16val polymorphism is associated with various diseases including breast cancer
malfunction
-
enhanced EcSOD expression in skeletal muscle inhibits endothelial activation, EcSOD is sufficient to inhibit endothelial activation in vitro and in vivo
malfunction
-
mutation of Cu,Zn-superoxide dismutase (SOD1) is responsible for genetically linked autosomal dominant neurodegenerative disease, amyotrophic lateral sclerosis (ALS) in humans
malfunction
-
pyrazolone derivatives are inhibitors of Cu/Zn superoxide dismutase 1 (SOD1)-dependent protein aggregation
malfunction
Role of nitric oxide (NO) modified erythrocytes superoxide dismutase (eSOD) in alopecia areata, a non-scarring hair loss disorder. dysfunctioning of SODis reported in patients with alopecia areata. Protein-A purified IgG of alopecia areata patients (AA-IgG) show strong binding to NO-eSOD in comparison with IgG from controls. In addition, AA-IgG from patients with alopecia universalis recognize NO-eSOD in a greater extentas compared to AA-IgG from patients with patchy persistent alopecia areata. Alopecia universalis patients' sera contain higher levels of NO or carbonyl contents and lower levels of SOD activity compared with patchy persistent alopecia areata patient or control sera
malfunction
-
enhanced EcSOD expression in skeletal muscle inhibits endothelial activation, EcSOD is sufficient to inhibit endothelial activation in vitro and in vivo
-
physiological function
SOD detoxifies the highly reactive superoxide anions to hydrogen peroxide and molecular oxygen
physiological function
-
the exogenous manganese superoxide dismutase is able to modify the intracellular level of reactive oxygen species by eliminating superoxide anion and producing hydrogen peroxide. The cell viability of the two tumoral cell lines, porcine aortic endothelial cells and B16F0 mouse melanoma cells, exposed to the enzyme, is not significantly affected but the cell multiplication is arrested. The enzyme is involved in the control of several biological processes including cell proliferation
physiological function
different SOD isozymes might play different roles in the developmental and tissue-specific regulation, the higher SOD activity in the middle part of the shoots can scavenge the fast-producing reactive oxygen species because it is the most abundant cell-division region
physiological function
different SOD isozymes might play different roles in these developmental, the higher SOD activity in the middle part of the shoots can scavenge the fast-producing reactive oxygen species because it is the most abundant cell-division region
physiological function
-
expression and activity of the mitochondrial P450 system along with substrate availability may contribute to mitochondrial function regulation via activation of IMS SOD1. Activation of intermembrane space SOD1 after incubation of rat liver intact mitochondria with P450 substrates significantly prevents the loss of aconitase activity in the mitochondrial matrix, general mechanism for the SOD1 activation mediated by P450 enzymes, overview
physiological function
-
manganese superoxide dismutase enzymes catalyze superoxide disproportionation by a mechanism that is more complex than those of the other SOD types. In particular the reduction of superoxide can proceed via one of two pathways. One pathway dominates when the O2- concentration is low relative to the enzyme concentration, and the other pathway dominates when the ratio [O2-]/[MnSOD] is high, overview
physiological function
-
protection by recombinant Cp-icCuZnSOD against alcohol-injury in human hepatocyte L02 cell line
physiological function
superoxide dismutases play a protective role against oxidative stress by catalyzing disproportionation of the superoxide anion radical to hydrogen peroxide and dioxygen
physiological function
the enzyme may play essential roles for survival of the parasite not only by protecting itself from endogenous oxidative stress, but also by detoxifying oxidative killing of the parasite by host immune effector cells
physiological function
detoxification of superoxide
physiological function
PgCuZnSOD plays a functional role in conferring oxidative stress tolerance to prokaryotic system
physiological function
-
purified SOD from the root of Stemona tuberosa shows biological activity on in vitro cell proliferation of skin fibroblast cells from humans
physiological function
superoxide dismutases are considered key enzymes in the control of oxidative stress because they can protect oxygen-metabolizing cells against the harmful effects of superoxide free radicals
physiological function
-
the enzyme may play an important role as an antioxidant in a wide temperature range
physiological function
the enzyme may play an important role in the innate immune system of hard clam
physiological function
-
EcSOD inhibits vascular cell adhesion molecule 1 expression and inflammatory leukocyte adhesion to the vascular wall of vital organs, blocking an early step of the pathology in organ damage under endotoxemia. Enhanced expression of EcSOD in skeletal muscle profoundly protects against Multiple organ dysfunction syndrome (MODS) by inhibiting endothelial activation and inflammatory cell adhesion, which might be a promising therapy for MODS
physiological function
enzyme RmFeSOD plays an important role in the adaptability of heavy metals
physiological function
manganese superoxide dismutase (MnSOD) is an important antioxidant enzyme involved in stress tolerance and able to protect plant cells from accumulated reactive oxygen species by converting superoxide to peroxide and oxygen
physiological function
manganese superoxide dismutase (MnSOD) is an important antioxidant enzyme involved in stress tolerance and able to protect plant cells from accumulated reactive oxygen species by converting superoxide to peroxide and oxygen. Enzyme MgMnSOD1 is predicted to be targeted to mitochondria and involved in removing the superoxide radical generated by respiration
physiological function
superoxide dismutase (SOD) is a prime antioxidant enzymethat destroys the effects of superoxide, thus limiting the dele-terious effects of reactive oxygen and nitrogen species. SOD is considered an important regulator of oxida-tive/nitrosative stress
physiological function
-
superoxide dismutase (SOD) is an enzyme that protects against oxidative stress from superoxide radicals in living cells
physiological function
-
superoxide dismutase is an antioxidant enzyme that plays an important role in the removal of harmful superoxide radicals, which are generated by metabolic processes in oxygen-utilizing organisms. Biological activity of purified SOD from the root of Stemona tuberosa on in vitro cell proliferation of skin fibroblast cells from human
physiological function
superoxide dismutases (SODs) are key enzymes functioning as the first line of antioxidant defense by virtue of the ability to convert highly reactive superoxide radicals to hydrogen peroxide and molecular oxygen
physiological function
superoxide dismutases (SODs) are key enzymes functioning as the first line of antioxidant defense by virtue of the ability to convert highly reactive superoxide radicals to hydrogen peroxide and molecular oxygen
physiological function
-
superoxide dismutases (SODs) are key enzymes functioning as the first line of antioxidant defense by virtue of the ability to convert highly reactive superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a central role in protecting plants against the toxic effects of reactive oxygen species generated during normal cellular metabolic activity or as a result of various environmental stresses, regulation mechanisms and functional role(s) during development and in response to biotic or abiotic stresses, overview. During the early stretching of soybean leaves, removing cytokines or growth factors can induce Fe-SOD mRNA accumulation in contrast, Fe-SOD mRNA accumulation is normal during any other stage by removing cytokines or growth factors. Fe-SOD expression is related to whether the development stage is leaf expansion or not
physiological function
-
superoxide dismutases (SODs) are key enzymes functioning as the first line of antioxidant defense by virtue of the ability to convert highly reactive superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a central role in protecting plants against the toxic effects of reactive oxygen species generated during normal cellular metabolic activity or as a result of various environmental stresses, regulation mechanisms and functional role(s) during development and in response to biotic or abiotic stresses, overview. The effect of a particular stress on SOD gene expression is likely governed by the subcellular sites at which oxidative stress is generated
physiological function
-
superoxide dismutases (SODs) are key enzymes functioning as the first line of antioxidant defense by virtue of the ability to convert highly reactive superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a central role in protecting plants against the toxic effects of reactive oxygen species generated during normal cellular metabolic activity or as a result of various environmental stresses, regulation mechanisms and functional role(s) during development and in response to biotic or abiotic stresses, overview. The effect of a particular stress on SOD gene expression is likely governed by the subcellular sites at which oxidative stress is generated
physiological function
-
superoxide dismutases (SODs) are key enzymes functioning as the first line of antioxidant defense by virtue of the ability to convert highly reactive superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a central role in protecting plants against the toxic effects of reactive oxygen species generated during normal cellular metabolic activity or as a result of various environmental stresses, regulation mechanisms and functional role(s) during development and in response to biotic or abiotic stresses, overview. The effect of a particular stress on SOD gene expression is likely governed by the subcellular sites at which oxidative stress is generated
physiological function
superoxide dismutases (SODs) are key enzymes functioning as the first line of antioxidant defense by virtue of the ability to convert highly reactive superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a central role in protecting plants against the toxic effects of reactive oxygen species generated during normal cellular metabolic activity or as a result of various environmental stresses, regulation mechanisms and functional role(s) during development and in response to biotic or abiotic stresses, overview. The effect of a particular stress on SOD gene expression is likely governed by the subcellular sites at which oxidative stress is generated
physiological function
superoxide dismutases (SODs) are key enzymes functioning as the first line of antioxidant defense by virtue of the ability to convert highly reactive superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a central role in protecting plants against the toxic effects of reactive oxygen species generated during normal cellular metabolic activity or as a result of various environmental stresses, regulation mechanisms and functional role(s) during development and in response to biotic or abiotic stresses, overview. The effect of a particular stress on SOD gene expression is likely governed by the subcellular sites at which oxidative stress is generated
physiological function
-
superoxide dismutases (SODs) are key enzymes functioning as the first line of antioxidant defense by virtue of the ability to convert highly reactive superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a central role in protecting plants against the toxic effects of reactive oxygen species generated during normal cellular metabolic activity or as a result of various environmental stresses, regulation mechanisms and functional role(s) during development and in response to biotic or abiotic stresses, overview. The effect of a particular stress on SOD gene expression is likely governed by the subcellular sites at which oxidative stress is generated
physiological function
-
superoxide dismutases (SODs) are key enzymes functioning as the first line of antioxidant defense by virtue of the ability to convert highly reactive superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a central role in protecting plants against the toxic effects of reactive oxygen species generated during normal cellular metabolic activity or as a result of various environmental stresses, regulation mechanisms and functional role(s) during development and in response to biotic or abiotic stresses, overview. The effect of a particular stress on SOD gene expression is likely governed by the subcellular sites at which oxidative stress is generated
physiological function
superoxide dismutases (SODs) are key enzymes functioning as the first line of antioxidant defense by virtue of the ability to convert highly reactive superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a central role in protecting plants against the toxic effects of reactive oxygen species generated during normal cellular metabolic activity or as a result of various environmental stresses, regulation mechanisms and functional role(s) during development and in response to biotic or abiotic stresses, overview. The effect of a particular stress on SOD gene expression is likely governed by the subcellular sites at which oxidative stress is generated. Chloroplastic Fe-SOD responds to increased oxy-radical formation in chloroplasts
physiological function
superoxide dismutases (SODs) are key enzymes functioning as the first line of antioxidant defense by virtue of the ability to convert highly reactive superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a central role in protecting plants against the toxic effects of reactive oxygen species generated during normal cellular metabolic activity or as a result of various environmental stresses, regulation mechanisms and functional role(s) during development and in response to biotic or abiotic stresses, overview. The effect of a particular stress on SOD gene expression is likely governed by the subcellular sites at which oxidative stress is generated. Cytosolic Cu/Zn-SOD responds to increased oxy-radical formation in the cytosol
physiological function
superoxide dismutases (SODs) are key enzymes functioning as the first line of antioxidant defense by virtue of the ability to convert highly reactive superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a central role in protecting plants against the toxic effects of reactive oxygen species generated during normal cellular metabolic activity or as a result of various environmental stresses, regulation mechanisms and functional role(s) during development and in response to biotic or abiotic stresses, overview. The effect of a particular stress on SOD gene expression is likely governed by the subcellular sites at which oxidative stress is generated. Mitochondrial Mn-SOD responds to increased oxy-radical formation in mitochondria. Posttranscriptional regulation of SODs, overview
physiological function
superoxide dismutases (SODs) are key enzymes functioning as the first line of antioxidant defense by virtue of the ability to convert highly reactive superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a central role in protecting plants against the toxic effects of reactive oxygen species generated during normal cellular metabolic activity or as a result of various environmental stresses, regulation mechanisms and functional role(s) during development and in response to biotic or abiotic stresses, overview. The effect of a particular stress on SOD gene expression is likely governed by the subcellular sites at which oxidative stress is generated. Molecular mechanisms of GTACT motif-dependent transcriptional suppression by Cu2+ are conserved in land plants
physiological function
-
superoxide dismutases (SODs) are key enzymes functioning as the first line of antioxidant defense by virtue of the ability to convert highly reactive superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a central role in protecting plants against the toxic effects of reactive oxygen species generated during normal cellular metabolic activity or as a result of various environmental stresses, regulation mechanisms and functional role(s) during development and in response to biotic or abiotic stresses, overview. The expression of the Mn-SOD gene is developmentally regulated
physiological function
-
superoxide dismutases (SODs) are key enzymes functioning as the first line of antioxidant defense by virtue of the ability to convert highly reactive superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a central role in protecting plants against the toxic effects of reactive oxygen species generated during normal cellular metabolic activity or as a result of various environmental stresses, regulation mechanisms and functional role(s) during development and in response to biotic or abiotic stresses, overview. The expression of the Mn-SOD gene is developmentally regulated
physiological function
superoxide dismutases (SODs) are key enzymes functioning as the first line of antioxidant defense by virtue of the ability to convert highly reactive superoxide radicals to hydrogen peroxide and molecular oxygen. The expression of the SOD genes from animals is related to hormone levels and cytokines in the body. A study suggested that removal of estradiol by ovariectomy decreases the activity of Cu/Zn-SOD and Mn-SOD in the intra-abdominal tissue of female rats compared with rats treated with ovariectomy but with added estradiol. In addition, a variety of cytokines such as growth factor, tumor necrosis factor, and interleukin regulate response to oxidative stress via regulation of SOD expression
physiological function
superoxide dismutases (SODs) are key enzymes functioning as the first line of antioxidant defense by virtue of the ability to convert highly reactive superoxide radicals to hydrogen peroxide and molecular oxygen. The expression of the SOD genes from animals is related to hormone levels and cytokines in the body. A study suggested that removal of estradiol by ovariectomy decreases the activity of Cu/Zn-SOD and Mn-SOD in the intra-abdominal tissue of female rats compared with rats treated with ovariectomy but with added estradiol. In addition, a variety of cytokines such as growthfactor, tumor necrosis factor, and interleukin regulate response to oxidative stress via regulation of SOD expression
physiological function
-
superoxide dismutases protect against oxidative stress by disproportionation of the superoxide anion radical to hydrogen peroxide and dioxygen through a redox cycle of metal ions
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
physiological function
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
physiological function
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
physiological function
Photobacterium sepia
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes. An increase in the Fe-SOD content, particularly evident in scum samples that are continuously exposed to high irradiances, may have a role in the photo adaptation of diazotrophic cyanobacteria and help to protect them from light injury in the Baltic Sea
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes. ElSOD is a cold-adapted SOD, which shows its potential valuein antioxidant utilization
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes. The enzyme of Tetraselmis gracilis is important to prevent oxidative stress such as nutrient and light availability
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes. The enzyme plays an important role in preventing oxidative stress triggered by a number of factors that affect growth, such as nutrient and light availability
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes. The organism is exposed to various challenging conditions (e.g. high temperature, hypoxia and the presence of sulphides, heavy metals and radiations), which increase the production of dangerous reactive oxygen species (ROS). Two different allelic forms of a Mn-SOD involved in reactive oxygen species detoxification, ApMn-SOD1 and ApMn-SOD2
physiological function
-
the bacterial manganese superoxide dismutase (MnSOD) localizes to the chromosomal portion of the cell and impart protection from ionizing radiation to DNA. MnSOD can bind to RNA leads to the possibility that MnSOD may confer protection to RNA, as well
physiological function
-
the enhanced activity of the SOD dimer in betel nut oral extract is responsible for the continuous production of hydrogen peroxide in the oral cavity. SOD may contribute to oral carcinogenesis through the continuous formation of hydrogen peroxide in the oral cavity, in spite of its protective role against cancer in vivo
physiological function
the enzyme plays an important role in protecting some tissues from reactive oxygen intermediates produced during challenge from Spiroplasma eriocheiris and Aeromonas hydrophila
physiological function
the enzyme shws antioxidant action
physiological function
the major isoenzyme is Cu/Zn-SODII, the minor Cu/Zn-SODI
physiological function
the ZnSOD is a potentially important virulence factor
physiological function
-
superoxide dismutases are considered key enzymes in the control of oxidative stress because they can protect oxygen-metabolizing cells against the harmful effects of superoxide free radicals
-
physiological function
-
the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes
-
physiological function
-
enzyme RmFeSOD plays an important role in the adaptability of heavy metals
-
physiological function
-
the enzyme may play an important role as an antioxidant in a wide temperature range
-
physiological function
-
the major isoenzyme is Cu/Zn-SODII, the minor Cu/Zn-SODI
-
physiological function
-
expression and activity of the mitochondrial P450 system along with substrate availability may contribute to mitochondrial function regulation via activation of IMS SOD1. Activation of intermembrane space SOD1 after incubation of rat liver intact mitochondria with P450 substrates significantly prevents the loss of aconitase activity in the mitochondrial matrix, general mechanism for the SOD1 activation mediated by P450 enzymes, overview
-
physiological function
-
EcSOD inhibits vascular cell adhesion molecule 1 expression and inflammatory leukocyte adhesion to the vascular wall of vital organs, blocking an early step of the pathology in organ damage under endotoxemia. Enhanced expression of EcSOD in skeletal muscle profoundly protects against Multiple organ dysfunction syndrome (MODS) by inhibiting endothelial activation and inflammatory cell adhesion, which might be a promising therapy for MODS
-
additional information
-
CpSOD contains an intracellular disulfide bond and two CuZnSOD family signatures
additional information
-
different values of the Mn/Fe ratio in the active site prove that the type of metal is crucial for the regulation of the activity of recombinant SmSOD, cambialistic nature of SmSOD, overview
additional information
-
the chimeric protein MnSOD-VHb is a dimer, in which the two subunits are associated via interaction between the SOD portions, since MnSOD monomers show a 40fold reduction in activity, but our chimeric MnSOD-VHb retained 84% activity compared to native MnSOD
additional information
-
active site Cys. Infection with pathogen Puccinia striiformis f.sp. tritici alters the kinetic properties of the cell wall enzyme
additional information
Geobacillus sp. EPT3 SOD contains the LPPLPYRYDALEP sequence, which is identical to the conserved amino acid sequence (LPXLPYXXXXLEP) found at the N-terminal region of many Mn-SODs
additional information
MnSOD47 contains the decapod crustacean signature (DXWEHXXY), which is a specific characteristic of Mn-superoxide dismutase
additional information
-
MnSOD47 contains the decapod crustacean signature (DXWEHXXY), which is a specific characteristic of Mn-superoxide dismutase
additional information
-
molecular metal specificity mechanism of th enzyme, overview
additional information
-
no evidence for the presence of either iron or copper/zinc SODs in Phytophthora cinnamomi
additional information
overexpression of PgCuZnSOD confers comparatively enhanced tolerance to methyl viologen induced oxidative stress in bacteria. Homology structure modeling of PgCuZnSOD, overview
additional information
-
overexpression of PgCuZnSOD confers comparatively enhanced tolerance to methyl viologen induced oxidative stress in bacteria. Homology structure modeling of PgCuZnSOD, overview
additional information
-
residues involved in the active site are H28, Y36, H82, Q149, D164, and H168, which are completely conserved in the EgMnSOD
additional information
secondary structure analysis using circular dichroism, overview
additional information
secondary structure analysis using circular dichroism, overview
additional information
secondary structure analysis using circular dichroism, overview
additional information
-
secondary structure analysis using circular dichroism, overview
additional information
Thermochaetoides thermophila
structure analysis by molecular replacement using human mitochondrial MnSOD variant, PDB ID 1var, modelling
additional information
the amount of enzyme required to inhibit 50% of pyrogallol autoxidation is 0.41, 0.56 and 13.73 mg at 65°C, 70°C, and 80°C, respectively
additional information
-
the amount of enzyme required to inhibit 50% of pyrogallol autoxidation is 0.41, 0.56 and 13.73 mg at 65°C, 70°C, and 80°C, respectively
additional information
the enzyme sequence contains an intracellular disulfide bond and two Cu/Zn-superoxide dismutase signatures
additional information
-
the enzyme sequence contains an intracellular disulfide bond and two Cu/Zn-superoxide dismutase signatures
additional information
three-dimensional structure modelling, overview. The active site is surrounded by aromatic amino acid residues Trp131, Trp84, Phe168, Tyr139, and Tyr83 and is localized near the potential contact of monomers in the dimer
additional information
-
three-dimensional structure modelling, overview. The active site is surrounded by aromatic amino acid residues Trp131, Trp84, Phe168, Tyr139, and Tyr83 and is localized near the potential contact of monomers in the dimer
additional information
structure homology modeling
additional information
-
structure homology modeling
additional information
-
blue mussels from chemically contaminated area in Le Havre harbor exhibited a third Cu/Zn-SOD isoform characterized by a more acidic isoelectric point (pI 4.55) and a native apparent molecular mass of 130 kDa. When maintained in clean marine water, mussels from this area showed a transitory decrease in total SOD activity accompanied by the disappearance of the SOD-3 band
additional information
circular dichroism spectral analysis of the enzyme's secondary structure
additional information
-
circular dichroism spectral analysis of the enzyme's secondary structure
additional information
-
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
-
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
-
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
-
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
-
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
-
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
-
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
-
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
-
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
-
ElSOD as a cold-adapted enzyme
additional information
enzyme tertiary structural modeling
additional information
-
enzyme tertiary structural modeling
additional information
-
histidine and tryptophan residues are involved in the catalytic activity
additional information
histidine and tryptophan residues are involved in the catalytic activity
additional information
NO-induced damage in eSOD causes alteration in hydrophobic or aromatic amino acids and protein carbonyl contents
additional information
-
NO-induced damage in eSOD causes alteration in hydrophobic or aromatic amino acids and protein carbonyl contents
additional information
-
SOD saves catechols from autoxidation and extends their bioavailability
additional information
structure models of three mutants His29Ala, His84Ala, and His171Ala, overview
additional information
the conserved histidine residues (His41, His89, His179), aspartate residue (Asp175), and WEHAYY domain play an important role in the active site of the Fe-binding sites
additional information
-
the conserved histidine residues (His41, His89, His179), aspartate residue (Asp175), and WEHAYY domain play an important role in the active site of the Fe-binding sites
additional information
the putative binding position of superoxide is determined from the crystal structure of the enzyme in complex with azide, providing a model for binding to the active site. Facilitation of the anionic ligand to the active site pit via a valley of positively-charged surface patches. Surrounding ridges of negative charge help guide the superoxide anion. Within the active site pit, Arg173 and Glu162 further guide and align superoxide for efficient catalysis. Superoxide coordination at the sixth position causes the electrostatic surface of the active site pit to become nearly neutral. Generation of a model for electrostatic-mediated diffusion, and efficient binding of superoxide for catalysis. The active site manganese ion is coordinated by His26, His74, Asp159, His163, and a single oxygen, typically thought to be a water or hydroxide ion. These ligands are referred to as the inner-sphere residues. Outer-sphereresidues surround the inner-sphere and include His30, Tyr34, Phe77, Trp78, Trp123, Gln143, Trp161 and, from across the dimer interface, Glu162. Distorted five-coordinate trigonal bipyramidal active site geometry of native human MnSOD, overview
additional information
-
the putative binding position of superoxide is determined from the crystal structure of the enzyme in complex with azide, providing a model for binding to the active site. Facilitation of the anionic ligand to the active site pit via a valley of positively-charged surface patches. Surrounding ridges of negative charge help guide the superoxide anion. Within the active site pit, Arg173 and Glu162 further guide and align superoxide for efficient catalysis. Superoxide coordination at the sixth position causes the electrostatic surface of the active site pit to become nearly neutral. Generation of a model for electrostatic-mediated diffusion, and efficient binding of superoxide for catalysis. The active site manganese ion is coordinated by His26, His74, Asp159, His163, and a single oxygen, typically thought to be a water or hydroxide ion. These ligands are referred to as the inner-sphere residues. Outer-sphereresidues surround the inner-sphere and include His30, Tyr34, Phe77, Trp78, Trp123, Gln143, Trp161 and, from across the dimer interface, Glu162. Distorted five-coordinate trigonal bipyramidal active site geometry of native human MnSOD, overview
additional information
-
tryptic peptide mapping
additional information
-
MnSOD47 contains the decapod crustacean signature (DXWEHXXY), which is a specific characteristic of Mn-superoxide dismutase
-
additional information
-
the conserved histidine residues (His41, His89, His179), aspartate residue (Asp175), and WEHAYY domain play an important role in the active site of the Fe-binding sites
-
additional information
-
secondary structure analysis using circular dichroism, overview
-
additional information
-
the amount of enzyme required to inhibit 50% of pyrogallol autoxidation is 0.41, 0.56 and 13.73 mg at 65°C, 70°C, and 80°C, respectively
-
additional information
-
residues involved in the active site are H28, Y36, H82, Q149, D164, and H168, which are completely conserved in the EgMnSOD
-
additional information
-
different values of the Mn/Fe ratio in the active site prove that the type of metal is crucial for the regulation of the activity of recombinant SmSOD, cambialistic nature of SmSOD, overview
-
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106000
x * 106000, or x * 97000, SDS-PAGE, differently glycosylated protein forms
108000
peroxisomal Mn-SOD, gel filtration
112000
mitochondrial Mn-SOD, gel filtration
123000
-
Cu,Zn-SOD, gel filtration
14000
-
4 * 14000, SDS-PAGE
14500
-
2 * 14500, SOD-1, SDS-PAGE
15100
-
2 * 15100, isoenzyme II, SDS-PAGE
15132
-
x * 15132, sequence calculation
15500
x * 15500, calculated, x * 16000, SDS-PAGE
15700
x * 15700, about, cytoplasmic CuZn-SOD, sequence calculation
15704
x * 17000, SDS-PAGE, x * 15704, MALDI-TOF
15821
-
2 * 15821, Cu,Zn-SOD, sequence calculation
15832
x * 15832, sequence calculation
15841
-
x * 15841, sequence calculation
15882
x * 15882, Cu/Zn-SOD sequence calculation
15900
-
2 * 15900, SOD-4, SDS-PAGE
15912
-
2 * 15912, mass spectrometry
15960
2 * 15960, sequence calculation, 2 * 17000, recombinant enzyme, SDS-PAGE
16300
-
2 * 16300, SDS-PAGE
16385
1 * 16385, sequence calculation, 1 * 16400, about, recombinant His6-and thioredoxin-tagged enzyme, mass spectrometry and SDS-PAGE
165000
-
nectarin I: Mn-SOD, native PAGE
17500
-
2 * 17500, Cu,Zn-SOD
175000
-
x * 175000, Cu,Zn-SOD, SDS-PAGE
17600
-
x * 17600 + x * 31500, SDS-PAGE
17700
Thermochaetoides thermophila
x * 17700, recombinant enzyme, SDS-PAGE
17900
2 * 17900, SDS-PAGE
18100
-
2 * 18100, Fe-SOD, SDS-PAGE
18200
-
2 * 18200, SDS-PAGE
18400
-
x * 18400, SDS-PAGE
185000
-
x * 185000, Cu,Zn-SOD, SDS-PAGE
186000
Megalodesulfovibrio gigas
-
Fe-SOD, gel filtration
19000
-
2 * 19000, SDS-PAGE
19250
-
x * 19250, Cu,Zn-SOD, SDS-PAGE
20400
-
2 * 20400, SOD-3, SDS-PAGE
21192
-
4 * 21192, MALDI-TOF, 4 * 23000, SDS-PAGE
21251
2 * 21251, mass spectrometry, 2 * 22000, SDS-PAGE
21300
-
4 * 21300, SDS-PAGE
21600
-
2 * 21600, SDS-PAGE after denaturation in boiling SDS
22321
-
4 * 22321, MALDI-TOF, 4 * 24000-25000, SDS-PAGE in absence, 4 * 25000, in presence of 2-mercaptoethanol
22340
-
4 * 22340, Mn-SOD, sequence calculation
22500
-
2 * 22500, Fe-SOD, SDS-PAGE
22532
-
2 * 23500, SDS-PAGE, 2 * 22532, sequence calculation
22650
x * 22650, sequence calculation
22900
-
2 * 22900, Mn-SOD
22930
2 * 23000, SDS-PAGE, 2 * 22930, sequence calculation
22931
x * 22931, Fe-SOD, amino acid sequence determination
23100
-
2 * 23100, SDS-PAGE
23600
-
2 * 23600, about, recombinant enzyme, sequence calcualtion, 2 * 25000, recombinant enzyme, SDS-PAGE
23652
2 * 23652, SOD1, sequence calculation
23954
4 * 23954, sequence calculation
240000 - 260000
gel filtration
24096
-
4 * 24096, amino acid sequence determination
24140
-
x * 24140, mass spectrometry
24204
4 * 24204, calculated from sequence
24225
x * 24225, calculated, x * 24000, SDS-PAGE
24228
x * 24228, calculated from sequence
24600
2 * 24600, calculated from sequence
24989
x * 24989, sequence calculation, MnSOD
26873
x * 26873, calculated
27400
2 * 27400, claculated, 2 * 29700, SDS-PAGE
28500
recombinant His-tagged enzyme, gel filtration
29700
2 * 27400, claculated, 2 * 29700, SDS-PAGE
30800 - 31600
-
mitochondrial cyanide-sensitive enzyme, gel filtration, sedimentation equilibrium analysis
31000 - 31500
-
gel filtration
31000 - 32200
-
gel filtration, sedimentation equilibrium analysis
31079
-
2 * 31079, sequence calculation
31500
-
x * 17600 + x * 31500, SDS-PAGE
32400
-
Cu,Zn-SOD, gel filtration
32700
-
Cu,Zn-SOD, sedimentation equilibrium analysis
34000
recombinant enzyme, native PAGE and gel filtration
34034
-
2 * 34034, sequence calculation and mass spectrometry
34589
2 * 34589, sequence calculation, 2 * 35000, recombinant His-tagged enzyme, SDS-PAGE, 2 * 34652, recombinant His-tagged enzyme, mass spectrometry, 2 * 53000, recombinant thioredoxin-fusion enzyme, SDS-PAGE
34652
2 * 34589, sequence calculation, 2 * 35000, recombinant His-tagged enzyme, SDS-PAGE, 2 * 34652, recombinant His-tagged enzyme, mass spectrometry, 2 * 53000, recombinant thioredoxin-fusion enzyme, SDS-PAGE
36000 - 38000
recombinant His-tagged enzyme, gel filtration
36031
x * 36031, calculated
36500
-
Fe-SOD, sedimentation equilibrium
38000
-
2 * 38000, recombinant chimera MnSOD-VHb, SDS-PAGE
39000
-
isoenzyme 3, gel filtration
40250
-
superoxide dismutase I, sedimentation equilibrium analysis
41000
-
Fe-SOD, gel filtration
41000 - 43000
-
gel filtration, sedimentation equilibrium
41400
-
sedimentation equilibrium analysis
42500
-
Mn-SOD, gel filtration
49300
recombinant His-tagged enzyme, gel filtration
50230
2 * 59000, SDS-PAGE, 2 * 50230, sequence calculation
53000
2 * 34589, sequence calculation, 2 * 35000, recombinant His-tagged enzyme, SDS-PAGE, 2 * 34652, recombinant His-tagged enzyme, mass spectrometry, 2 * 53000, recombinant thioredoxin-fusion enzyme, SDS-PAGE
55000
-
Cu,Zn-SOD, gel filtration
57000
in solution, gel filtration
62160
-
sequence calculation
66000
-
PAGE, isozyme SODI
68500
-
Cu,Zn-SOD, gel filtration
69130
recombinant His-tagged enzyme, mass spectrometry
73000
-
Mn-SOD, gel filtration
76000
-
recombinant chimera MnSOD-VHb, gel filtration
82000 - 84000
-
Mn-SOD, gel filtration, sedimentation equilibrium
87000
tetrameric form, gel filtration
89000
-
sedimentation equilibrium analysis
90000
-
SOD-III, gel filtration
92000
-
Mn-SOD, gel filtration
93000 - 95000
-
gel filtration, PAGE
94000
-
Mn-SOD, gel filtration
94400
Thermochaetoides thermophila
-
gel filtration
97000
x * 106000, or x * 97000, SDS-PAGE, differently glycosylated protein forms
98500
recombinant enzyme, sedimentation velocity analysis
100000
-
-
100000
-
analytical ultracentrifugation
130000
-
PAGE, isoform with pI 4.55
130000
-
isozyme 3, native PAGE
130700
recombinant His-tagged enzyme, gel filtration
130700
recombinant His-tagged enzyme, gel filtration
15000
-
2 * 15000, SDS-PAGE
15000
-
x * 30000-31000, isozyme 1, SDS-PAGE, x * 15000, isozyme 2, SDS-PAGE
155000
-
PAGE, isoform with pI 4.6
155000
-
isozyme 2, native PAGE
15800
-
x * 15800, MALDI-TOF-MS
15800
2 * 42000, recombinant GST-tagged SeCuZnSOD, SDS-PAGE, 2 * 15800, untagged enzyme, SDS-PAGE
16000
-
2 * 16000, Cu,Zn-SOD, SDS-PAGE
16000
-
2 * 16000, Cu,Zn-SOD, SDS-PAGE
16000
-
2 * 16000, Cu,Zn-SOD, SDS-PAGE
16000
-
2 * 16000, Cu,Zn-SOD, SDS-PAGE
16000
-
2 * 16000, SDS-PAGE, isoenzyme B
16000
-
2 * 16000, SDS-PAGE
16000
x * 15500, calculated, x * 16000, SDS-PAGE
16400
about, recombinant His6-and thioredoxin-tagged enzyme, mass spectrometry
16400
-
x * 16400, Cu,Zn-SOD, SDS-PAGE
16500
recombinant His6-and thioredoxin-tagged enzyme, gel filtration
16500
-
2 * 16500, Cu,Zn-SOD-II, SDS-PAGE
16500
-
2 * 16500, SOD-1, SDS-PAGE
16800
-
2 * 16800, SDS-PAGE
16800
2 * 16800, SDS-PAGE
17000
-
2 * 17000, SDS-PAGE
17000
-
2 * 17000, SOD-2, SDS-PAGE
17000
x * 17000, SDS-PAGE, x * 15704, MALDI-TOF
17000
2 * 15960, sequence calculation, 2 * 17000, recombinant enzyme, SDS-PAGE
18000
-
2 * 18000, SDS-PAGE
18000
-
x * 18000, Cu,Zn-SOD, SDS-PAGE
18300
-
2 * 18300, Mn-SOD, SDS-PAGE
18300
-
2 * 18300, Cu,Zn-SOD, SDS-PAGE
18500
-
2 * 18500, Fe-SOD, SDS-PAGE
18500
-
2 * 18500, isozyme I, SDS-PAGE
19500
amino acid sequence determination, SDS-PAGE
19500
-
2 * 19500, Fe-SOD, SDS-PAGE
19500
-
2 * 19500, isozyme II, SDS-PAGE
20000
-
SODI, native PAGE
20000
-
2 * 20000, SDS-PAGE
20000
-
2 * 20000, SDS-PAGE
20000
-
2 * 20000, Fe-SOD, SDS-PAGE
205000
-
PAGE, isoform with pI 4.7
205000
-
isozyme 1, native PAGE
21000
SodB, gel filtration
21000
-
2 * 21000, Fe-SOD
21000
-
4 * 21000, Mn-SOD, SDS-PAGE
21000
-
4 * 21000, Mn-SOD, SDS-PAGE
21000
x * 21000, recombinant His-tagged enzyme, SDS-PAGE
21500
SDS-PAGE
21500
-
amino acid sequence determination
21500
amino acid sequence determination
21500
recombinant Cu,Zn-SOD
21700
-
2 * 21700, Mn-SOD, SDS-PAGE
21700
-
x * 21700, SDs-PAGE
21700
4 * 21700, SDS-PAGE
22000
-
PAGE, isozyme SODII
22000
x * 22000, SDS-PAGE
22000
-
2 * 22000, SDS-PAGE
22000
-
2 * 22000, Mn-SOD, SDS-PAGE
22000
-
4 * 22000, Mn-SOD, SDS-PAGE
22000
-
4 * 22000, Mn-SOD, SDS-PAGE
22000
-
x * 22000, Fe-SOD, SDS-PAGE
22000
Megalodesulfovibrio gigas
-
x * 22000, Fe-SOD, SDS-PAGE
22000
-
x * 22000, amino acid sequence determination
22000
2 * 21251, mass spectrometry, 2 * 22000, SDS-PAGE
22000
-
x * 22000, recombinant Mn-SOD, SDS-PAGE
22400
-
4 * 22400, SDS-PAGE
22400
-
4 * 22400, Mn-SOD, SDS-PAGE
22400
2 * 22400, calculated from sequence
22400
2 * 22400, simultaneous treatment with low SDS concentrations and heat results in an almost quantitative conversion into a tetrameric form of the enzyme with a specific activity of about 2.5 times higher than the activity of the dimer, suggesting that even though the protein is stable and active in a dimeric state, its physiological form may be tetrameric
23000
-
2 * 23000, SDS-PAGE
23000
Thermochaetoides thermophila
x * 23000, SDS-PAGE
23000
-
2 * 23000, gel filtration, isoenzyme 2 and 3
23000
-
2 * 23000, Fe-/Mn-SOD, SDS-PAGE
23000
-
4 * 21192, MALDI-TOF, 4 * 23000, SDS-PAGE
23000
-
2 * 23000, isozyme SODI, SDS-PAGE
23000
2 * 23000, SDS-PAGE, 2 * 22930, sequence calculation
23000
4 * 23000, recombinant SodA, SDS-PAGE
23500
-
2 * 23500, SDS-PAGE
23500
Thermochaetoides thermophila
-
4 * 23500, SDS-PAGE
23500
-
2 * 23500, Mn-SOD, SDS-PAGE
23500
-
2 * 23500, SDS-PAGE, 2 * 22532, sequence calculation
24000
-
2 * 24000, SDS-PAGE
24000
-
x * 24000, SDS-PAGE
24000
x * 24000, SDS-PAGE
24000
x * 24000, SDS-PAGE
24000
4 * 24000, SDS-PAGE
24000
-
4 * 24000, SOD-III, SDS-PAGE
24000
x * 24225, calculated, x * 24000, SDS-PAGE
24000
-
4 * 24000, alpha2beta2, SDS-PAGE
24000
4 * 24000, recombinant enzyme, SDS-PAGE
24000
-
4 * 24000, wild-type and mutant enzymes, SDS-PAGE
24000
-
4 * 24000, SDS-PAGE and gel filtration
24270
2 * 24270, sequence calculation
24270
2 * 24270, calculated from sequence
24577
in crystals, 4 * 24577, sequence calculation and gel filtration
24577
in solution, 2 * 24577, sequence calculation and gel filtration
24800
2 * 24800, cytMnSOD
24800
x * 24800, about, sequence calculation
25000
-
SODIV, native PAGE
25000
x * 25000, SDS-PAGE
25000
x * 25000, SDS-PAGE
25000
x * 25000, SDS-PAGE
25000
x * 25000, SDS-PAGE
25000
-
4 * 25000, SDS-PAGE
25000
-
2 * 25000, SDS-PAGE
25000
2 * 25000, SDS-PAGE
25000
-
x * 25000, recombinant enzyme, SDS-PAGE
25000
-
4 * 25000, Mn-SOD, reducing SDS-PAGE
25000
-
x * 25000, mitochondria, SDS-PAGE
25000
-
4 * 22321, MALDI-TOF, 4 * 24000-25000, SDS-PAGE in absence, 4 * 25000, in presence of 2-mercaptoethanol
25000
-
2 * 23600, about, recombinant enzyme, sequence calcualtion, 2 * 25000, recombinant enzyme, SDS-PAGE
25000
-
x * 25000, recombinant His-tagged enzyme, SDS-PAGE
25000
x * 25000, recombinant His-tagged enzyme, SDS-PAGE
25400
4 * 25400, Mn-SOD, SDS-PAGE
25400
x * 25400, calculated, x * 28000, SDS-PAGE
26000
band I, native PAGE
26000
-
2 * 26000, SDS-PAGE
26000
-
2 * 26000, SDS-PAGE
26000
-
2 * 26000, SDS-PAGE
26000
-
2 * 26000, SDS-PAGE
26000
-
4 * 26000, Fe-SOD, SDS-PAGE
26000
2 * 26000, recombinant enzyme, SDS-PAGE
27000
-
4 * 27000, Mn-SOD, SDS-PAGE
27000
-
and dimer and octamer, 4 * 27000, SDS-PAGE
27000
-
and dimer and tetramer, 8 * 27000, SDS-PAGE
27000
-
and tetramer and octamer, 2 * 27000, SDS-PAGE
27000
4 * 27000, peroxisomal Mn-SOD, SDS-PAGE
28000
-
4 * 28000, recombinant EC-SOD, SDS-PAGE
28000
x * 25400, calculated, x * 28000, SDS-PAGE
30000
-
Cu,Zn-SOD isoenzyme I, gel filtration, sedimentation equilibrium centrifugation
30000
-
Cu,Zn-SOD, native PAGE
30000
untagged enzyme, gel filtration
30000
-
2 * 30000, SDS-PAGE
30500
-
PAGE
30500
Radix lethospermi
-
2 * 30500, SDS-PAGE, MS
31000
-
gel filtration
31000
-
gel filtration, sedimentation equilibrium
31000
-
about, Cu,Zn-SOD and Mn-SOD, gel filtration
31000
-
Cu,Zn-SOD, sedimentation equilibrium
31000
-
enzyme from cytoplasm
31000 - 33000
-
SOD-2, SOD-4
31000 - 33000
-
gel filtration, SOD-1
31200
-
-
31200
-
Cu,Zn-SOD, sedimentation equilibrium centrifugation analysis
32000
-
gel filtration
32000
-
nonreducing SDS-PAGE
32000
-
x * 32000, native enzyme, SDS-PAGE
32000 - 32500
-
gel filtration
32000 - 32500
-
Cu,Zn-SOD
32000 - 32500
-
Cu,Zn-SOD
32500
-
Cu,Zn-SOD
32500
-
sedimentation equilibrium centrifugation analysis
33000
-
gel filtration
33000
-
Fe-SOD, gel filtration
33000
-
Cu,Zn-SOD-II, gel filtration
33000
-
Cu,Zn-SOD isoenzyme II, gel filtration, sedimentation equilibrium analysis
35000
-
gel filtration
35000
-
dimeric wild-type holo-enzyme
35000
2 * 34589, sequence calculation, 2 * 35000, recombinant His-tagged enzyme, SDS-PAGE, 2 * 34652, recombinant His-tagged enzyme, mass spectrometry, 2 * 53000, recombinant thioredoxin-fusion enzyme, SDS-PAGE
36000
-
gel filtration
36000
-
Fe-SOD, gel filtration
36000
Pibocella sp.
-
native polyacrylamide gel electrophoresis
37400
-
gel filtration
38500
-
-
39800
Fe-SOD
39800
-
Cu,Zn-SOD II, gel filtration
40000
-
gel filtration
40000
-
sedimentation equilibrium analysis
40000
-
native enzyme, gel filtration
40000
-
Fe-SOD, gel filtration, sedimentation analysis
40000
-
native polyacrylamide gel electrophoresis
41500
-
gel filtration
42000
-
Cu,Zn-SOD I, gel filtration
42000
2 * 42000, recombinant GST-tagged SeCuZnSOD, SDS-PAGE, 2 * 15800, untagged enzyme, SDS-PAGE
42000 - 43000
-
-
43000
-
gel filtration
43000
-
isoenzyme 2, gel filtration
43000
-
Mn-SOD, gel filtration
43000
-
Fe-/Mn-SOD, gel filtration
44000
-
gel filtration
44000
-
Mn-SOD, gel filtration
44000
band II, native PAGE
45000
-
-
45000
non-reducing SDS-PAGE
45000
dimeric form, gel filtration
45000
x * 45000, SDS-PAGE of native protein, x * 34000-38000 and x * 29000-33000, SDS-PAGE of deglycosylated protein
45000
x *17000, recombinant SOD1, SDS-PAGE, x * 45000, recombinant SOD1-Lys7, SDS-PAGE
46000
-
-
46000
-
isozyme SODI, gel filtration
46000
Amphiprora kufferathii
-
native polyacrylamide gel electrophoresis
47000
-
-
47000
-
Fe-SOD, gel filtration
48000
-
48000
-
mass spectrometry
50000
-
gel filtration
50000
recombinant enzyme, gel filtration
50000
-
SODIII, native PAGE
52000
-
recombinant enzyme, gel filtration
52000
-
Mn-SOD, gel filtration
56000
gel filtration
56000
-
Mn-SOD, gel filtration
59000
Amphiprora kufferathii
-
native polyacrylamide gel electrophoresis
59000
2 * 59000, SDS-PAGE, 2 * 50230, sequence calculation
60000
-
gel filtration
60000
Radix lethospermi
-
gel filtration
60000
-
SODII, native PAGE
61000
gel filtration
63000
-
gel filtration
63000
-
Fe-SOD, gel filtration
69000
-
-
69000
-
Cu,Zn-SOD, gel filtration
69000
recombinant His-tagged enzyme, gel filtration
80000
-
-
80000
-
Mn-SOD, gel filtration
82000
-
-
82000
SodA, gel filtration
85000
-
sedimentation equilibrium, SOD-3
85000
recombinant His-tagged Mn-SOD, gel filtration
87900
-
gel filtration
87900
-
wild-type and mutant enzymes, gel filtration
88000
-
gel filtration
88000
recombinant enzyme, gel filtration
88000
-
Mn-SOD, gel filtration
88000
-
Mn-SOD, native PAGE
91000
-
-
91000
-
Fe-SOD, sedimentation equilibrium analysis
96000
-
enzyme from mitochondria
96000
-
Mn-SOD gel filtration
additional information
-
-
additional information
-
primary structure of human erythrocyte enzyme
additional information
-
two distinct bands exhibiting SOD activity appear on native PAGE: one band, with higher mobility, appears when the cells are grown without CuSO4, and the other band appears when the cells are grown with 10 mM CuSO4. Cells grown with 3 mM CuSO4 produce both SOD isoforms
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
heterodimer
-
1 * 17600+ 1 * 31500, SDS-PAGE
octamer
-
and dimer and tetramer, 8 * 27000, SDS-PAGE
?
-
x * 185000, Cu,Zn-SOD, SDS-PAGE
?
-
x * 185000, Cu,Zn-SOD, SDS-PAGE
-
?
x * 15835, mass spectrometry and dynamic light scattering
?
x * 38159, mass spectrometry and dynamic light scattering
?
-
x * 38159, mass spectrometry and dynamic light scattering
-
?
-
x * 15835, mass spectrometry and dynamic light scattering
-
?
-
x * 19250, Cu,Zn-SOD, SDS-PAGE
?
-
x * 19250, Cu,Zn-SOD, SDS-PAGE
-
?
-
x * 18000, Cu,Zn-SOD, SDS-PAGE
?
-
x * 18000, Cu,Zn-SOD, SDS-PAGE
-
?
-
x * 175000, Cu,Zn-SOD, SDS-PAGE
?
-
x * 175000, Cu,Zn-SOD, SDS-PAGE
-
?
-
x * 31000, native enzyme, SDS-PAGE
?
x * 22650, sequence calculation
?
-
x * 22650, sequence calculation
-
?
x *17000, recombinant SOD1, SDS-PAGE, x * 45000, recombinant SOD1-Lys7, SDS-PAGE
?
-
x *17000, recombinant SOD1, SDS-PAGE, x * 45000, recombinant SOD1-Lys7, SDS-PAGE
-
?
x * 24225, calculated, x * 24000, SDS-PAGE
?
-
x * 15841, sequence calculation
?
x * 25000, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 25000, recombinant His-tagged enzyme, SDS-PAGE
-
?
x * 24000, about, sequence calculation
?
x * 22931, Fe-SOD, amino acid sequence determination
?
-
x * 22931, Fe-SOD, amino acid sequence determination
-
?
x * 15500, calculated, x * 16000, SDS-PAGE
?
x * 25400, calculated, x * 28000, SDS-PAGE
?
x * 17000, SDS-PAGE, x * 15704, MALDI-TOF
?
x * 18000, recombinant His-tagged enzyme, SDS-PAGE
?
x * 24989, sequence calculation, MnSOD
?
-
x * 24989, sequence calculation, MnSOD
-
?
-
x * 15920, sequence calculation, x * 18000, SDS-PAGE
?
-
x * 22000, recombinant Mn-SOD, SDS-PAGE
?
-
x * 15132, sequence calculation
?
-
x * 30000-31000, isozyme 1, SDS-PAGE, x * 15000, isozyme 2, SDS-PAGE
?
x * 15700, about, cytoplasmic CuZn-SOD, sequence calculation
?
-
x * 15764-15809, Cu,Zn-SOD wild-type and mutant D90A, electrospray mass spectroscopy
?
-
x * 22000, amino acid sequence determination
?
-
x * 15800, MALDI-TOF-MS
?
-
x * 15764-15809, Cu,Zn-SOD wild-type and mutant D90A, electrospray mass spectroscopy
-
?
-
x * 22000, amino acid sequence determination
-
?
x * 15832, sequence calculation
?
x * 15882, Cu/Zn-SOD sequence calculation
?
-
x * 15882, Cu/Zn-SOD sequence calculation
-
?
x * 24800, about, sequence calculation
?
-
x * 25000, SDS-PAGE
-
?
-
x * 25000, SDS-PAGE
-
?
Megalodesulfovibrio gigas
-
x * 22000, Fe-SOD, SDS-PAGE
?
Megalodesulfovibrio gigas Fe-SOD
-
x * 22000, Fe-SOD, SDS-PAGE
-
?
x * 21000, recombinant His-tagged enzyme, SDS-PAGE
?
x * 45000, SDS-PAGE of native protein, x * 34000-38000 and x * 29000-33000, SDS-PAGE of deglycosylated protein
?
x * 32000, recombinant His-tagged enzyme, SDS-PAGE, x * 30960, recombinant His-tagged enzyme, sequence calculation
?
-
x * 22500-29000, nectarin I: Mn-SOD, SDS-PAGE and mass spectroscopy
?
-
x * 25000, SDS-PAGE
-
?
-
detection of isoforms with 34500, 36000 and 50000 Da in non-denaturing gels
?
x * 106000, or x * 97000, SDS-PAGE, differently glycosylated protein forms
?
-
x * 25000, recombinant enzyme, SDS-PAGE
?
-
x * 22000, Fe-SOD, SDS-PAGE
?
-
x * 24000, SDS-PAGE
-
?
-
x * 25000, mitochondria, SDS-PAGE
?
-
x * 25000, mitochondria, SDS-PAGE
-
?
-
x * 22500-24000, Fe-SOD, SDS-PAGE
?
x * 24228, calculated from sequence
?
-
x * 22500-24000, Fe-SOD, SDS-PAGE
-
?
-
x * 24228, calculated from sequence
-
?
-
x * 16400, Cu,Zn-SOD, SDS-PAGE
?
-
x * 15800-16600 , two isozymes, sequence calculation, x * 18000, SDS-PAGE
?
-
x * 15800-16600 , two isozymes, sequence calculation, x * 18000, SDS-PAGE
-
?
-
x * 25000, recombinant His-tagged enzyme, SDS-PAGE
?
x * 15320, SaCSD1, sequence calculation
?
-
x * 30000, about, sequence calculation, x * 25000, recombinant enzyme, SDS-PAGE
?
-
x * 17600 + x * 31500, SDS-PAGE
?
-
x * 32000, native enzyme, SDS-PAGE
?
Thermochaetoides thermophila
x * 23000, SDS-PAGE
?
Thermochaetoides thermophila
x * 17700, recombinant enzyme, SDS-PAGE
?
-
x * 25000, SDS-PAGE
-
?
x * 26000, recombinant enzyme mutants H29A and H171A, SDS-PAGE
dimer
-
2 * 21600, SDS-PAGE after denaturation in boiling SDS
dimer
-
2 * 21600, SDS-PAGE after denaturation in boiling SDS
-
dimer
-
2 * 16000, Cu,Zn-SOD, SDS-PAGE
dimer
Anas platyrhynchos domestica CuZn-SOD
-
2 * 16000, Cu,Zn-SOD, SDS-PAGE
-
dimer
-
2 * 18100, Fe-SOD, SDS-PAGE
dimer
-
2 * 18100, Fe-SOD, SDS-PAGE
-
dimer
-
2 * 15821, Cu,Zn-SOD, sequence calculation
dimer
-
2 * 15821, Cu,Zn-SOD, sequence calculation
-
dimer
-
2 * 20000, SDS-PAGE
dimer
-
2 * 16300, SDS-PAGE
dimer
-
2 * 16000, SDS-PAGE, isoenzyme B
dimer
-
2 * 16000, SDS-PAGE, isoenzyme B
-
dimer
-
2 * 20000, Fe-SOD, SDS-PAGE
dimer
-
2 * 20000, Fe-SOD, SDS-PAGE
-
dimer
-
2 * 22000, Mn-SOD, SDS-PAGE
dimer
-
2 * 16000, Cu,Zn-SOD, SDS-PAGE
dimer
-
2 * 22000, Mn-SOD, SDS-PAGE
-
dimer
-
2 * 16000, Cu,Zn-SOD, SDS-PAGE
-
dimer
-
2 * 16000, SDS-PAGE
dimer
-
2 * 18300, Mn-SOD, SDS-PAGE
dimer
-
2 * 18300, Mn-SOD, SDS-PAGE
-
dimer
-
2 * 16500, Cu,Zn-SOD-II, SDS-PAGE
dimer
2 * 17900, SDS-PAGE
dimer
-
2 * 23000, gel filtration, isoenzyme 2 and 3
dimer
-
2 * 23000, gel filtration, isoenzyme 2 and 3
-
dimer
2 * 23652, SOD1, sequence calculation
dimer
2 * 26000, recombinant enzyme, SDS-PAGE
dimer
-
2 * 15000, SDS-PAGE
dimer
-
2 * 26000, SDS-PAGE
dimer
-
2 * 18000, SDS-PAGE
dimer
-
2 * 18000, SDS-PAGE
-
dimer
-
2 * 22900, Mn-SOD
dimer
-
2 * 21000, Fe-SOD
dimer
-
2 * 22900, Mn-SOD
-
dimer
-
2 * 21000, Fe-SOD
-
dimer
-
2 * 22900, Mn-SOD
-
dimer
-
2 * 21000, Fe-SOD
-
dimer
-
2 * 16000, Cu,Zn-SOD, SDS-PAGE
dimer
-
2 * 16000, Cu,Zn-SOD, SDS-PAGE
-
dimer
-
2 * 23500, Mn-SOD, SDS-PAGE
dimer
-
the homodimer contains an extended C-terminal tail comprising residues 193-213. Dimer interface and domain interface structure analysis: the shortest domain contacts involve residues Phe17, Leu52, Phe53, Tyr71, and Phe75 on one domain and Val145, Pro151, Val154, Tyr173, Phe177, His180, Cys189, Leu198, Ile205, and His210 on the other domain, and the dimer interface is stabilized by 10 hydrogen bonds and approximately 102 non-bonded contacts, involving 32 residues from both chains, overview
dimer
-
wild-type holo-enzyme
dimer
2 * 33000, recombinant enzyme, SDS-PAGE
dimer
-
2 * 15912, mass spectrometry
dimer
-
2 * 15912, mass spectrometry
-
dimer
2 * 34589, sequence calculation, 2 * 35000, recombinant His-tagged enzyme, SDS-PAGE, 2 * 34652, recombinant His-tagged enzyme, mass spectrometry, 2 * 53000, recombinant thioredoxin-fusion enzyme, SDS-PAGE
dimer
-
2 * 22000, SDS-PAGE
dimer
-
2 * 22000, SDS-PAGE
-
dimer
-
2 * 18500, Fe-SOD, SDS-PAGE
dimer
-
2 * 18500, Fe-SOD, SDS-PAGE
-
dimer
-
2 * 17500, Cu,Zn-SOD
dimer
-
2 * 17500, Cu,Zn-SOD
-
dimer
-
2 * 24000, SDS-PAGE
dimer
-
2 * 24000, SDS-PAGE
-
dimer
-
2 * 15000-20000, SDS-PAGE
dimer
-
2 * 23100, SDS-PAGE
dimer
-
2 * 23100, SDS-PAGE
-
dimer
-
2 * 16800, SDS-PAGE
dimer
-
2 * 16800, SDS-PAGE
-
dimer
-
2 * 26000, SDS-PAGE
dimer
-
2 * 26000, SDS-PAGE
-
dimer
-
2 * 25000, SDS-PAGE
dimer
-
2 * 25000, SDS-PAGE
-
dimer
-
2 * 23000, SDS-PAGE
dimer
-
2 * 23500, SDS-PAGE
dimer
-
2 * 23500, SDS-PAGE
-
dimer
-
2 * 22000, SDS-PAGE
dimer
-
2 * 20400, SOD-3, SDS-PAGE
dimer
-
2 * 16500, SOD-1, SDS-PAGE
dimer
-
2 * 15700, SDS-PAGE
dimer
-
2 * 19000, SDS-PAGE
dimer
-
2 * 19000, SDS-PAGE
-
dimer
2 * 21251, mass spectrometry, 2 * 22000, SDS-PAGE
dimer
-
2 * 21700, Mn-SOD, SDS-PAGE
dimer
-
2 * 21700, Mn-SOD, SDS-PAGE
-
dimer
-
2 * 19500, Fe-SOD, SDS-PAGE
dimer
-
2 * 19500, Fe-SOD, SDS-PAGE
-
dimer
-
2 * 20000, SDS-PAGE
dimer
Radix lethospermi
-
2 * 30500, SDS-PAGE, MS
dimer
-
2 * 17000, SDS-PAGE
dimer
-
2 * 17000, SDS-PAGE
-
dimer
-
2 * 17000, SDS-PAGE
-
dimer
-
2 * 23600, about, recombinant enzyme, sequence calcualtion, 2 * 25000, recombinant enzyme, SDS-PAGE
dimer
-
2 * 23600, about, recombinant enzyme, sequence calcualtion, 2 * 25000, recombinant enzyme, SDS-PAGE
-
dimer
-
a noncovalently bound homodimer, primary structure
dimer
-
a noncovalently bound homodimer, primary structure
-
dimer
-
2 * 18300, Cu,Zn-SOD, SDS-PAGE
dimer
-
2 * 16000, Cu,Zn-SOD, SDS-PAGE
dimer
-
cytoplasmic enzyme
dimer
-
cytoplasmic enzyme
-
dimer
-
2 * 18300, Cu,Zn-SOD, SDS-PAGE
-
dimer
-
2 * 16000, Cu,Zn-SOD, SDS-PAGE
-
dimer
-
cytoplasmic enzyme
-
dimer
-
2 * 23000, Fe-/Mn-SOD, SDS-PAGE
dimer
-
2 * 23000, Fe-/Mn-SOD, SDS-PAGE
-
dimer
-
2 * 22500, Fe-SOD, SDS-PAGE
dimer
-
2 * 15100, isoenzyme II, SDS-PAGE
dimer
-
isoenzyme I, SDS-PAGE
dimer
-
2 * 18200, SDS-PAGE
dimer
-
2 * 22500, Fe-SOD, SDS-PAGE
-
dimer
-
2 * 26000, SDS-PAGE
dimer
-
2 * 26000, SDS-PAGE
-
dimer
-
2 * 19500, isozyme II, SDS-PAGE
dimer
-
2 * 18500, isozyme I, SDS-PAGE
dimer
2 * 24270, sequence calculation
dimer
2 * 22400, calculated from sequence
dimer
2 * 24270, calculated from sequence
dimer
-
2 * 24270, calculated from sequence
-
dimer
-
2 * 22400, calculated from sequence
-
dimer
2 * 16800, SDS-PAGE
dimer
-
2 * 23000, isozyme SODI, SDS-PAGE
dimer
-
and tetramer and octamer, 2 * 27000, SDS-PAGE
dimer
-
2 * 26000, SDS-PAGE
dimer
-
2 * 26000, SDS-PAGE
-
dimer
-
2 * 17000, SOD-2, SDS-PAGE
dimer
-
2 * 15900, SOD-4, SDS-PAGE
dimer
-
2 * 14500, SOD-1, SDS-PAGE
dimer
-
2 * 14500, SOD-1, SDS-PAGE
-
dimer
-
2 * 17000, SOD-2, SDS-PAGE
-
dimer
-
2 * 15900, SOD-4, SDS-PAGE
-
homodimer
2 * 25000, SDS-PAGE
homodimer
in solution, 2 * 24577, sequence calculation and gel filtration
homodimer
2 * 24600, calculated from sequence
homodimer
-
2 * 24600, calculated from sequence
-
homodimer
-
2 * 25000, SDS-PAGE
-
homodimer
2 * 15600, about, sequence calculation
homodimer
2 * 17500, His-tagged enzyme, SDS-PAGE, 2 * 15160, sequence calculation
homodimer
2 * 17500, about, sequence calculation, 2 * 18800, about, SDS-PAGE
homodimer
enzyme tertiary structural modeling, each monomer contains an eight-barrel chain with seven loops
homodimer
-
2 * 23500, SDS-PAGE, 2 * 22532, sequence calculation
homodimer
-
2 * 23500, SDS-PAGE, 2 * 22532, sequence calculation
-
homodimer
2 * 59000, SDS-PAGE, 2 * 50230, sequence calculation
homodimer
2 * 59000, recombinant His-tagged enzyme, SDS-PAGE
homodimer
-
2 * 38000, recombinant chimera MnSOD-VHb, SDS-PAGE
homodimer
-
2 * 34034, sequence calculation and mass spectrometry
homodimer
-
2 * 34034, sequence calculation and mass spectrometry
-
homodimer
2 * 23000, SDS-PAGE, 2 * 22930, sequence calculation
homodimer
-
2 * 23000, SDS-PAGE, 2 * 22930, sequence calculation
-
homodimer
-
2 * 31079, sequence calculation
homodimer
2 * 24800, cytMnSOD
homodimer
2 * 18000, recombinant His-tagged enzyme, SDS-PAGE
homodimer
2 * 23500, about, sequence calculation, 2 * 31000, recombinant His-tagged enzyme, SDS-PAGE
homodimer
-
2 * 23500, about, sequence calculation, 2 * 31000, recombinant His-tagged enzyme, SDS-PAGE
-
homodimer
-
2 * 20000, native enzyme, SDS-PAGE
homodimer
2 * 42000, recombinant GST-tagged SeCuZnSOD, SDS-PAGE, 2 * 15800, untagged enzyme, SDS-PAGE
homodimer
-
2 * 30000, SDS-PAGE
homodimer
-
2 * 23000, SDS-PAGE
homodimer
2 * 27400, claculated, 2 * 29700, SDS-PAGE
homodimer
2 * 15960, sequence calculation, 2 * 17000, recombinant enzyme, SDS-PAGE
homotetramer
in crystals, 4 * 24577, sequence calculation and gel filtration
homotetramer
-
4 * 22000, Mn-SOD, SDS-PAGE
homotetramer
-
4 * 14000, SDS-PAGE
homotetramer
-
4 * 21192, MALDI-TOF, 4 * 23000, SDS-PAGE
homotetramer
-
4 * 21192, MALDI-TOF, 4 * 23000, SDS-PAGE
-
homotetramer
4 * 24000, mtMnSOD
homotetramer
-
4 * 24000, SDS-PAGE and gel filtration
homotetramer
-
4 * 24000, SDS-PAGE and gel filtration
-
monomer
1 * 17500, His-tagged enzyme, SDS-PAGE, 1 * 15160, sequence calculation
monomer
-
1 * 100000, Mn-SOD, reducing SDS-PAGE
monomer
-
1 * 100000, Mn-SOD, reducing SDS-PAGE
-
monomer
1 * 50230, sequence calculation, 1 * 59000, SDS-PAGE
monomer
1 * 33000, recombinant enzyme, SDS-PAGE
monomer
1 * 16385, sequence calculation, 1 * 16400, about, recombinant His6-and thioredoxin-tagged enzyme, mass spectrometry and SDS-PAGE
monomer
-
1 * 33000, SDS-PAGE after treatment with urea and 2-mercaptoethanol
monomer
-
1 * 33000, SDS-PAGE after treatment with urea and 2-mercaptoethanol
-
monomer
-
1 * 66000, SODI, 1 * 22000, SODII, SDS-PAGE
monomer
-
1 * 15700, SDS-PAGE
monomer
1 * 21400, about, sequence calculation, 1 * 27000, recombinant His-tagged enzyme, SDS-PAGE
monomer
-
crystallization data
monomer
1 * 21000, recombinant SodB, SDS-PAGE
monomer
-
1 * 21000, recombinant SodB, SDS-PAGE
-
monomer or dimer
-
the kinetic mechanism for holo SODs involves native dimer-monomer intermediate, and unfolded monomer, with variable metal dissociation from the monomeric states depending on solution conditions, overview. Naturally occuring mutants seem to favour increased formation of a Zn-free monomer intermediate, which is implicated in the formation of toxic aggregates. Kinetic basis for the extremely high stability of wild-type holo SOD, overview
monomer or dimer
x * 26000, SDS-PAGE
tetramer
4 * 23954, sequence calculation
tetramer
-
4 * 22340, Mn-SOD, sequence calculation
tetramer
-
4 * 22340, Mn-SOD, sequence calculation
-
tetramer
4 * 25400, Mn-SOD, SDS-PAGE
tetramer
4 * 27000, peroxisomal Mn-SOD, SDS-PAGE
tetramer
-
4 * 21300, SDS-PAGE
tetramer
-
4 * 28000, recombinant EC-SOD, SDS-PAGE
tetramer
-
4 * 21300, SDS-PAGE
-
tetramer
-
4 * 26000, Fe-SOD, SDS-PAGE
tetramer
-
4 * 26000, Fe-SOD, SDS-PAGE
-
tetramer
-
4 * 24096, amino acid sequence determination
tetramer
-
4 * 22321, MALDI-TOF, 4 * 24000-25000, SDS-PAGE in absence, 4 * 25000, in presence of 2-mercaptoethanol
tetramer
-
4 * 25000, SDS-PAGE
tetramer
-
4 * 25000, SDS-PAGE
-
tetramer
-
4 * 27000, Mn-SOD, SDS-PAGE
tetramer
-
4 * 27000, Mn-SOD, SDS-PAGE
-
tetramer
4 * 24000, SDS-PAGE
tetramer
4 * 24204, calculated from sequence
tetramer
-
4 * 24000, SDS-PAGE
-
tetramer
-
4 * 24204, calculated from sequence
-
tetramer
-
4 * 22400, Mn-SOD, SDS-PAGE
tetramer
-
4 * 22000, Mn-SOD, SDS-PAGE
tetramer
-
4 * 22000, Mn-SOD, SDS-PAGE
-
tetramer
-
4 * 22000, Mn-SOD, SDS-PAGE
-
tetramer
-
4 * 22400, Mn-SOD, SDS-PAGE
-
tetramer
-
4 * 24000, alpha2beta2, SDS-PAGE
tetramer
4 * 24000, recombinant enzyme, SDS-PAGE
tetramer
-
4 * 24000, wild-type and mutant enzymes, SDS-PAGE
tetramer
-
4 * 25000, Mn-SOD, reducing SDS-PAGE
tetramer
-
mitochondrial enzyme
tetramer
-
mitochondrial enzyme
-
tetramer
-
mitochondrial enzyme
-
tetramer
-
4 * 25000, Mn-SOD, reducing SDS-PAGE
-
tetramer
2 * 22400, simultaneous treatment with low SDS concentrations and heat results in an almost quantitative conversion into a tetrameric form of the enzyme with a specific activity of about 2.5 times higher than the activity of the dimer, suggesting that even though the protein is stable and active in a dimeric state, its physiological form may be tetrameric
tetramer
-
2 * 22400, simultaneous treatment with low SDS concentrations and heat results in an almost quantitative conversion into a tetrameric form of the enzyme with a specific activity of about 2.5 times higher than the activity of the dimer, suggesting that even though the protein is stable and active in a dimeric state, its physiological form may be tetrameric
-
tetramer
4 * 21700, SDS-PAGE
tetramer
Thermochaetoides thermophila
-
4 * 23500, SDS-PAGE
tetramer
Thermochaetoides thermophila CT2
-
4 * 23500, SDS-PAGE
-
tetramer
-
4 * 22400, SDS-PAGE
tetramer
-
4 * 22400, SDS-PAGE
-
tetramer
-
4 * 21000, Mn-SOD, SDS-PAGE
tetramer
-
4 * 21000, Mn-SOD, SDS-PAGE
-
tetramer
-
4 * 21000, Mn-SOD, SDS-PAGE
tetramer
-
4 * 21000, Mn-SOD, SDS-PAGE
-
tetramer
-
4 * 21000, Mn-SOD, SDS-PAGE
-
tetramer
-
and dimer and octamer, 4 * 27000, SDS-PAGE
tetramer
4 * 23000, recombinant SodA, SDS-PAGE
tetramer
-
4 * 23000, recombinant SodA, SDS-PAGE
-
tetramer
-
4 * 24000, SOD-III, SDS-PAGE
tetramer
-
4 * 24000, SOD-III, SDS-PAGE
-
trimer or tetramer
-
x * 24140, mass spectrometry
trimer or tetramer
-
x * 24140, mass spectrometry
-
additional information
three-dimensional structure modelling, overview
additional information
-
three-dimensional structure modelling, overview
additional information
enzyme structural analysis by circular dichroism analysis, recombinnat AhSOD is an intrinsically disorder enzyme, sequence comparisons and three-dimensional model
additional information
-
enzyme structural analysis by circular dichroism analysis, recombinnat AhSOD is an intrinsically disorder enzyme, sequence comparisons and three-dimensional model
additional information
-
peptide mapping by tryptic digest and amino acid sequence determination and analysis, the enzyme does neither contain a Tyr residue nor a carbohydrate chain occupying an N-linkage site -N-I-Y-,overview, homology modeling of Cu/Zn-SOD
additional information
-
peptide mapping by tryptic digest and amino acid sequence determination and analysis, the enzyme does neither contain a Tyr residue nor a carbohydrate chain occupying an N-linkage site -N-I-Y-,overview, homology modeling of Cu/Zn-SOD
-
additional information
-
isoform SOD1 stabilizes and activates calcineurin in rat brain cytosol via a nearly 90fold decrease in the KM for p-nitrophenylphosphate. SOD1 prevents the loss of iron and Zn from the active site of calcineurin, possibly by a conformation-dependent interaction. SOD1 also activates human calcineurin by 74%
additional information
the enzyme exists in both monomeric and dimeric forms, the latter being more active. Circular dichroic spectroscopy analysis confirms the thermostable nature of Cj-Cu,Zn SOD, secondary structure analysis, overview
additional information
homology structure modeling of PgCuZnSOD, overview
additional information
-
homology structure modeling of PgCuZnSOD, overview
additional information
Cu,Zn-SOD exists as 70% dimeric form and 30% monomeric form
additional information
-
Cu,Zn-SOD exists as 70% dimeric form and 30% monomeric form
additional information
-
Cu,Zn-SOD exists as 70% dimeric form and 30% monomeric form
-
additional information
SOD1 possesses a short amino-terminal extension which could represent, in this heterotrophic dinoflagellate lacking a chloroplast, a putative mitochondrial targeting signal
additional information
SOD1 possesses a short amino-terminal extension which could represent, in this heterotrophic dinoflagellate lacking a chloroplast, a putative mitochondrial targeting signal
additional information
SOD1 possesses a short amino-terminal extension which could represent, in this heterotrophic dinoflagellate lacking a chloroplast, a putative mitochondrial targeting signal
additional information
-
SOD1 possesses a short amino-terminal extension which could represent, in this heterotrophic dinoflagellate lacking a chloroplast, a putative mitochondrial targeting signal
additional information
MnSOD molecular modelling of the highly conserved sequence, structure modelling and comparison with MnSODs from other organisms
additional information
-
MnSOD molecular modelling of the highly conserved sequence, structure modelling and comparison with MnSODs from other organisms
additional information
-
MnSOD molecular modelling of the highly conserved sequence, structure modelling and comparison with MnSODs from other organisms
-
additional information
-
N-terminal amino acid sequence
additional information
modelling of the three-dimensional structure of SOD monomer, overview
additional information
-
three-dimensional structure of Mn-SOD monomer
additional information
-
three-dimensional structure of Mn-SOD monomer
-
additional information
-
isoform SOD1 stabilizes and activates calcineurin in rat brain cytosol by 47%
additional information
asymmetric structure of the zinc-deficient enzyme, overview
additional information
-
asymmetric structure of the zinc-deficient enzyme, overview
additional information
hEC-SOD is present both as a monomer (33 kDa) and a dimer (66 kDa), enzyme secondary structure determination by circular dichroism, recombinant hEC-SOD purified from Sf9 insect cells is mainly composed of beta-sheet structures
additional information
-
hEC-SOD is present both as a monomer (33 kDa) and a dimer (66 kDa), enzyme secondary structure determination by circular dichroism, recombinant hEC-SOD purified from Sf9 insect cells is mainly composed of beta-sheet structures
additional information
-
enzyme is only active as tetramer or pentamer
additional information
the enzyme sequence comprises eight beta-sheets forming a beta-barrel topology, alignment and modeling studies confirmed the conservation of Cu/ZnSOD at primary and tertiary levels. Structure homology modeling and three-dimensional structure, overview
additional information
-
the enzyme sequence comprises eight beta-sheets forming a beta-barrel topology, alignment and modeling studies confirmed the conservation of Cu/ZnSOD at primary and tertiary levels. Structure homology modeling and three-dimensional structure, overview
additional information
cytMnSOD is composed of a leader sequence with 61 amino acid peptide, putative Mn binding sites H111, H159, D244 and H248, two N-glycosylation sites, NHT and NMA, and the MnSOD domain, MSD. mtMnSOD is composed of putative Mn binding sites H49, H97, D181 and H185, two N-glycosylation sites, NHT and NLS, MSD, and a mitochondrial-targeting sequence with 21 aa peptide
additional information
cytMnSOD is composed of a leader sequence with 61 amino acid peptide, putative Mn binding sites H111, H159, D244 and H248, two N-glycosylation sites, NHT and NMA, and the MnSOD domain, MSD. mtMnSOD is composed of putative Mn binding sites H49, H97, D181 and H185, two N-glycosylation sites, NHT and NLS, MSD, and a mitochondrial-targeting sequence with 21 aa peptide
additional information
-
cytMnSOD is composed of a leader sequence with 61 amino acid peptide, putative Mn binding sites H111, H159, D244 and H248, two N-glycosylation sites, NHT and NMA, and the MnSOD domain, MSD. mtMnSOD is composed of putative Mn binding sites H49, H97, D181 and H185, two N-glycosylation sites, NHT and NLS, MSD, and a mitochondrial-targeting sequence with 21 aa peptide
additional information
-
amino-terminal peptide sequence
additional information
-
the purified SOD appears to be monomeric and converts to its dimeric form with increased enzymatic activity in betel nut oral extract. This irreversible conversion is mainly induced by slaked lime, resulting from the increase in pH of the oral cavity. Oral extract from chewing areca nut alone also induces SOD dimerization due to the presence of arginine
additional information
circular dichroism spectral analysis of the enzyme's secondary structure. The enzyme conserves the beta-barrel structure of the CuZn-SODs in its recombinant form
additional information
-
circular dichroism spectral analysis of the enzyme's secondary structure. The enzyme conserves the beta-barrel structure of the CuZn-SODs in its recombinant form
additional information
-
immunoblot analysis shows isoforms of 25 and 75 kDa with increased expression of the 75 kDa isoform after treatment with corticotrophin
additional information
-
the N-terminal sequence of the purified native enzyme is VLKAVCVLKGTGEVT
additional information
-
secondary, quarternary and three-dimensional structure
additional information
-
secondary, quarternary and three-dimensional structure
-
additional information
Thermochaetoides thermophila
-
the enzyme contains the sequence TLPDLKYD at the N-terminus
additional information
Thermochaetoides thermophila
subunit interface structure, overview
additional information
Thermochaetoides thermophila CT2
-
the enzyme contains the sequence TLPDLKYD at the N-terminus
-
additional information
-
secondary structure analysis by CD spectroscopy, the enzyme has a high alpha-helical content of 70%, overview
additional information
structure models of three enzyme mutants His29Ala, His84Ala, and His171Ala, overview
additional information
-
secondary structure analysis by CD spectroscopy, the enzyme has a high alpha-helical content of 70%, overview
-
additional information
-
amino acid sequence comparisons, the swortfish SOD has a higher content of arginine and tyrosine than the corresponding bovine enzyme and appears to dissociate more readily into subunits. The swortfish enzyme has a higher content of arginine and tyrosine, high homology with the other eukaryotic enzymes,and low homology with the Photobacterium leiognuthi enzyme
additional information
secondary structure analysis using circular dichroism, overview. At pH 7.0 and 28°C, SodA contains 29% alpha-helix and 16% beta-sheets. The elements of secondary structures are more sensitive to pH than to temperature
additional information
secondary structure analysis using circular dichroism, overview. At pH 7.0 and 28°C, SodA contains 29% alpha-helix and 16% beta-sheets. The elements of secondary structures are more sensitive to pH than to temperature
additional information
secondary structure analysis using circular dichroism, overview. At pH 7.0 and 28°C, SodA contains 29% alpha-helix and 16% beta-sheets. The elements of secondary structures are more sensitive to pH than to temperature
additional information
-
secondary structure analysis using circular dichroism, overview. At pH 7.0 and 28°C, SodA contains 29% alpha-helix and 16% beta-sheets. The elements of secondary structures are more sensitive to pH than to temperature
additional information
secondary structure analysis using circular dichroism, overview. At pH 7.0 and 28°C, SodB contains 44% alpha-helix and 13% beta-sheets. The elements of secondary structures are more sensitive to pH than to temperature
additional information
secondary structure analysis using circular dichroism, overview. At pH 7.0 and 28°C, SodB contains 44% alpha-helix and 13% beta-sheets. The elements of secondary structures are more sensitive to pH than to temperature
additional information
secondary structure analysis using circular dichroism, overview. At pH 7.0 and 28°C, SodB contains 44% alpha-helix and 13% beta-sheets. The elements of secondary structures are more sensitive to pH than to temperature
additional information
-
secondary structure analysis using circular dichroism, overview. At pH 7.0 and 28°C, SodB contains 44% alpha-helix and 13% beta-sheets. The elements of secondary structures are more sensitive to pH than to temperature
additional information
-
secondary structure analysis using circular dichroism, overview. At pH 7.0 and 28°C, SodA contains 29% alpha-helix and 16% beta-sheets. The elements of secondary structures are more sensitive to pH than to temperature
-
additional information
-
secondary structure analysis using circular dichroism, overview. At pH 7.0 and 28°C, SodB contains 44% alpha-helix and 13% beta-sheets. The elements of secondary structures are more sensitive to pH than to temperature
-
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purified recombinant apo, Mn-bound and Fe-bound enzyme, in presence of PEG, 2-3 days, X-ray diffraction structure determination and analysis at 1.56 A, 1.35 A, and 1.48 A, respectively
purified recombinant enzyme by hanging drop vapour diffusion method, 6.5 mg/ml protein in a solution containing 0.1 M Tris-HCl, 1.4 M sodium citrate pH 8.5, 18°C, few days, X-ray diffraction structure determination and analysis at 1.7 A resolution
analysis of both solution and crystal structure of superoxide dismutase paralog lacking two Cu ligands and without enzymic activity. In solution, protein is monomeric. In crystal structure, it is well structured and organized in covalent dimers. Discussion of order/disorder transition
-
extracellular enzyme, tetraborate crystallization of ethanolic enzyme extract, then recrystallization from buffer than from water
MnSOD-2 and MnSOD-3, at 3 and 8 mg/ml respectively, in 10 mM Tris-HCl, pH 7.8, mixing of 0.001 ml protein and reservoir solution, the latter containing 0.1 M bicine pH 9.2 and 3.0 M ammonium sulfate for MnSOD-2, and 0.1 M bicine, pH 9.2, and 2.7 M ammonium sulfate for MnSOD-3, X-ray diffraction structure determination and analysis at 1.7-1.8 A resolution
-
two different monoclinic crystal forms, both with space group P21. Form 1 contains a homodimer in the asymetric unit, form II contains two homodimers per asymmetric unit. Comparison with isostructural MnSOD of Escherichia coli
extracellular enzyme, tetraborate crystallization of ethanolic enzyme extract, then recrystallization from buffer than from water
-
recombinant His6-tagged enzyme, hanging drop vapor diffusion method, 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, at 23°C, mixing of 0.001 ml protein solution with 0.001 ml precipitant solution containing 1.9 M ammonium sulfate in 0.2 M Tris-HCl buffer, pH 8.0, X-ray diffraction structure determination and analysis at 2.4 A resolution, modelling
-
comparison of native protein and enzyme nitrated at active site residue Y34, no significant change in conformation upon nitration
crystal structures of unfluorinated and fluorinated enzyme are nearly superimposable. Ratio kcat/Km decreases from 0.8 per mM and s for wild-type to 0.03 per mM and s for the fluorinated mutant which is in significant part due to 3-fluorotyrosine residues distant from the active-site metal
-
enzyme 10 mg per ml in Tris/HCl 50 mM, pH 8.2 by dialysis against ammonium sulfate 2.8 M, pH 8.2, 4°C
-
from recombinant Mn-SOD, asymmetric unit, hanging drop technique, room temperature, equilibration of 3-4 mg/ml enzyme in ammonium phosphate, pH 5.9, plus 10% 2-methyl-2,4-pentanediol against 32% 2-methyl-2,4-pentanediol, X-ray analysis
-
mutant enzymes F66A and F66L, hanging drop vapor diffusion method, 0.005 ml of enzyme solution are mixed with 0.005 ml of precipitant solution containing 2.5 M ammonium sulfate, 100 mM imidazole, and 100 mM malic acid, pH 8.5, equilibration against 1 ml of precipitant solution, 1 week, room temperature, X-ray diffraction structure determination and analysis at 2.2 A and 2.3 A resolution, respectively
purified enzyme MnSOD in complex with azide, hanging-drop vapor diffusion, mixing of 0.001 ml of 21 mg/ml protein solution with 0.001 ml of reservoir solution 1.8 M potassium phosphate, pH 7.8, at room temperature for1 day, to obtain the azide complex, 0.002 ml of reservoir containing 200 mM sodium azide are added to drops of 6 day crystals, X-ray diffraction structure determination and analysis at 1.77-1.82 A resolution
purified recombinant SOD1, hanging drop vapour diffusion, 0.001 ml of 10 mg/ml protein in 50 mM sodium citrate, pH 5.5, 1 mM DTT, 100 mM CuSO4, and 100 mM ZnSO4, is mixed with 0.001 ml of reservoir solution containing 21-25% w/v PEG 4000, 0.1 M sodium acetate, pH 4.2-5.2, X-ray diffraction structure determination and analysis at 3.5 A, molecular replacement
purified zinc-deficient mutant enzyme, 0.002 ml of solution containing 15.7 mg/ml protein in 50 mM Na/K phosphate, pH 7.7, is mixed with 0.002 ml of reservoir solution containing 2.45 M ammonium sulfate, 200 mM NaCl in 50 mM Tris, pH 7.5, room temperature, less than 1 week, X-ray diffraction structure determination and analysis at 2.0 A resolution, modelling
recombinant human Cu,Zn-SOD expressed in yeast, hanging drop method by vapour diffusion from 50 mM phosphate, pH 7.7, resulting in 3 different crystal forms
-
wild-type, beta-barrel mutant H43R, dimer interface mutant A4V
-
from Cu,Zn-SOD, always twinned, hexagonal crystals with asymmetric units, from 2-methyl-2,4-pentanediol in potassium phosphate buffer, pH 6.5, hanging drop technique by vapour diffusion, X-ray analysis
-
purified recombinant enzyme, two different crystal forms, 15 mg/ml protein, mixing of equal volumes of 0.002 ml of protein and reservoir solution, from 1.8 M ammonium sulfate, 00.1 M NaCl, 100 mM FeCl3, 100 mM HEPES, pH 7.0, and 3% v/v isopropanol, at 20°C, mixing of equal volumes of protein and reservoir solution, 3-5 days, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement
-
Fe-SOD, dialysis against 55% saturated ammonium sulfate solution, pH 4.5, 1 week at 2°C under reduced pressure
-
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
-
purified native and recombinant enzyme, hanging drop vapour diffusion method, 21°C, 2 mg/ml protein, from 8% v/v PEG 8000, 0.1 M Tris-HCl, pH 8.5, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement
-
asymmetric unit, from Cu,Zn-SOD, sitting drop technique by vapour diffusion, 25 mM citrate, 10 mM phosphate buffer, pH 6.5, 6% w/v polyethylene glycol, stabilization by 35% polyethylene glycol, X-ray analysis, modeling of three-dimensional structure
-
dialysis against 0.1 mM EDTA than against water, Mn-SOD
-
extracellular enzyme, tetraborate crystallization of ethanolic enzyme extract, then recrystallization from buffer than from water
-
purified enzyme, hanging drop vapor diffusion method, 20°C, mixing of 0.003 ml of the concentrated protein solution with 0.003 ml of the reservoir solution containing 16.25% PEG 4000, 0.2 M ammonium sulfate, 5% w/v 2-propanole, 0.1 M HEPES, pH 7.5, X-ray diffraction structure determination and analysis at 2.5 A resolution
-
purified recombinant enzyme, hanging-drop vapour-diffusion, 0.0025 ml of 10.5 mg/ml protein in 20 mM Tris-HCl, pH 8.2, are mixed with 0.0025 ml of reservoir solution containing 1.4 M sodium potassium phosphate, pH 8.2, equilibration against 0.8 ml of reservoir solution, 16°C, 4 days, method screening and optimization, X-ray diffraction structure determination and analysis at 1.9 A resolution
Thermochaetoides thermophila
purified recombinant Mn-SOD enzyme, X-ray diffraction structure determination and analysis at 2.0 A resolution
Thermochaetoides thermophila
-
Thermosynechococcus vestitus
-
Mn-SOD, from ammonium sulfate solution, octahedral crystals
-
extracellular enzyme, tetraborate crystallization of ethanolic enzyme extract, then recrystallization from buffer than from water
-
recombinant, His-tagged enzyme
-
extracellular enzyme, tetraborate crystallization of ethanolic enzyme extract, then recrystallization from buffer than from water
-
extracellular enzyme, tetraborate crystallization of ethanolic enzyme extract, then recrystallization from buffer than from water
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
E12Q
superoxide dismutase activity shows a 29% increase in activity relative to activity of the wild-type enzyme
E12V
superoxide dismutase activity shows a 47% increase in activity relative to activity of the wild-type enzyme
A16V
naturally occuring ala16val polymorphism genotyping, overview
A4V
-
mutation causing familial amyotrophic lateral scerosis, 30% of wild-type activity, 1.06 atoms of copper and 1.43 atoms of zinc per subunit
C111S
site-directed mutagenesis, the mutant has 1.07 copper and 1.18 zinc per subunit
C140S
-
catalytic efficiency similar to wild-type, product inhibition is less than in wild-type
C140S/Q143A
-
catalysis does not follow Michaelis-Menten kinetics, substrate inhibition with KI-value of 0.06 mM
D124N
site-directed mutagenesis, the mutant has 0.93 copper and 0.03 zinc per subunit
D124N/C111S
site-directed mutagenesis, the mutant has 0.93 copper and 0.03 zinc per subunit
D83S
site-directed mutagenesis, the mutant has 0.93 copper and 0.08 zinc per subunit
D83S/C111S
site-directed mutagenesis, the mutant has 0.93 copper and 0.08 zinc per subunit
E100G
-
an amyotrophic lateral sclerosis-associated naturally occuring SOD mutant, misfolding/aggregation mechanism with folding and unfolding kinetics, overview
E93A
-
construction of transgenic mice overexpressing wild-type and mutant SOD1, biochemical changes occur in the hindlimb muscle of young, presymptomatic G93A hSOD1 transgenic mice, cdk5 activity is reduced in hindlimb muscle of 27-day-old G93A hSOD1 transgenic mice by suppression through the mutant E93A enzyme, phenotype, overview, mutant G93A SOD1 also suppresses muscle cdk5 activity in vitro
F50E/G51E
-
about 20% of wild-type activity, monomeric
F66A
site-directed mutagenesis, alteration of the active site surrounding, the mutant is 3fold less sensitive to product inhibition compared to the wild-type enzyme
F66L
site-directed mutagenesis, alteration of the active site surrounding, the mutant shows residual product inhibition with formation of a peroxide-inhibited enzyme and increased catalytic activity
G41N
-
Cu,Zn-SOD, site-directed mutagenesis, analogous to mutant found in familial amyotrophic lateral sclerosis, 47% activity compared to the wild-type
G93R
-
an amyotrophic lateral sclerosis-associated naturally occuring SOD mutant, misfolding/aggregation mechanism with folding and unfolding kinetics, overview
H46R
-
an amyotrophic lateral sclerosis-associated naturally occuring SOD mutant, misfolding/aggregation mechanism with folding and unfolding kinetics, overview
H63C
-
Cu,Zn-SOD, mutant with exchange of metal-bridging proton-donor His63 for Cys, binds Cu2+, but not Zn2+, 1% remaining activity compared to wild-type
H80S/D83S
site-directed mutagenesis, the mutant has 0.93 copper and 0.08 zinc per subunit
H80S/D83S/C6A/C111S
site-directed mutagenesis, the mutant has 1.07 copper and 1.18 zinc per subunit
N73S
-
ratio kcat/Km about twofold smaller than in wild-type, product inhibition similar to wild-type
N73S/C140S/Q143A
-
catalytic efficiency much smaller than wild-type, no appreciable product inhibition
N73S/Q143A
-
catalytic efficiency much smaller than wild-type, no appreciable product inhibition
Q143A
-
dramatically reduced product inhibition, reduced catalytic activity and efficiency
Y34F
-
about 12fold decrease in kcat value
D90A
-
Cu,Zn-SOD, mutant found in familial amyotrophic lateral sclerosis, activity similar compared to native and recombinant wild-type, but enhanced OH- generating activity, mutant is more sensitive to inhibition by copper-chelators
-
G41N
-
Cu,Zn-SOD, site-directed mutagenesis, analogous to mutant found in familial amyotrophic lateral sclerosis, 47% activity compared to the wild-type
-
G85R
-
Cu,Zn-SOD, site-directed mutagenesis, analogous to mutant found in familial amyotrophic lateral sclerosis, 99% activity compared to the wild-type
-
H43R
-
Cu,Zn-SOD, site-directed mutagenesis, analogous to mutant found in familial amyotrophic lateral sclerosis, 66% activity compared to the wild-type
-
H63C
-
Cu,Zn-SOD, mutant with exchange of metal-bridging proton-donor His63 for Cys, binds Cu2+, but not Zn2+, 1% remaining activity compared to wild-type
-
G93A
-
site-directed mutagenesis
H155Q
-
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
Y41F
-
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
Y88F
site-directed mutagenesis, substitution of Tyr88 to Phe does not affect the metal specificity of the enzyme
H30A
-
active site mutant, site-directed mutagenesis, activity, sensitivity to heat and inhibitors unchanged compared to wild-type
K170R
-
active site mutant, site-directed mutagenesis, unchanged activity, decreased thermal stability, more stable to 2,4,6-trinotrobenzenesulfonate than the wild-type, completely inactivated by phenylglyoxal
H30A
-
active site mutant, site-directed mutagenesis, activity, sensitivity to heat and inhibitors unchanged compared to wild-type
-
K170R
-
active site mutant, site-directed mutagenesis, unchanged activity, decreased thermal stability, more stable to 2,4,6-trinotrobenzenesulfonate than the wild-type, completely inactivated by phenylglyoxal
-
H171A
site-directed mutagenesis, the mutation changes the metal-binding specificity of the mutant enzyme from Mn to Fe. The alpha-helix content of mutant His171Ala is 59% suggesting that the mutant folds with a reasonable secondary structure. Mutant His171Ala exhibits a 39.6% higher activity than the wild-type. Mutant His171Ala is a Fe-SOD with Zn, Ni,and Fe contents of 180, 77, and 530 ng/mg, respectively. Mutant His171Ala exhibits a specific activity 39.6% higher than that of the wild type enzyme
H29A
site-directed mutagenesis, the mutation changes the metal-binding specificity of the mutant enzyme from Mn to Fe. The alpha-helix content of mutant His29Ala is 66% , suggesting that the mutant folds with a reasonable secondary structure. Mutant His29Ala shows an activity comparable to that of the wild-type. Zn, Ni, and Fe contents of the His29Ala enzyme mutant are 180, 76, and 300 ng/mg, respectively, and the amount of Fe is almost twice that of Zn and fourtimes that of Ni, suggesting that His29Ala mainly is a Fe-SOD. The mutant exhibits a specific activity comparable to that of the wild-type enzyme
H84A
site-directed mutagenesis, the mutant exhibits a specific activity comparable to that of the wild-type enzyme
P143S/P145L
site-directed mutagenesis, gain-of-function, the mutant shows increased activirty compared to the wild-type SOD1
P143S/P145L
-
site-directed mutagenesis, gain-of-function, the mutant shows increased activirty compared to the wild-type SOD1
-
Y34F
-
the mutant shows metalcofactor kinetics similar to the human not the Deinococcus radiodurans Mn-SOD, formation of human-like Mn3+SOD and human-like Mn3+SOD-O2 - adduct, overview
Y34F
unlike wild-type, F- binding is retained at high pH-values. N3- inhibitis Y34F with a 20fold lower KI-value than for wild-type
D90A
-
Cu,Zn-SOD, mutant found in familial amyotrophic lateral sclerosis, activity similar compared to native and recombinant wild-type, but enhanced OH- generating activity, mutant is more sensitive to inhibition by copper-chelators
D90A
-
mutant related to amyothrophic lateral sclerosis, improvement of expression by coexpression with yeast copper chaperone
G85R
-
Cu,Zn-SOD, site-directed mutagenesis, analogous to mutant found in familial amyotrophic lateral sclerosis, 99% activity compared to the wild-type
G85R
-
an amyotrophic lateral sclerosis-associated naturally occuring SOD mutant, misfolding/aggregation mechanism with folding and unfolding kinetics, overview
G93A
-
mutant related to amyothrophic lateral sclerosis, improvement of expression by coexpression with yeast copper chaperone
G93A
-
an amyotrophic lateral sclerosis-associated naturally occuring SOD mutant, misfolding/aggregation mechanism with folding and unfolding kinetics, overview
G93A
-
naturally occuring mutation, mutant SOD1-induced cytotoxicity protection
H43R
-
Cu,Zn-SOD, site-directed mutagenesis, analogous to mutant found in familial amyotrophic lateral sclerosis, 66% activity compared to the wild-type
H43R
-
mutation causing familial amyotrophic lateral scerosis, 59% of wild-type activity, 1.4 atoms of copper and 1.11 atoms of zinc per subunit
R213G
-
site-directed mutagenesis, mutant mice with R213G knock-in mutation, a human single nucleotide polymorphism leading to reduced binding EcSOD in peripheral organs, exacerbate the organ damages. Phenotype, overview
R213G
-
site-directed mutagenesis, mutant mice with R213G knock-in mutation, a human single nucleotide polymorphism leading to reduced binding EcSOD in peripheral organs, exacerbate the organ damages. Phenotype, overview
-
additional information
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generation of a highly thermostable and stress tolerant superoxide dismutase by N-terminal modification and metal incorporation engineering. Recombinant wild-type enzyme SODAp and NTD-fused N-terminal domain ntdSODAp are incorporated with metal cofactors by two ways: the Fe2+- and Mn2+-contained SODs are obtained by in vivo modification (Mn-med SODAp and ntdSODAp) and in vitro reconstitution (Mn-rec SODAp and ntdSODAp), respectively
additional information
construction of two mutant strains KO1 and KOS, lacking either sodA-1 or both sodA-1 and sodA-2, through homologous recombination
additional information
construction of two mutant strains KO1 and KOS, lacking either sodA-1 or both sodA-1 and sodA-2, through homologous recombination
additional information
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construction of two mutant strains KO1 and KOS, lacking either sodA-1 or both sodA-1 and sodA-2, through homologous recombination
additional information
construction of two mutant strains KO2 and KOS, lacking either sodA-2 or both sodA-1 and sodA-2, through homologous recombination
additional information
construction of two mutant strains KO2 and KOS, lacking either sodA-2 or both sodA-1 and sodA-2, through homologous recombination
additional information
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construction of two mutant strains KO2 and KOS, lacking either sodA-2 or both sodA-1 and sodA-2, through homologous recombination
additional information
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construction of two mutant strains KO2 and KOS, lacking either sodA-2 or both sodA-1 and sodA-2, through homologous recombination
-
additional information
-
construction of two mutant strains KO1 and KOS, lacking either sodA-1 or both sodA-1 and sodA-2, through homologous recombination
-
additional information
construction of a chimeric SOD1 mutant fused to Saccharomyces cerevisiae superoxide dismutase 1 copper chaperone-fusion enzyme, Lys7, the chimeric mutant SOD1-Lys7 shows increased activirty compared to the wild-type SOD1 and SOD1 mutant P143S/P145L
additional information
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construction of a chimeric SOD1 mutant fused to Saccharomyces cerevisiae superoxide dismutase 1 copper chaperone-fusion enzyme, Lys7, the chimeric mutant SOD1-Lys7 shows increased activirty compared to the wild-type SOD1 and SOD1 mutant P143S/P145L
-
additional information
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chemical modification of the enzyme with linoleic and alpha-linolenic acids using two different methods leads to higher retained enzymatic activity compared with SOD modified by macromolecular substances. Enhanced heat stability, acid and alkali resistance, and anti-pepsin/trypsin ability of the modified SOD are observed and compared to those of the natural enzyme, the apparent oil-water partition coefficient of the modified enzyme is especially increased, overview
additional information
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enzyme null mutant cell is not sensitive to H2O2, 3-morpholinosydnonimine, or paraquat challenge, but is killed by exogenous superoxide generated by the xanthine/xanthine oxidase method
additional information
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construction of a sodC null mutant strain KEK1, which is not sensitive to a H2O2, 3-morpholinosydnonimine, or paraquat challenge, but is killed by exogenous superoxide generated by the xanthine/xanthine oxidase method. The sodC mutant also exhibits a growth defect in liquid medium compared to the parental strain, which can be complemented in trans. The mutant organism is killed more rapidly than the parental strain in murine macrophage-like cell line RAW 264.7, but killing is eliminated when macrophages are treated with an NADPH oxidase inhibitor, overview
additional information
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enzyme null mutant cell is not sensitive to H2O2, 3-morpholinosydnonimine, or paraquat challenge, but is killed by exogenous superoxide generated by the xanthine/xanthine oxidase method
-
additional information
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construction of a sodC null mutant strain KEK1, which is not sensitive to a H2O2, 3-morpholinosydnonimine, or paraquat challenge, but is killed by exogenous superoxide generated by the xanthine/xanthine oxidase method. The sodC mutant also exhibits a growth defect in liquid medium compared to the parental strain, which can be complemented in trans. The mutant organism is killed more rapidly than the parental strain in murine macrophage-like cell line RAW 264.7, but killing is eliminated when macrophages are treated with an NADPH oxidase inhibitor, overview
-
additional information
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Cu,Zn-enzyme disruption mutant, no Cu,Zn-dependent activity, increase in Fe-dependent activity by 30-40%. Under illuminated conditions, 60% reduction of cell survival rate compared to wild type
additional information
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strains with mutations in the enzyme gene SOD2 exhibit increased susceptibility to oxidative stress as well as poor growth at elevated temperature
additional information
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naturally occuring hybrids between Fe-SOD and Mn-SOD, altered metal content
additional information
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naturally occuring hybrids between Fe-SOD and Mn-SOD, altered metal content
additional information
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naturally occuring hybrids between Fe-SOD and Mn-SOD, altered metal content
-
additional information
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naturally occuring hybrids between Fe-SOD and Mn-SOD, altered metal content
-
additional information
construction of a fusion protein between the N-terminal domain of superoxide dismutase from Geobacillus thermodenitrificans NG80-2 and superoxide dismutase from Sulfolobus solfataricus. 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. The N-terminal domain is a good candidate for improving stability of both mesophilic and thermophilic superoxide dismutase from either bacteria or archaea via simple genetic manipulation
additional information
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construction of a fusion protein between the N-terminal domain of superoxide dismutase from Geobacillus thermodenitrificans NG80-2 and superoxide dismutase from Sulfolobus solfataricus. 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. The N-terminal domain is a good candidate for improving stability of both mesophilic and thermophilic superoxide dismutase from either bacteria or archaea via simple genetic manipulation
-
additional information
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replacement of all of the nine tyosine residues in each of the four enzyme subunits by 3-fluorotyrosine. Crystal structures of unfluorinated and fluorinated enzyme are nearly superimposable. Ratio kcat/Km decreases from 0.8 per mM and s for wild-type to 0.03 per mM and s for the fluorinated mutant which is in significant part due to 3-fluorotyrosine residues distant from the active-site metal
additional information
construction of a zinc-deficient enzyme, structure analysis, the loss of zinc from SOD is potentially important for both the aggregation and zinc-deficient Cu,Zn-SOD hypotheses, and leads to an altered dimer, phenotypes, overview
additional information
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construction of a zinc-deficient enzyme, structure analysis, the loss of zinc from SOD is potentially important for both the aggregation and zinc-deficient Cu,Zn-SOD hypotheses, and leads to an altered dimer, phenotypes, overview
additional information
-
the recombinant SOD is cvalently linked to lecithin, which increases its half-life after administration to humans
additional information
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deletion analysis of the key DNA binding elements in the SOD-1 gene promoter identifies the distal hypoxia response element, but not the peroxisome proliferator response element or nuclear factor-kappaB element, as essential for the suppressive effects of docosahexaenoic acid
additional information
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engineering of a novel chimera of human Mn-SOD and Vitreoscilla hemoglobin, i.e. MnSOD-VHb, for rapid detoxification of reactive oxygen species, the recombinant bifunctional enzyme possesses MnSOD and peroxidase-like activities. The greater antioxidant capability is possibly due to the close proximity between the active site of MnSOD and the heme moiety of VHb, synergistic functions of SOD and peroxidase, overview
additional information
generation of a catalytically active truncated (residues 19-240) mutant form of human EC-SOD (hEC-SOD)
additional information
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generation of a catalytically active truncated (residues 19-240) mutant form of human EC-SOD (hEC-SOD)
additional information
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the mutant enzymes lacking the glutamate and lysine residues close to the active site can be a competent superoxide reductase
additional information
overexpression of recombinant Cu/Zn-SOD1 in strain L3 does not significantly increase the SOD specific activity, and in some cases, a net reduction of the enzymatic activity occurs, cell phenotypes, overview
additional information
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overexpression of recombinant Cu/Zn-SOD1 in strain L3 does not significantly increase the SOD specific activity, and in some cases, a net reduction of the enzymatic activity occurs, cell phenotypes, overview
additional information
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overexpression of recombinant Cu/Zn-SOD1 in strain L3 does not significantly increase the SOD specific activity, and in some cases, a net reduction of the enzymatic activity occurs, cell phenotypes, overview
-
additional information
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hyaluronan levels are increased in the bronchoalveolar lavage fluid after asbestos-induced pulmonary injury, and this response is markedly enhanced in EC-SOD knock-out mice, overview
additional information
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phenotype of homozygous LDL-receptor-knockout mice, heterozygous ob/+, and wild-type C57BL6 mice, overview
additional information
the recombinant pea chloroplastic SOD possesses nearly 6fold higher superoxide dismutase activity and 5fold higher peroxidase activity as compared to commercially available CuZn-superoxide dismutase from Bos taurus. The recombinant protein harbors all the characteristics features of this class of enzyme. The recombinant enzyme is exceptionally stable concerning pH and temperature and maintains its activity upon prolonged storage
additional information
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the recombinant pea chloroplastic SOD possesses nearly 6fold higher superoxide dismutase activity and 5fold higher peroxidase activity as compared to commercially available CuZn-superoxide dismutase from Bos taurus. The recombinant protein harbors all the characteristics features of this class of enzyme. The recombinant enzyme is exceptionally stable concerning pH and temperature and maintains its activity upon prolonged storage
additional information
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construction of an enzyme-deletion mutant, the mutant strain is less virulent in mice than the wild-type strain or the complemented strain, overview
additional information
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construction of mutants of strain PAO1 lacking manganese-SOD, iron-SOD, or both, the mutants are injected into the hemocoel of Bombyx mori, the virulence decreases in the order: wild-type PAO1, manganese-SOD deficient PAO1, iron-SOD deficient PAO1, and double mutant PAO1, which is avirulent at a dose of 105 cells or less, the virulence of the double mutant can be partially restored by expression of a wild-type enzyme variant, overview
additional information
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construction of mutants of Pseudomonas putida lacking manganese-superoxide dismutase MnSOD, iron-superoxide dismutase FeSOD, or both, phenotypes, overview, the sodA sodB mutant does not grow on components washed from bean root surfaces or glucose in minimal medium, the sodB and sodA sodB mutants are more sensitive than wild-type to oxidative stress generated within the cell by paraquat treatment
additional information
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
additional information
-
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
additional information
-
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
-
additional information
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naturally occuring exchange of Arg-189 for Lys in the active site of Mn-SOD, sensitivity to lysine-modifying agents
additional information
the enzyme is not significantly modified in light mitochondrial (LMF) fractions by any treatment
additional information
the enzyme is not significantly modified in light mitochondrial (LMF) fractions by any treatment
additional information
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polysialylation of SOD, method development and optimization, overview. Optimal conditions for the cross-linking reaction are the ratio of polysialic acid and SOD of 40:1 with a reaction time of 24 h. Under this condition, the average cross-linking ratio is 3.9 and average molecular weight was 95 kDa derived from the molecular weight of polysialic acid with 16.2 kDa and CuZn-SOD with 32 kDa. The molecular size of the polysialylated enzyme was about 90-100 kDa, enhancement of hydratability of SOD through polysialylation, analysis by atomic force microscopy, overview
additional information
structure models of three enzyme mutants His29Ala, His84Ala, and His171Ala, overview
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0 - 50
-
purified native enzyme, stable for 120 min
10 - 50
purified recombinant enzyme, 10 min, 83% activity within this range remaining
107
the denaturation temperature of the enzyme is 107.3°C
107.3
denaturing temperature
15 - 90
-
temperature stability profile, overview
20 - 40
recombinant enzyme, 1 h, about 90% activity remaining, completely stable for 45 min
20 - 90
secondary structure of SOD_ASAC is stable within this temperature range
22 - 50
-
purified Cu,Zn-SOD, completely stable
25
purified recombinant enzyme, 120 min, completely stable
25 - 45
-
stable for 90 min, unstable above
25 - 75
purified recombinant His-tagged enzyme, no significant change in enzyme activity at 25-45°C for up to 1 h, at 75°C, 60% of enzyme activity is retained after 1 h of treatment, suggesting that the SaCSD1 is relatively thermostable
25 - 90
-
the recombinant enzyme retains more than 80% activity between 10°C and 60°C, but loses activity rapidly, which is reduced to 54% and 40% at 70°C and 80°C, respectively, and it is almost inactive at 90°C
30 - 37
purified recombinant His-tagged enzyme, 60 min, stable
30 - 50
purified enzyme mutants H29A and H171A, 30 min, stable
30 - 60
about 80% activity remaining after 60 min
35
-
pH 7.0, stable below, inactivation above
4 - 50
purified enzyme, 60 min, completely stable
4 - 70
the recombinant purified enzyme is fairly stable at 4°C and 37°C, but is rapidly inactivated at 50°C and 70°C
40 - 90
over 50% activity within this range, most stable at 70°C, profile overview
44.5
purified recombinant His-tagged enzyme, 60 min, loss of 50% activity
5 - 50
-
purified isozyme SODI, stable
50 - 70
-
purified isozyme SODI, inactivation, thermal inactivation of wheat seedling MnSOD follows first-order reaction kinetics, and the temperature dependence of rate constants is in agreement with the Arrhenius equation
57
purified recombinant enzyme, loss of over 50% activity
62
t1/2, purified recombinant His-tagged enzyme, 20-60 min
70 - 110
-
recombinant N-terminal domain of the enzyme SOD obtained by in vitro reconstitution (Mn-rec ntdSODAp) exhibits improved optimum temperature at 70°C and dramatically enhanced thermostability especially at 110°C with enhanced pH stability from pH 4 to pH 10
70.45
midpoint of thermal transition (Tm)
71 - 73
-
half-inactivation occurring after 10 min exposure at 71-73°C, depending on the bound metal
75.8
-
melting temperature of holoenzyme
80 - 90
-
purified recombinant enzyme, 60 min, stable
100
-
recombinant wild-type enzyme SODAp retains 44&% of maximal activity, while recombinant Mn-rec ntdSODAp N-termina domain retains 58% activity
100
purified recombinant His-tagged enzyme, 5% activity remaining after 1 h, inactivation after 2 h
100
-
purified enzyme, loss of 5% activity after 10 min boiling for the chloroplast enzyme and 35% for the cytosolic enzyme, after 1 h, 70% remaining activity, of the leaf enzyme, 20% of the rhizome enzyme
100
-
purified enzyme, strong stability at pH 6.0-7.0, the enzyme survives boiling for 10 min without losing more than 60% of activity
100
purified recombinant enzyme, 60 min, loss of 70% activity
100
-
60 min, complete loss of activity
100
-
4 min, purified enzyme, inactivation
100
-
complete loss of activity
100
the Mn2+-reconstituted recombinant enzyme is not inactivated at all after 5 h of incubation at 100°C. A 1 h incubation leads to a 50% decrease in the activity of the Fe2+-reconstituted enzyme
100
-
purified recombinant enzyme, complete inactivation after 30 min
100
purified recombinant enzyme, half-life is 8.7 h, inactivation according to first order kinetics
100
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
100
-
purified recombinant enzyme, 57% activity remaining activity after 60 min, half-life is about 70 min
105
5 h, no loss of activity
105
purified recombinant enzyme, half-life is 1.5 h, inactivation according to first order kinetics
105
half-life 2.1 h for wild-type, 5.7 h for fusion protein with the N-terminal domain of superoxide dismutase from Geobacillus thermodenitrificans NG80-2
110
5 h, 44% loss of activity
110
purified recombinant enzyme, loss of 80% activity after 10 min, and inactivation after 20 min
110
-
purified recombinant enzyme, 20% activity remaining activity after 30 min
121
Cj-Cu,Zn SOD retains 50% of the maximum activity after autoclaving, autoclaved Ca-Cu,Zn SOD exhibits 40% of maximum activity of unautoclaved enzyme at 20°C and 30°C. Thermal inactivation kinetics of Ca-Cu,Zn SOD, overview
121
Ca-Cu Z- SOD retains 50% of the maximum activity after autoclaving, autoclaved Ca-Cu,Zn SOD exhibits 40% of maximum activity of unautoclaved enzyme at 20°C and 30°C. Thermal inactivation kinetics of Ca-Cu,Zn SOD, overview
37
purified recombinant His-tagged enzyme, 48 h, over 80% activity remaining
37
-
wild-type, purified stable for at least 1 week
4
-
Mn-SOD, complete loss of activity after 7 days
4
-
25% loss of activity after 4 months
40
-
1 h, about 20% loss of activity
40
-
and below, completely stable
40
-
purified enzyme, completely stable after 20 min, after 1 h, 98% remaining activity of the leaf enzyme, 88% of the rhizome enzyme
40
-
60 min, 40% loss of activity
40
-
60 min, 40% loss of activity
40
-
60 min, 40% loss of activity
40
-
60 min, 40% loss of activity
40
and below, 30 min, purified recombinant enzyme, completely stable
40
30 min, purified enzyme, 50% activity remaining
40
-
60 min, 40% loss of activity
40
-
60 min, 40% loss of activity
40
-
pH 7.0, stable up to, rapidly inactivated above
40
-
60 min, 40% loss of activity
40
purified recombinant His-tagged enzyme, 40 min, 82.2% activity remains
40
-
pH 7.8, half-life: 70 min, isoenzyme I, 177 min, isoenzyme II
40
-
purified enzyme, 90 min, completely stable, 90% activity remaining after 120 min
40
-
60 min, 40% loss of activity
45
purified recombinant His-tagged enzyme, 40 min, 50% activity remaining
45
-
stable up to 45°C for 1 h
45
purified recombinant His-tagged enzyme, completely stable at, 60 min
45
Radix lethospermi
-
pH 7.8, stable up to 30 min
50
-
1 h, about 55% loss of activity
50
or below, pH 7.0, stable for at least 30 min
50
purified recombinant His-tagged enzyme, completely stable for 6 h, after 48 h 30% activity remaining
50
-
melting temperature of apoenzyme
50
4 h, pH 7.8, 80% residual activity
50
stable for at least 90 min, rapid inactivation above
50
purified recombinant enzyme, stable
50
highly thermostable at
50
purified recombinant enzyme, 1 h, stable at
50
-
loss of 40% activity after 60 min
50
Megalodesulfovibrio gigas
-
1 h, stable
50
-
30 min, purified enzyme, completely stable
50
-
40 min, 50% loss of activity
50
purified recombinant His-tagged enzyme, 40 min, 59.4% activity remains
50
-
88.5% remaining activity after 1 h
50
recombinant enzyme, 1 h, 80% activity remaining
50
-
purified native enzyme, more than 85% of its initial activity is retained after 1 h of incubation. The enzyme is highly stable at temperatures below 50°C
50
-
purified recombinant His-tagged enzyme, 1 h, 78% activity remaining
50
-
purified enzyme, 30 min, 90% activity remaining, 80% after 120 min
50
purified native enzyme, 60 min, completely stable
50 - 60
purified recombinant His-tagged enzyme, 60 min, over 80% activity remaining
50 - 60
purified recombinant enzyme, stable
50 - 60
Thermochaetoides thermophila
-
purified enzyme, completely stable
50 - 60
Thermochaetoides thermophila
purified recombinant enzyme, 60 min, stable
55
-
10 min, about 45% loss of activity, 30 min, 75% loss of activity
55
-
70% loss of activity after preexposure
55
23 min, 50% residual activity
60
-
10 min, about 75% loss of activity
60
-
30 min, 53% remaining activity
60
-
5 min, complete inactivation of isoenzyme B, 50% loss of isoenzyme A activity
60
90 min, 10% residual activity
60
-
purified enzyme, completely stable after 20 min, after 1 h, 90% remaining activity of the leaf enzyme, 70% of the rhizome enzyme
60
10 min, 65% residual activity
60
-
21.2 min, loss of 50% activity
60
-
30 min, purified enzyme, 73% remaining activity
60
purified enzyme, 60 min, loss of 20% activity
60
purified recombinant enzyme, loss of 50% activity after 20 min, of about 85% activity after 100 min, and inactivation after 120 min
60
-
5 min, 50% loss of activity
60
recombinant enzyme, 1 h, 60% activity remaining
60
-
purified native enzyme, 45% of its initial activity is retained after 1 h of incubation
60
-
pH 7. 8, half-life: 5 min, isoenzyme I, 34 min, isoenzyme II
60
-
purified enzyme, 120 min, 30% activity
60
-
purified native enzyme, loss of 50% activity after 120 min
60
purified native enzyme, 95% remaining activity after 60 min
60
Thermochaetoides thermophila
the puurified recombinant enzyme retains 93% of maximal activity after 60 min
60 - 70
-
the purified enzyme is quite stable
60 - 70
purified recombinant His-tagged enzyme, more than 73% activity remains after 30 min. The residual activity declines sharply from 73.07% to 28.75% between 60°C and 70°C, T1/2 is 63°C
65
-
purified enzyme, half-life is 110 min
65
half-life of 14.7 min, thermal inactivation rate constant Kd of 0.0321 per min
70
-
recombinant Cu,Zn-SOD, after 2 h 20% activity remaining, after 3 h all activity is lost
70
-
loss of activity after 30 min, Cu,Zn-SOD
70
-
loss of activity after 30 min, Cu,Zn-SOD
70
-
loss of activity after 30 min, Cu,Zn-SOD
70
-
loss of activity after 30 min, Cu,Zn-SOD
70
purified recombinant His-tagged enzyme, 20% activity remaining after 1 h, inactivation after 3 h
70
purified recombinant His-tagged enzyme, 60 min, loss of 96% activity
70
-
half-life: 12.75 min
70
-
10 min, 40% residual activity
70
purified recombinant enzyme, half-life is 48 min
70
-
5 min, complete loss of activity
70
-
40 min, 40% loss of activity
70
50% activity remaining after 30 min, inactivation after 60 min
70
purified recombinant His-tagged enzyme, 60 min, 54% activity remaining
70
-
10 min, purified enzyme, 46% remaining activity, inactivation after 20 min
70
purified enzyme, 60 min, inactivation
70
-
purified native enzyme exhibits high thermal stability at 70°C over the pH range from pH 4.0 to pH 9.0, with 96.2% activity remaining after 40 min, 88.2% after 60 min at pH 7.4
70
purified recombinant His-tagged enzyme, 20 min, almost no activity remains
70
-
complete loss of activity after 40 min
70
-
12 h, purified recombinant enzyme, 90% remaining activity
70
recombinant enzyme, 1 h, 20% activity remaining
70
-
purified native enzyme, 37% of its initial activity is retained after 1 h of incubation
70
-
purified Cu,Zn-SOD, complete inactivation
70
-
purified enzyme, 90 min, inactivation
70
-
purified native enzyme, loss of 70% activity after 120 min
70
purified native enzyme, 55% remaining activity after 60 min
70
purified recombinant enzyme, 65% remaining activity after 60 min
70
Thermochaetoides thermophila
-
60 min, 60% activity remaining
70
Thermochaetoides thermophila
purified recombinant enzyme, retains 65% of the maximum activity at 70°C for 60 min
70
Thermochaetoides thermophila
purified recombinant enzyme, 60 min, 75% activity remaining
70
-
60 min, 55% residual activity
70
purified enzyme mutants H29A and H171A, 30 min, retain 51% and 36.7% activity, respectively, mutant H29A retains 20% activity after 1 h, half-lives of SOD activity for His171Ala and His29Ala mutants are 33 and 15 min
70 - 80
-
purified enzyme, 30-45 min, irreversible thermoinactivation
70 - 80
-
the initial activities of the polysialyated enzyme show 35-55% higher than those of the native enzyme after incubation at 70°C, and 31-45% at 80°C, the native enzyme is almost inactivated after incubation for 3 h, while the polysialylated SOD still has 49-61% residual activities
75
-
total loss of activity
75
-
loss of 66% activity
75
-
purified enzyme, half-life is 22 min
75
purified recombinant His-tagged enzyme, 20 min, inactivation
75
-
native wild-type enzyme: half-life 4.7 h, recombinant wild-type enzyme: half-life: 2.8 h, recombinant mutant H30A: half-life 2.7 h, recombinant mutant K170R half-life 0.36 h
75
purified recombinant enzyme, inactivation
80
purified recombinant enzyme, 66 h, 50% activity remaining
80
-
purified enzyme, half-life is 9.8-20.8 min
80
recombinant enzyme SOD Cj-Cu,Zn SOD shows a residual SOD activity of 26.07% after being heated for 160 min
80
-
purified enzyme, completely stable after 20 min, after 1 h, 80% remaining activity of the leaf enzyme, 52% of the rhizome enzyme
80
purified recombinant enzyme, 48% remaining activity after 10 min
80
purified recombinant enzyme, 60 min, completely stable
80
purified recombinant enzyme, 1 h, 64% activity remaining
80
-
10 min, purified enzyme, 13% remaining activity, inactivation after 15 min
80
-
purified native enzyme, with 71.1% activity remaining after 10 min at pH 7.4
80
15 min, more than 95% stable, 75 min, more than 80% stable
80
-
purified recombinant enzyme, 40% remaining activity after 30 min, complete inactivation after 4 h
80
-
purified native enzyme, inactivation after 90 min
80
purified native enzyme, inactivation after 60 min
80
purified recombinant enzyme, half-life is about 40 min
80
Thermochaetoides thermophila
-
half-life of the purified enzyme is about 25 min
80
Thermochaetoides thermophila
purified recombinant enzyme, half-life is 22 min
80
Thermochaetoides thermophila
purified recombinant enzyme, 25 min, 50% activity remaining
80
-
28 min, 50% residual activity
80
mutant H171A retains 20% activity after 1 h
80
-
3 h, retains 85% of activity
80
purified recombinant enzyme, 1 h, 90% activity remaining
85
the enzyme is stable in aqueous solution at temperatures up to 85°C
85
-
30 min, 15% remaining activity
85
15 min, more than 95% stable, 75 min, more than 80% stable
90
dimer: half-life 99 min, dimeric form is more stable than monomeric form
90
purified recombinant enzyme, inactivation after 10 min
90
purified recombinant enzyme, 60 min, loss of 20% activity
90
purified recombinant enzyme, 1 h, 57% activity remaining
90
purified recombinant enzyme, 57% activity remaining after incubation for 1 h
90
purified recombinant enzyme, 10 min, inactivation
90
-
5 min, purified enzyme, inactivation
90
-
nectarin I: Mn-SOD, 85% remaining activity after 1 h
90
-
purified native enzyme, with 67.8% activity remaining after 10 min at pH 7.4
90
45 min, less than 10% of initial activity
90
-
complete loss of activity after 5 min
90
-
purified recombinant enzyme, 10% remaining activity after 30 min
90
purified native enzyme, inactivation after 50 min
90
purified recombinant enzyme, 20% remaining activity after 50 min
90
Thermochaetoides thermophila
-
purified enzyme, 30 min, 20% activity remaining
90
Thermochaetoides thermophila
purified recombinant enzyme, half-life is 7 min
90
Thermochaetoides thermophila
purified recombinant enzyme, 30 min, 20% activity remaining
90
-
20 min, 20% residual activity
90
purified recombinant enzyme, 1 h, 70% activity remaining
95
60 min, less than 10% of initial activity
95
2 h, purified recombinant enzyme, 96% remaining activity, half-life is 33 h, inactivation according to first order kinetics
95
purified enzyme, half-life is 48 h or above
95
-
10 min, stable up to
95
-
2 h, retains 50% of activity
95
purified recombinant enzyme, 4.68 h, 50% activity remaining
additional information
thermal stability and activity of the enzyme directly depends on the nature of the reconstituted metal and the degree of saturation of binding sites
additional information
-
thermal stability and activity of the enzyme directly depends on the nature of the reconstituted metal and the degree of saturation of binding sites
additional information
an increased net negative charge on the surface of asFeSOD may explain its lower thermostability compared to the enzyme from Escherichia coli, structure-thermostability relationship, overview
additional information
-
an increased net negative charge on the surface of asFeSOD may explain its lower thermostability compared to the enzyme from Escherichia coli, structure-thermostability relationship, overview
additional information
-
a highly thermostable enzyme, occurrence of an additional sulfur-containing hydrogen bond involving the M110 residue and the effect of the A138 residue on the backbone entropy
additional information
-
SODI displays a Tm value of 54°C and therefore its structure is rather labile to temperature
additional information
SODI displays a Tm value of 54°C and therefore its structure is rather labile to temperature
additional information
-
SODII displays a Tm value of 80°C and therefore its structure is rather stable to temperature
additional information
SODII displays a Tm value of 80°C and therefore its structure is rather stable to temperature
additional information
-
the enzyme is remarkably stable at high temperatures
additional information
circular dichroic spectroscopy analysis confirms the thermostable nature of Cj-Cu,Zn SOD. Thermal inactivation first-order kinetics
additional information
thermal inactivation kinetics fit the first-order inactivation rate equation, recombinant enzyme
additional information
-
thermal inactivation kinetics fit the first-order inactivation rate equation, recombinant enzyme
additional information
-
two protein denaturation peaks at 65°C and 84°C by differential scanning calorimetry
additional information
-
high thermostability
additional information
-
comparison of thermostability of various Gluconobacter strains
additional information
-
a higher thermostable enzyme
additional information
-
activation energy for enzyme thermal denaturation, 143.5 kJ per mol
additional information
-
a highly thermostable enzyme
additional information
Photobacterium sepia
-
a highly thermostable enzyme
additional information
-
thermal stability of Mn-SOD at several temperatures, enzyme is more labile at higher temperatures
additional information
-
-
additional information
phenylmethanesulfonyl fluoride attachment to the active site Tyr41 increases the heat stability of the enzyme, overview
additional information
-
phenylmethanesulfonyl fluoride attachment to the active site Tyr41 increases the heat stability of the enzyme, overview
additional information
-
a thermostable enzyme
additional information
-
due to its extraordinary heat stability, unfolding dynamics of this protein cannot be investigated by conventional physical methods below 100°C
additional information
due to its extraordinary heat stability, unfolding dynamics of this protein cannot be investigated by conventional physical methods below 100°C
additional information
Thermochaetoides thermophila
an increased number of charged residues and an increase in the number of intersubunit salt bridges and the Thr:Ser ratio compared to enzymes from other species are identified as potential reasons for the thermostability of CtMnSOD
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2 forms, 1 dimer and 1 monomer
2 isoenzymes: superoxide dismutase I and II
-
3 electromorphs: AA, BB, AB
-
3 isoenzymes of anaero-SOD and 3 isoenzymes of aero-SOD
-
3 isoenzymes: 1, 2 and 3
-
after overexpression in Escherichia coli
allozyme variants: DSDS and DSDF
-
analytical isolation of the enzyme in a 2D electrophoresis from strains KT2440 and PAO1, overview
-
both isozymes SODI, SODII
-
Cu,Zn-SOD from erythrocytes
-
Cu,Zn-SOD from shoots and cotyledons
-
Cu,Zn-SOD wild-type and mutant recombinant from Escherichia coli
-
Cu,Zn-SOD, amino acid analysis
-
Cu,Zn-SOD, native and recombinant from Pichia pastoris
Cu,Zn-SOD, recombinant from Escherichia coli and native enzyme
-
Cu,Zn-SOD, wild-type and mutants recombinant from Spodoptera frugiperda cells
-
Cu/Zn-SOD from digestive gland and gills
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, recombinant His6-and thioredoxin-tagged enzyme from Escherichia coli, 12.2fold by two steps of nickel affinity chromatography and desalting gel filtration
EC-SOD recombinant from Escherichia coli as His-tagged protein and partially from insect cells
-
enzyme is stable under aerobic conditions
-
Fe-SOD and reconstructed Fe-/Mn-SOD
four isozymes by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration. SODI is purified 424fold, SODII 635fold, SODIII 336fold, and SODIV 489fold
-
intermediate between Fe- and Mn-SOD, contains Zn2+ as well
-
large scale immunoisolation of native mutant and wildtype SOD1
-
Mn-SOD recombinant from Escherichia coli
native Cu,Zn-SOD 6.1fold from mycelial extracts
-
native Cu,Zn-SOD about 13fold by two steps of hydrophobic interaction chromatography and two steps of anion exchange chromatography
-
native Cu/Zn-SOD and Mn-SOD partially by subcellular fractionation, further purfication of mitochondrial Cu/Zn-SOD by anion exchange chromatography and, for analysis, by RP-HPLC
-
native EC-SOD from mouse lungs by hyaluronic acid affinity chromatography
-
native enzyme 115fold by heat treatment at 60°C for 10 min, gel filtration, anion exchange and hydrophobic interaction chromatography
native enzyme 28.5fold from strain NBIMCC 1984 by thermal treatment, dialysis, ion exchange chromatography, and chromatofocusing
-
native enzyme 308.5fold by ammonium sulfate precipitation, cation and anion ion exchange chromatography, and gel filtration
-
native enzyme 3fold from roots by ammonium sulfate fractionation and anion exchange chromatography
-
native enzyme 50fold from strain OS-77 by hydrophobic interaction and anion exchange chromatography, followed by gel filtration
-
native enzyme 61.5fold by ammonium sulfate fractionation, anion exchange chromatography, gel filtration, hydrophobic interaction chromatography and again gel filtration, to homogeneity
-
native enzyme 7.49fold to homogeneity by ammonium sulfate fractionation, anion exchange chromatography, and hydrophobic interaction chromatography
Thermochaetoides thermophila
-
native enzyme by ammonium sulfate fractionation, ion exchange chromatography, and gel filtration
-
native enzyme from bulbs by ammonium sulfate fractionation, dialysis, gel filtration, and anion exchange chromatography
-
native enzyme from hepatopancreas 6781fold by anion exchange chromatography and gel filtration
native enzyme from leaves to apparent homogeneity
-
native enzyme from mitochondrial intermembrane space of livber microsomes
-
native enzyme from plants 13.7fold by ammonium sulfate fractionation, cation and anion exchange chromatography, and gel filtration
-
native enzyme from post-ribosomal supernatant by anion exchange, hydrophobic interaction, and hydroxyapatite chromatography, followed by gel filtration, to homogeneity
-
native enzyme from sardinelle viscera to homogeneity 7.17fold by heat treatment at 65°C for 15 min, ammonium sulfate fractionation, and gel filtration
-
native enzyme from sperm 7.5-38fold, superoxide dismutase release from spermatozoa after cold shock and homogenization, followed by ion exchange chromatography and gel filtration
-
native enzyme from tubers/roots 3fold by ammonium sulfate fractionation and anion exchange chromatography
-
native enzyme to homogeneity
-
native enzyme to homogeneity by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography
native enzyme, and recombinant enzyme from Escherichia coli strain JM109(DE3)
native extracellular enzyme to homogeneity from the culture medium by ultrafiltration, gel filtration, dialysis, and anion exchange chromatography
-
native isozyme SODI by 23fold gel filtration, hydrophobic interaction chromatography, and anion-exchange chromatography
native isozyme SODII by 153fold gel filtration, hydrophobic interaction chromatography, and anion-exchange chromatography to homogeneity
native isozymes SODI and SODII 154fold and 98fold, respectively, from seedlings by heat treatment at 40°C for 15 min, ammonium sulfate fractionation, anionic exchange chromatography, and gel filtration
-
native peroxisomal Mn-SOD 5600fold from peroxisomal membranes, to homogeneity by ammonium sulfate fractionation, batch anion-exchange chromatography, and anion-exchange and gel filtration, mitochondrial Mn-SOD partially
nectarin I: Mn-SOD from nectar
-
overview: purification of extracellular superoxide dismutases
purification of extracellular enzyme Fe-SOD 101.62fold from human blood serum by anion exchange chromatography and gel filtration
-
purification of extracellular enzyme Fe-SOD 103.73fold from human blood serum by anion exchange chromatography and gel filtration
-
recombinant chimera MnSOD-VHb from Escherichia coli strain BL21(DE3)
-
recombinant Cu, ZnSOD from Pichia pastoris strain GS115 by anion exchange chromatography
Thermochaetoides thermophila
recombinant Cu,ZnSOD from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, cleavage of the GST fusion protein
recombinant enzyme 3.4fold from Escherichia coli strain BL21 (DE3) by two-stage ultrafiltration to 92.6% purity
-
recombinant enzyme expressed in Escherichia coli
recombinant enzyme from Escherichia coli by ammonium sulfate fractionation, gel filtration, and anion exchange chromatography, to homogeneity
-
recombinant enzyme from Escherichia coli strain BL21(DE3)
recombinant enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant enzyme from Escherichia coli strain BL21(DE3) to homogeneity
-
recombinant enzyme from Escherichia coli strain BL21(DE3)pLys to near homogeneity
recombinant enzyme from Escherichia coli strain QC779
recombinant enzyme from Pichia pastoris strain GS115 by anion exchange chromatography
recombinant enzyme from Pichia pastoris strain GS115 by dialysis and anion exchange chromatography
Thermochaetoides thermophila
recombinant enzyme with his-tag
recombinant from Escherichia coli
-
recombinant GST-tagged SeCuZnSOD from Escherichia coli by glutathione affinity chromatography
recombinant His-tagged Cu,Zn-SOD from Escherichia coli
recombinant His-tagged enzyme 12.6fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme 14fold from Escherichia coli strain strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme 25fold from Escherichia coli strain BL21(DE3) by immobilized metal-ion affinity and ion exchange chromatography, and isoelectric focusing to over 95% purity
recombinant His-tagged enzyme 3.2fold from Escherichia coli strain Rosetta-gami by nickel affinity chromatography
recombinant His-tagged enzyme by nickel affinity chromatography from Escherichia coli strain Rosetta-gami(DE3)
recombinant His-tagged enzyme from Escherichia coli
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and dialysis
recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and dialysis, anion exchange chromatography and dialysis, and ultrafiltration
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to near homogeneity
recombinant His-tagged enzyme from Escherichia coli strain BL21-SI by nickel affinity chromatography, dialysis, and ultrafiltration to over 97% purity
recombinant His-tagged enzyme from Escherichia coli strain M15 by nickel affinity chromatography, dialysis, and ultrafiltration
recombinant His-tagged enzyme from Escherichia coli strain Rosetta(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain Rosetta-gami by nickel affinity chromatgraphy
-
recombinant His-tagged enzyme from Escherichia coli strain Rosetta-gami by nickel affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strains DH5alpha and M15 by nickel affinity chromatography
recombinant His-tagged MnSOD-2 and MnSOD-3 by nickel affinity and anion exchange chromatography, followed by gel filtration
-
recombinant His-tagged SOD from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant His-tagged soluble chloroplastic isoform CuZn-SOD from Escherichia coli by nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes and His-tagged SOD1-Lys7 from Escherichia coli BL21(DE3) by nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli BL21(DE3) by nickel affinity chromatography
recombinant His-tagged wild-type enzyme SODAp and NTD-fused N-terminal domain ntdSODAp from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant His6-tagged type A isozyme from Escherichia coli strain BL21(DE3) by His-trap affinity chromatography and gel filtration
-
recombinant MBP-tagged enzyme from Escherichia coli strain BL21(DE3) by amylose affinity chromatography
recombinant Mn-SOD from Escherichia coli strain QC774 by anion exchange chromatography
-
recombinant MnSOD from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, cleavage of the GST fusion protein
recombinant SOD1 from Leishmania tarentolae strain P10 to 90% purity by ultracentrifugation, hydrophobic interaction chromatography and dialysis
recombinant soluble Cp-icCuZnSOD by nickel affinity chromatography
-
recombinant soluble enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
recombinant wild-type and mutant from Escherichia coli
recombinant wild-type and truncated mutant FLAG-tagged hEC-SOD enzymes from Spodoptera frugiperda Sf9 cells by affinity chromatography
SOD-I and SOD-III, of 4 isoenzymes
-
SOD-II, SOD-III, SOD-IV
-
soluble recombinant enzyme from Escherichia coli by ammonium sulfate fractionation and anion exchange chromatography to homogeneity
soluble recombinant enzyme SOD2 from Escherichia coli cell-free extract by dialysis, anion exchange chromatography, again dialysis, and ultrafiltration
structural intermediate between Mn-SOD and Fe-SOD
-
var. gemmifera, 3 isoenzymes
-
-
-
-
Thermosynechococcus vestitus
-
Cu,Zn-SOD
-
extracellular enzyme
-
Fe-SOD
-
Fe-SOD
Megalodesulfovibrio gigas
-
Mn-SOD
-
Mn-SOD from liver
-
overview: purification of extracellular superoxide dismutases
-
overview: purification of extracellular superoxide dismutases
-
overview: purification of extracellular superoxide dismutases
-
partially
-
recombinant enzyme from Escherichia coli strain BL21(DE3)
recombinant enzyme from Escherichia coli strain BL21(DE3)
recombinant enzyme from Pichia pastoris strain GS115 by anion exchange chromatography
recombinant enzyme from Pichia pastoris strain GS115 by anion exchange chromatography
Thermochaetoides thermophila
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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AhSOD DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3)
atypical SOD, functional and structural intermediate between Fe-SOD and Mn-SOD, expression in Escherichia coli
-
cDNA library construction, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, genetic structure, the primary transcript is represented by five exons and encodes a peptide of 154 amino acids, quantitative PCR expression analysis. Screening of Of-cCu/ZnSOD 5'-flanking region reveal the presence of several important transcription factor binding sites that potentially govern the Cu/ZnSOD expression. Recombinant overexpression of MBP-tagged enzyme in Escherichia coli strain BL21(DE3)
construction of replication-deficient E1-partially E3-deleted clinical good manufacturing practice-grade adenoviruses encoding rabbit EC-SOD, free from contaminants, infusion of rabbit aorta segments, overview
-
Cu,Zn-SOD, expression in Escherichia coli as His-tagged protein, DNA and amino acid sequence analysis
Cu,Zn-SOD, expression of wild-type and mutant in Escherichia coli
-
Cu,Zn-SOD, overexpression in Escherichia coli
Cu,Zn-SOD, overexpression of wild-type and mutants in Spodoptera frugiperda cells Sf21 via baculovirus infection
-
Cu/Zn-SOD, DNA and amino acid sequence determination and analysis, semi-quantitative and/or real-time RT-PCR enzyme expression analysis
-
cytoplasmic manganese SOD, DNA and amino acid sequence determination and analysis
-
cytosolic MnSOD isozyme, DNA and amino acid sequence determination and analysis, phylogenetic analysis, sequence comparison, quantitative real-time RT-PCR expression analysis
DNA and amino acid sequence determination and analysis
-
DNA and amino acid sequence determination and analysis, ala16val polymorphism genotyping, overview, stably expression of human MnSOD-A16 and MnSOD-V16 variants in mouse fibroblasts
DNA and amino acid sequence determination and analysis, and sewquence comaprison, genetic structure, overview
-
DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)pLys
DNA and amino acid sequence determination and analysis, phylogenetic analysis, quantitative real-time PCR enzyme expresion analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta-gami
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli
DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain M15
DNA and amino acid sequence determination and analysis, phylogenetic analysis, semiquantitative PCR enzyme expression analysis
DNA and amino acid sequence determination and analysis, phylogenetic tree, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
DNA and amino acid sequence determination and analysis, real-time PCR enzyme expression analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
DNA and amino acid sequence determination and analysis, real-time RT-PCR expression analysis, sequence comparisons, expression in Escherichia coli strain QC779
DNA and amino acid sequence determination and analysis, sequence comparison
DNA and amino acid sequence determination and analysis, sequence comparison, expression of soluble enzyme in Escherichia coli strain BL21(DE3)
DNA and amino acid sequence determination and analysis, sequence comparison, His-tagged enzyme expression in Escherichia coli strains DH5alpha and M15
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-SI
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
DNA and amino acid sequence determination and anaylsis, expression of wild-type and mutant in Escherichia coli
DNA and amino acid sequence determnination and analysis, expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
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EC-SOD, overexpression in Escherichia coli as His-tagged protein and in Tn-5B1-4 cells of Trichoplusia ni via baculovirus infection
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expressed in Escherichia coli. Although the recombinant protein is soluble, little activity is observed due to the lack of metal incorporation. Reconstitution of the enzyme by heat treatment with either Mn2+ or Fe2+ yields a highly active protein
expressed in THP-1- cells
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expression analysis in homozygous LDL-receptor-knockout mice, heterozygous ob/+, and wild-type C57BL6 mice
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expression analysis in TCAP-1 treated or untreated cells at different pH
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expression in Escherichi coli
expression in Escherichia coli
expression in Escherichia coli strain BL21 (DE3)
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expression in Escherichia coli strain BL21(DE3)
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expression in Pichia pastoris, DNA and amino acid sequence determination and comparison
expression of H63C mutant in Escherichia coli
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expression of His-tagged SOD in Escherichia coli strain BL21(DE3)
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expression of His6-and thioredoxin-tagged enzyme in Escherichia coli
expression of human SOD in Escherichia coli
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expression of recombinant chimera MnSOD-VHb in Escherichia coli strain BL21(DE3)
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expression of SOD1 in Leishmania tarentolae strain P10
expression of the CuZn-SOD in Escherichia coli
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expression of wild-type and mutant enzymes in Escherichia coli
expression of wild-type and mutant enzymes in Escherichia coli strain JM109(DE3)
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Fe-SOD, expression in Escherichia coli, DNA and amino acid sequence determination
from genomic DNA, expression in Escherichia coli strain QC774
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from muscle, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis
gene BbSod1, DNA and amino acid sequence determination and analysis, phylogenetic analysis, subcloning in Escherichia coli strain DH5alpha, expression as His-tagged wild-type and mutant enzymes and as His-tagged Saccharomyces cerevisiae superoxide dismutase 1 copper chaperone-fusion enzyme, i.e. SOD1-Lys7, in Escherichia coli BL21(DE3)
gene CSD1, DNA and amino acid sequence determination and analysis, expression as GST-tagged protein in Escherichia coli strain BL21(DE3)
gene CSD1, DNA and amino acid sequence determination and analysis, sequence comparisons, real-time quantitative PCR enzyme expression analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta-gami
gene Ctsod, DNA and amino acid sequence determination and analysis, phylogenetic tree, subcloning in Escherichia coli strains DH5a and JM109, expression in Pichia pastoris strain GS115, the recombinant yeast exhibit higher stress resistance than the control yeast cells to salt and superoxide-generating agents, such as paraquat and menadione
Thermochaetoides thermophila
gene CuZnSOD, DNA and amino acid sequence determination and analysis, recombinant His6-tagged Cp-icCuZnSOD with high enzyme activity is induced to be expressed in Escherichia coli strain BL21(DE3) as a soluble form by IPTG supplemented with Cu/Zn ions at 20°C for 8 h
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gene cz1, expression of Cu,ZnSOD in Pichia pastoris strain GS115
Thermochaetoides thermophila
gene dhsod-1, DNA and amino acid sequence determination and analysis, sequence comparisons
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gene Fe-SOD, DNA and amino acid sequence deteremination and analysis, sequence comparisons, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) cytosol, expression as thioredoxin-fusion protein in Escherichia coli
gene KmSod1, DNA and amino acid sequence determination and analysis, sequence comparisons, overexpression of Cu/Zn-SOD under the control of the KlADH4 promoter in strain L3 from a multicopy plasmid, subcloning in Escherichia coli strain DH5alpha
gene locus Asac_0498, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta-gami(DE3)
gene MgMnSOD1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, tissue expression analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta(DE3). Expression of HBT95-MgMnSOD1-sGFP vector driven by a CaMV 35S promoter to determine the intracellular localization of MgMnSOD1
gene MgMnSOD2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, tissue expression analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta(DE3)
gene mnsod, expression in Pichia pastoris strain GS115. Transformed recombinant yeast cells exhibit higher stress resistance to salt and oxidative stress-inducing agents than control yeast cells
Thermochaetoides thermophila
gene MSD1, DNA and amino acid sequence determination and analysis, expression as GST-tagged protein in Escherichia coli strain BL21(DE3)
gene RmFeSOD, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3). Under copper stress experiment, the RmFeSOD-expressing Escherichia coli cells exhibit a better growth than nontransformed bacteria
gene RsrSOD, recombinant expression under the control of the CaMV35S promoter, in Brassica oleracea var. italica via Agrobacterium tumefaciens-mediated transformation. Both gene expression and enzyme activity of SOD increase significantly in transgenic lines when challenged with Hyaloperonospora parasitica, the causal agent of downy mildew. Three lines exhibit high resistance against downy mildew, with disease symptoms restricted completely
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gene SeCuZnSOD, DNA and amino acid sequence determination and analysis, genomic organization, sequence alignment and phylogenetic analysis, quantitative RT-PCR expression analysis, recombinant expression as GST-tagged enzyme in Escherichia coli
gene SOD, and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
gene sod, cloning from genomic DNA, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain JM109(DE3)
gene sod, DNA and amino acid sequence determination and analysis
gene sod, DNA and amino acid sequence determination and analysis, expression analysis, sequence comparisons
gene sod, DNA and amino acid sequence determination and analysis, functional overexpression of the soluble enzyme in Escherichia coli
gene sod, DNA and amino acid sequence determination and analysis, genetic structure, sequence comparison, phylogenetic tree, inducible expression in Pichia pastoris strain GS115 using the AOX1 promoter
gene sod, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene sod, expression of wild-type and mutant soluble enzymes in Escherichia coli strain QC774, that lacks the genes encoding endogeneous FeSOD, SodB-, and MnSOD, SodA-
gene sod-1, expression analysis
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gene Sod1, a single copy, expression analysis, recombinant expression in transgenic Oryza sativa plants, plants are more tolerant to methyl viologen mediated oxidative stress in comparison to the untransformed control plants and also withstand salinity stress
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gene SOD2, recombinant expression in Escherichia coli
gene SOD3, cloning of EC-SOD and recombinant expression of wild-type and truncated mutant FLAG-tagged hEC-SOD enzymes in Spodoptera frugiperda Sf9 cells using the baculovirus transfection method, both full length and truncated hEC-SOD proteins are enzymatically active
gene sod3, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic tree, semiquantitative and quantitative RT-PCR expression analysis
gene sod3, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic tree, semiquantitative and quantitative RT-PCR expression analysis, recombinant expression as thioredoxin-fusion enzyme
gene sodA, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree
gene sodA, DNA and amino acid sequence determination and analysis, sequence comparison
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gene sodA, DNA and amino acid sequence determination and analysis, sequence comparison, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene sodA, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, semi-quantitative expression analysis
gene sodA, DNA and amino acid sequence determination and analysis, subcloning in Escherichia coli strains DH5alpha and BW19851, complementation of an enzyme-deficient mutant strain
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gene sodA, expression of SodA in and complementation of enzyme-deficient Escherichia coli strain PN134. Expressing YeSodA confers resistance to paraquat to the Escherichia coli strain
gene sodA-1, DNA and amino acid sequence determination and analysis, chromosomal organization, expression in Escherichia coli strain QC779
gene sodA-2, DNA and amino acid sequence determination and analysis, chromosomal organization, expression in Escherichia coli strain QC779
gene sodB, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
gene sodB, DNA and amino acid sequence determination and analysis, sequence comparison, expression in Escherichia coli strain BL21(DE3)
gene sodB, expression of SodB in and complementation of enzyme-deficient Escherichia coli strain PN134. Expressing YeSodB confers resistance to paraquat to the Escherichia coli strain
gene sodB, overexpression of the His6-tagged type A isozyme in Escherichia coli strain BL21(DE3)
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gene sodC, DNA and amino acid sequence determination and analysis
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gene sodC, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged enzyme in Escherichia coli, recombinant overexpression of the enzyme from AS454(pREB102) in an Escherichia coli sodC mutant leads to complementation restoring resistance to H2O2 killing to wild-type levels
gene sodC, SodC cannot be expressed in Escherichia coli strain BL21(DE3)
gene sodC, subcloning in Escherichia coli, complementation of the sodC mutant, expression of a SodC-FLAG fusion protein in strain K56-2
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His-tagged MnSOD-2 and MnSOD-3
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isozyme SODI, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis
isozyme SODII, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis
mitochondrial MnSOD isozyme, DNA and amino acid sequence determination and analysis, phylogenetic analysis, sequence comparison, quantitative real-time RT-PCR expression analysis
Mn-SOD, DNA and amino acid sequence determination and analysis, semi-quantitative and/or real-time RT-PCR enzyme expression analysis
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Mn-SOD, expression in Escherichia coli
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Mn-SOD, expression in Escherichia coli as His-tagged protein, DNA sequence analysis
Mn-SOD, expression of wild-type and mutants in Escherichia coli
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MnSOD, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic tree, and quantitative real-time RT-PCR expression analysis, expression in Escherichia coli strain BL21(DE3)
molecular heterogeneity of the enzyme in Crypthecodinium cohnii at both genomic and transcriptional levels, DNA and amino acid sequence determination and analysis of genes sod1-sod17, phylogenetic analysis, the Crypthecodinium cohnii SODs form a monophyletic group and are all acquired by the same event of horizontal gene transfer, functional overexpression of sod1 in Escherichia coli
overexpressed as a GST fusion protein at a high level in Escherichia coli
overexpression in Saccharomyces cerevisiae mutant lacking Cu,Zn-SOD, restores activity of the mutant
overexpression of wild-type and mutant enzymes in hind limb muscle of transgenic mice
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recombinant expression in in a copper-tolerant yeast, Cryptococcus sp. strain N6, two distinct bands exhibiting SOD activity appear on native PAGE: one band, with higher mobility, appears when the cells are grown without CuSO4, and the other band appears when the cells are grown with 10 mM CuSO4. Cells grown with 3 mM CuSO4 produce both SOD isoforms
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recombinant expression in Mus musculus, CX3CR1-GFP mice, heterogenic parabiosis between mutant and wild-type mice confers a significant protection to wild-type mice, whereas mice with R213G knock-in mutation, a human single nucleotide polymorphism leading to reduced binding EcSOD in peripheral organs, exacerbate the organ damages. Recombinant EcSOD overexpressed in skeletal muscle-specific mutant mice redistributes to other peripheral organs through the circulation and enriches at the endothelium of the vasculatures. Mutant mice are resistant to endotoxemia (induced by lipopolysaccharide injection) in developing MODS with significantly reduces mortality and organ damages compared with the wild-type littermates
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recombinant expression of His-tagged soluble chloroplastic isoform CuZn-SOD in its enzymatically active and stable form in Escherichia coli, and optimization of culture conditions, best at 18°C and upon isopropyl beta-D-1-thiogalactopyranoside induction, recombinant enzyme production process optimization
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli BL21(DE3)
recombinant expression of His-tagged wild-type enzyme SODAp and NTD-fused N-terminal domain ntdSODAp in Escherichia coli strain BL21(DE3)
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SaFe-SOD, DNA and amino acid sequence determination and analysis, quantitative real-time PCR enzyme expression analysis, functional recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta-gami
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semi-quantitative enzyme expression analysis
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single copy gene, DNA and amino acid sequence determination and analysis
SOD, DNA and amino acid sequence determination and analysis, promoter analysis, phylogentic tree
strains KT2440 and PAO1, genome expression profiling, overview
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subcloning in Escherichia coli, expression of iron-SOD or manganese-SOD in and complementation of an enzyme-deficient double mutant strain
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two splicing variants of PthipI-SODC1, presence of two transcripts of PthipI-SODC1, hipI-SODC1b and hipI-SODC1s. hipI-SODC1b is 69 bp longer than hipI-SODC1s due to an alternative splicing event involving an alternative donor splice site in the sixth intron. Transcript analysis
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Cu,Zn-SOD, overexpression in Escherichia coli
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Cu,Zn-SOD, overexpression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
expression in Escherichia coli
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expression in Escherichia coli
expression in Escherichia coli
from muscle, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis
from muscle, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis
from muscle, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis
gene sod, DNA and amino acid sequence determination and analysis
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gene sod, DNA and amino acid sequence determination and analysis
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2-[(3-iodophenyl)methylsulfanyl]-5-pyridin-4-yl-1,3,4-oxadiazole, a known protein kinase inhibitor, decreases enzyme mutant G93A-SOD1 expression in vitro and in the brain and spinal cord in vivo. Compounds 3-[1-(3-hydroxypropyl)-1H-pyrrolo[2,3-b]pyridin-3-yl]-4-(pyrazin-2-yl)-1H-pyrrole-2,5-dione, 2-chloro-1-(4,5-dibromothiophen-2-yl)ethan-1-one, 2-bromo-1-(4-bromophenyl)ethan-1-one, 4-(5-[[(3-iodophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(3-methoxyphenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(3-fluorophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-[5-([[4-(trifluoromethyl)phenyl]methyl]sulfanyl)-1,3,4-oxadiazol-2-yl]pyridine, 4-(5-[[(3-chlorophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(3-nitrophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(3-bromophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(4-methoxyphenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(4-chlorophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(4-bromophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(4-iodophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(4-fluorophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(4-methylphenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(4-nitrophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(4-nitrophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine suppress the enzyme expression
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4 constitutive isozymes, 3 cold-inducible isozymes in bulbs, at 4°C, overview
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a decrease in mRNA levels is observed for Sod1 with osmotic stress treatment
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after challenge with lipopolysaccharide (LPS), expression of pfSOD mRNA in hemocytes is increased, reaching the highest level at 8 h, then dropping to basal levels at 36 h
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betulinic acid, i.e. BetA, from Pulsatilla chinensis suppresses SOD2 expression by BetA-induced cAMP-response element-binding protein, i.e. CREB protein, dephosphorylation at Ser133, which subsequently prevents SOD2 transcription through the required cAMP-response element-binding protein-binding motif on the SOD2 promoter, mechanism, overview
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both gene expression and enzyme activity of recombinant SOD expressed in Brassica oleracea var. italica increase significantly in transgenic lines when challenged with Hyaloperonospora parasitica, the causal agent of downy mildew
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challenge with Vibrio anguillarum increases Mm-icCu/Zn-SOD expression
constitutive overexpression of group IId WRKY gene GhWRKY39-1 in Nicotiana benthamiana confers a greater resistance to infection by both the bacterial pathogen Ralstonia solanacearum and the fungal pathogen Rhizoctonia solani. The transgenic plants also exhibit elevated mRNA levels of several pathogenrelated (PR) genes, including PR1c, PR2, and PR4. Moreover, the transgenic plants display enhanced tolerance to salt and oxidative stress and show elevated expression of several oxidationrelated genes encoding SOD, APX, CAT, and glutathioneS-transferase
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docosahexaenoic acid inhibits enzyme transcription in cancer cells, involvement of hypoxia-inducible factor-2alpha signaling, but not of peroxisome proliferator-activated receptor alpha, overview. Suppression of SOD-1 expression by clofibrate also requires hypoxia-inducible factor-2alpha and the binding element in the SOD-1 promoter
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effects of abiotic and biotic stresses on SOD expression, overview
enzyme expression is increased when cells are cultured with Cu2+, Cr2+, Fe3+ and Ni2+
expressions of Mn-SOD and Ni-SOD genes are highly induced
expressions of Mn-SOD and Ni-SOD genes are highly induced. The expression of the SOD genes from plants is influenced by plant growth stage and growth regulating substances. The effects of the hormone abscisic acid and osmotic stress can induce expression of Cu/Zn-SOD and Mn-SOD genes in maize
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Fe-SODs and Cu/Zn-SODs are constitutively expressed. Effects of abiotic and biotic stresses on SOD expression, overview
gene sodB gene, encoding Fe-SOD, is expressed highly in logarithmic phase cells but is downregulated in stationaryphase cells, except when the medium is amended with FeCl3 suggesting that downregulation of Pseudomonas putida sodB in stationary phase cells is due to Fe2+ depletion in this phase of growth. Removal of Fe2+ by adding a Fe-chelator decreases the sodB transcript level, even in logarithmicphase cells
GSK3B-IX and aloisine-A induce the enzyme expression
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in Pennisetum seedlings, abiotic stress-induced PgCuZnSOD transcript upregulation directly correlates to high protein and activity induction. PgCuZnSOD mRNA levels gradually increase to several folds on exposure of Pennisetum seedlings corresponding to gradual increase in the time period of different stress treatments i.e. dehydration, methyl viologen, NaCl and high temperature (48°C) with an exception in cold stress (4°C) where the transcript initially increased (0-12 h time-point) in comparison to control and later decreased (24 h time-point) with regards to initial rise
in Portunus trituberculatus challenged with the Hematodinium parasite, transcripts in hemocytes are decreased significantly at 3 h, and then increased significantly at 12 and 24 h, followed by significant reduction from 48 to 192 h
induced overproduction of the CyAbrB transcription factor CalA (cyanobacterial AbrBlike, Alr0946) in the cyanobacterium Nostoc sp. PCC 7120 downregulates the abundance of Fe-SOD, one of two types of SODs in strain PCC 7120. Purified recombinant CalA interacts with the promoter region of alr2938, encoding Fe-SOD, indicating a transcriptional regulation of Fe-SOD by CalA
infection of the organism by white spot syndrome virus increases the expression of cMn-SOD. Transcript levels increase transiently 1 h post-infection and then decrease as the viral infection progresses to levels significantly lower than uninfected controls by 12 h post-infection
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KCN inhibits Cu,Zn-SOD expression
microRNA miR398, conserved in several plant species, targets two of the three Cu/Zn-SODs of Arabidopsis thaliana (CSD1 and CSD2) by triggering cleavage or inhibiting translation of their mRNAs
mRNA transcription of enzyme ecCuZnSOD in hemocytes and gill is upregulated after inoculation with Spiroplasma eriocheiris and Aeromonas hydrophila. mtMnSOD in hepatopancreas is upregulated after Aeromonas hydrophila inoculation, whereas it is downregulated after Spiroplasma eriocheiris challenge, enzyme expression pattern, overview
mRNA transcription of enzyme ecCuZnSOD in the hepatopancreas, hemocytes, and gill is upregulated after inoculation with Spiroplasma eriocheiris and Aeromonas hydrophila, enzyme expression pattern, overview
mtMnSOD in hepatopancreas is upregulated after Aeromonas hydrophila inoculation, whereas it is downregulated after Spiroplasma eriocheiris challenge, enzyme expression pattern, overview
NaCl treatment increases the transcript level of cytosolic Cu/Zn-SOD in young and mature leaves rather than in old leaves. Expression of the cytosolic Cu/Zn-SOD gene is induced by exogenous abscisic acid
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no suppression of MnSOD by KCN
other transcription factors such as NAC, GRAS, MYB, and C3H are also involved in the regulation of SOD genes. Effects of abiotic and biotic stresses on SOD expression, overview
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overexpression of yeast transcription factor ACE1 in Arabidopsis thaliana increases the activities of Cu/Zn-SOD, indicating that ACE1 plays an important role in the regulation of SOD gene expression. The Cu/ZnSOD gene is remarkably activated by ginsenoside Rb2 through transcription factor AP2 binding sites and its induction
regulation of the expression of miR398, overview. Effects of abiotic and biotic stresses on SOD expression, overview
salinity (50 mM NaCl) causes a decrease in activities of SOD during germination. After stress the activity increases in recovered plants. During vegetative growth, the activity of SOD is strongly enhanced and responsible for salt tolerance
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screening of Of-cCu/ZnSOD 5'-flanking region reveal the presence of several important transcription factor binding sites that potentially govern the Cu/ZnSOD expression
Sod1 mRNA levels are induced by iron, light stress and by direct H2O2stress treatment, thus confirming their role in oxidative stress response
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temporal expression of SOD in hemocytes of bay scallops is challenged with bacteria Vibrio anguillarum, highest level at 12 h post-injection and return to normal between 24 h and 48 h post-injection
the activity of superoxide dismutase is not altered in response to any treatment of methyl jasmonate (0.0001 mM, 0.01 mM and 0.1 mM) or salicylic acid (1 mM, 5 mM and 10 mM)
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the Arabidopsis thaliana Fe-SOD gene promoter containing the GTACT motif is repressed by Cu2+. Molecular mechanisms of GTACT motif-dependent transcriptional suppression by Cu2+ are conserved in land plants
the enzyme Fe-SOD is induced after exposure to toxic metal ions
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the enzyme is downregulated by UV-B radiation
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the enzyme is induced by Cd2+
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the expression of the enzyme is increased in plerocercoid larvae after treated with paraquat and significantly induced under oxidative stress
the FeSOD gene is expressed at low levels in Rhodobacter capsulatus cells grown under anaerobic or semiaerobic conditions, but expression is strongly induced upon exposure of the bacteria to air
the mRNA levels of Cu/Zn-SOD is increased in general during the metal (copper, zinc and cadmium) or thermal treatments
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the mRNA levels of Mn-SOD is increased in general during the metal (copper, zinc and cadmium) or thermal treatments
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the transcriptional profile and temporal assessment of Of-cCu/ZnSOD transcripts in animals under pathological (bacteriaor viral-induced) and physiological (H2O2-induced oxidative) stress conditions using quantitative PCR expression analysis, in which the enzyme expression exhibits significantly upregulated levels. Lipopolysaccharide induces the enzyme expression, and H2O2 causes a transient increase in Of-cCu/ZnSOD transcription
transgenic Nicotiana tabacum plants that overexpress a group IIe WRKY gene designated as BdWRKY36 from Brachypodium distachyon show higher SOD, POX, and CAT activity than the wild-type under drought stress. This implies that ROSscavenging systems might be more effective in transgenic than in wild-type plants. Overexpression of the BdWRKY36 gene may function in activation of the antioxidant defense system, which results in transgenic plants suffering less ROS-mediated injury under drought stress
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treatment with CuSO4 inhibits expression of SOD protein, addition of Mn2+ to the medium reduces the enzyme expressions
under 0.25 M and 0.5 M salt stress, the expression of SaCSD1 is downregulated in roots, but upregulated in leaves
up-regulation of SOD mRNA with low salinity stress, increase levels of Sod mRNA by thermal and osmotic stresses
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UV-irradiation induces the enzyme
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effects of abiotic and biotic stresses on SOD expression, overview
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effects of abiotic and biotic stresses on SOD expression, overview
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effects of abiotic and biotic stresses on SOD expression, overview
effects of abiotic and biotic stresses on SOD expression, overview
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effects of abiotic and biotic stresses on SOD expression, overview
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effects of abiotic and biotic stresses on SOD expression, overview
effects of abiotic and biotic stresses on SOD expression, overview
effects of abiotic and biotic stresses on SOD expression, overview
effects of abiotic and biotic stresses on SOD expression, overview
effects of abiotic and biotic stresses on SOD expression, overview
effects of abiotic and biotic stresses on SOD expression, overview
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enzyme expression is increased when cells are cultured with Cu2+, Cr2+, Fe3+ and Ni2+
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enzyme expression is increased when cells are cultured with Cu2+, Cr2+, Fe3+ and Ni2+
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expressions of Mn-SOD and Ni-SOD genes are highly induced
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expressions of Mn-SOD and Ni-SOD genes are highly induced
Fe-SODs and Cu/Zn-SODs are constitutively expressed. Effects of abiotic and biotic stresses on SOD expression, overview
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Fe-SODs and Cu/Zn-SODs are constitutively expressed. Effects of abiotic and biotic stresses on SOD expression, overview
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Fe-SODs and Cu/Zn-SODs are constitutively expressed. Effects of abiotic and biotic stresses on SOD expression, overview
treatment with CuSO4 inhibits expression of SOD protein, addition of Mn2+ to the medium reduces the enzyme expressions
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treatment with CuSO4 inhibits expression of SOD protein, addition of Mn2+ to the medium reduces the enzyme expressions
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