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Enzyme Nomenclature
Information on EC 1.15.1.1 - superoxide dismutase
Word Map on EC 1.15.1.1
- 1.15.1.1
- catalase
- radical
- malondialdehyde
- injury
- gsh
- neuron
- endothelial
- ascorbate
- dysfunction
- artery
- erythrocyte
- hepatic
- vascular
- wistar
- gsh-px
- ischemia
- diabetes
-
tbars
-
thiobarbituric
-
intraperitoneal
- inflammation
- renal
- lactate
-
amyotrophic
-
reperfusion
-
histopathological
- sclerosis
- xanthine
- neurodegenerative
- cerebral
-
neuroprotective
-
motor
-
chemiluminescence
-
mime
- myocardial
- cardiac
- pulmonary
- myeloperoxidase
- peroxynitrite
- neutrophil
-
hydroperoxide
- glutathione-s-transferase
- coronary
- diagnostics
- ceruloplasmin
- environmental protection
- mannitol
-
endothelium-derived
-
albino
-
ischemia-reperfusion
-
endothelium-dependent
- synthesis
- drug development
- biotechnology
- alpha-tocopherol
- agriculture
- medicine
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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
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EC NUMBER 
COMMENTARY 
1.15.1.1
-
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RECOMMENDED NAME
GeneOntology No.
superoxide dismutase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 superoxide + 2 H+ = O2 + H2O2
active site, manganese-binding site and contact site between monomers; amino acid sequence alignment and comparison; mechanism
-
2 superoxide + 2 H+ = O2 + H2O2
active site, manganese-binding site and contact site between monomers; amino acid sequence alignment and comparison; mechanism
-
2 superoxide + 2 H+ = O2 + H2O2
active site is not conserved, differing from others of Mn-SOD and Fe-SOD; amino acid sequence alignment and comparison; mechanism
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison; mechanism
-
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
active site, manganese-binding site and contact site between monomers; 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 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 composition, comparison
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
Anas platyrhynchos domestica
-
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 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; 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; amino acid sequence alignment and comparison
-
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
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
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
mechanism; mechanism; mechanism; three-dimensional structure
-
-
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
active site, manganese-binding site and contact site between monomers; amino acid sequence alignment and comparison; mechanism; mechanism
-
-
2 superoxide + 2 H+ = O2 + H2O2
active site, manganese-binding site and contact site between monomers; amino acid sequence alignment and comparison; mechanism; mechanism
-
-
2 superoxide + 2 H+ = O2 + H2O2
active site, manganese-binding site and contact site between monomers; amino acid sequence alignment and comparison; mechanism; mechanism; mechanism
-
-
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; amino acid composition, comparison; 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; mechanism; mechanism
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison; amino acid composition, comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
amino acid composition, comparison; 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; mechanism
-
-
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; amino acid composition, comparison; amino acid sequence alignment and comparison; 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; amino acid sequence alignment and comparison
-
-
2 superoxide + 2 H+ = O2 + H2O2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
superoxide:superoxide oxidoreductase
A metalloprotein; also known as erythrocuprein, hemocuprein or cytocuprein. Enzymes from most eukaryotes contain both copper and zinc; those from mitochondria and most prokaryotes contain manganese or iron.
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CAS REGISTRY NUMBER
COMMENTARY
9054-89-1
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
; isolated from a terrestrial acidic hot spring, Kamchatka peninsula, Russia, gene ASAC_0498
UniProt
5 isozymes: SOD-II, SOD-III, SOD-IV, and SOD-V are Cu,Zn-SODs, SOD-I is a Mn-SOD
-
-
collected from soil and water samples from hot springs in Mae Hong Son Province of Thailand, gene sodA
UniProt
collected from soil and water samples from hot springs in Mae Hong Son Province of Thailand, gene sodA
UniProt
a grass specie adapted to the extreme climate of the Maritime Antarctic
-
-
collected from a tepid spring, 41°C, pH 7.9, in Oguni-tyo, Kumamoto, Japan, gene sodA
-
-
collected from a tepid spring, 41°C, pH 7.9, in Oguni-tyo, Kumamoto, Japan, gene sodA
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-
Cu,Zn-SOD
-
-
Fe-SOD; subsp. piscicida, formerly Pasteurelle piscicida
SwissProt
structural intermediate between Mn-SOD and Fe-SOD
-
-
MnSOD1; strain 905, isolated from wheat rhizosphere, colonizes wheat rhizosphere with large population size, gene sodA-1
UniProt
MnSOD2; strain 905, isolated from wheat rhizosphere, colonizes wheat rhizosphere with large population size, gene sodA-2
UniProt
MnSOD1; strain 905, isolated from wheat rhizosphere, colonizes wheat rhizosphere with large population size, gene sodA-1
UniProt
MnSOD2; strain 905, isolated from wheat rhizosphere, colonizes wheat rhizosphere with large population size, gene sodA-2
UniProt
superoxide dismutase paralog lacking two Cu ligands and without enzymic activity
-
-
commercial prepapration, enzyme additionally catalyzes the reductive decomposition of S-nitroso-L-glutathione in presence of thiols
-
-
enzyme has a divalent-metal dependent nucleolytic activity, DNA-cleavage obeys Michaelis-Menten kinetics
Uniprot
ATCC 50050, a heterotrophic dinoflagellate, a multi-copy gene family comprising genes sod1-sod17 encoding FeSODs
UniProt
FeSOD fragment; ATCC 50050, a heterotrophic dinoflagellate, a multi-copy gene family comprising genes sod1-sod17 encoding FeSODs
UniProt
homozygous LDL-receptor-knockout mice, heterozygous ob/+, and wild-type C57BL6 mice
-
-
strain GUH-2; structural intermediate between Mn-SOD and Fe-SOD, Zn-containing
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-
expression in tobacco leaves, enzyme has superoxide dismutase activity, but no oxalate oxidase activity
SwissProt
metal content depends on O2-concentration; structural intermediate between Mn-SOD and Fe-SOD
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-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
-
MnSOD ala16val polymorphism is associated with various diseases including breast cancer
physiological function
additional information
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
Leptopilina SOD3 clusters with predicted extracellular insect Cu,Zn-SODs, phylogenetic analysis; 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; Leptopilina SOD3 clusters with predicted extracellular insect Cu,Zn-superoxide dismutases, phylogenetic analysis
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
SOD detoxifies the highly reactive superoxide anions to hydrogen peroxide and molecular oxygen
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
-
protection by recombinant Cp-icCuZnSOD against alcohol-injury in human hepatocyte L02 cell line
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
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
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; 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
-
the enzyme may play an important role as an antioxidant in a wide temperature range
physiological function
PgCuZnSOD plays a functional role in conferring oxidative stress tolerance to prokaryotic system
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 in the innate immune system of hard clam
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
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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
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physiological function
-
the enzyme may play an important role as an antioxidant in a wide temperature range
-
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
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additional information
-
CpSOD contains an intracellular disulfide bond and two CuZnSOD family signatures
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
-
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
-
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 analysis by molecular replacement using human mitochondrial MnSOD variant, PDB ID 1var, modelling
additional information
-
molecular metal specificity mechanism of th enzyme, 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
overexpression of PgCuZnSOD confers comparatively enhanced tolerance to methyl viologen induced oxidative stress in bacteria. Homology structure modeling of PgCuZnSOD, overview
additional information
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active site Cys. Infection with pathogen Puccinia striiformis f.sp. tritici alters the kinetic properties of the cell wall enzyme
additional information
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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
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
secondary structure analysis using circular dichroism, overview; secondary structure analysis using circular dichroism, overview; secondary structure analysis using circular dichroism, overview
additional information
secondary structure analysis using circular dichroism, overview; secondary structure analysis using circular dichroism, overview; secondary structure analysis using circular dichroism, overview
additional information
secondary structure analysis using circular dichroism, overview; secondary structure analysis using circular dichroism, overview; secondary structure analysis using circular dichroism, overview
additional information
-
no evidence for the presence of either iron or copper/zinc SODs in Phytophthora cinnamomi
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
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residues involved in the active site are H28, Y36, H82, Q149, D164, and H168, which are completely conserved in the EgMnSOD
-
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
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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 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
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secondary structure analysis using circular dichroism, overview; secondary structure analysis using circular dichroism, overview; secondary structure analysis using circular dichroism, overview
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
O2.- + 4-[3-(4-iodophenyl)-2-(4-nitrophenyl)-2H-5-tetrazolio]-1,3-benzene disulfonate
?
i.e. WST-1, activity assay detection method
-
-
?
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
-
enzyme activity determination by xanthine-xanthine oxidase-nitro blue tetrazolium assay
-
-
ir
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
-
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
the SOD-catalyzed reaction proceeds through a redox cycle of metal ions, active site geometry, overview
-
-
?
2 superoxide + 2 H+
O2 + H2O2
detoxification of superoxide
-
-
?
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
-
-
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
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
-
-
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
-
-
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
-
-
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
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
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
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
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
-
SOD is a regulatory enzyme involved in the degradation of superoxide anions in living organisms
-
-
?
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
-
periplasmic Cu,ZnSOD protects the bacterium from exogenously generated O2.- and contributes to intracellular survival of the bacterium in macrophages
-
-
?
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
a metalloenzyme that eliminates superoxide radicals by dismutation into hydrogen peroxide and molecular oxygen
-
-
?
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
-
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
SOD is a regulatory enzyme involved in the degradation of superoxide anions in living organisms
-
-
?
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
-
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
-
the enzyme is important in defense of cells against oxidative stress
-
-
?
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
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
-
-
?
pyrogallol + ?
?
enzyme inhibits the autooxidation of pyrogallol
-
-
?
pyrogallol + ?
?
-
enzyme inhibits the autooxidation of pyrogallol
-
-
?
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
?
-
-
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 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
?
-
-
coupled assay method using inhibition of the autooxidation of pyrogallol
-
-
-
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 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 measurement by the ferricytochrome c method, using xanthine/xanthine oxidase as the source of superoxide radicals
-
-
-
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
?
-
-
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
?
-
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
?
-
-
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
?
-
-
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
?
-
-
Cu,Zn-dependent enzyme protects photoheterotrophic cells from periplasmic superoxide generated by exposure to low O2 under illuminated conditions
-
-
-
additional information
?
-
-
enzyme activity is measured byy the enzyme caused inhibition of the xanthine oxidase coupling reaction
-
-
-
additional information
?
-
-
Fe2+-containing active site structure, overview
-
-
-
additional information
?
-
-
Fe2+-containing active site structure, overview
-
-
-
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
?
-
-
unusual covalent modification of the conserved Tyr41 in the active site, interactions Tyr41-His155, 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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 superoxide + 2 H+
O2 + H2O2
O29903
detoxification of superoxide
-
-
?
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
Q9Y8H8
the SOD-catalyzed reaction proceeds through a redox cycle of metal ions, active site geometry, overview
-
-
?
O2- + H+
O2 + H2O2
Q96UT6
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
A6MHS2, Q6QHT3
isozyme MnSOD1, the product of sodA-1 gene, is expressed at lower level compared to MnSOD2, overview
-
-
?
O2.- + H+
O2 + H2O2
A6MHS2, Q6QHT3
isozyme MnSOD2, encoded by sodA-2, plays a more important role in antioxidative stress compared to MnSOD1, overview
-
-
?
O2.- + H+
O2 + H2O2
A6MHS2, Q6QHT3
isozyme MnSOD2, encoded by sodA-2, plays a more important role in antioxidative stress compared to MnSOD1, overview
-
-
?
O2.- + H+
O2 + H2O2
A6MHS2, Q6QHT3
isozyme MnSOD1, the product of sodA-1 gene, is expressed at lower level compared to MnSOD2, overview
-
-
?
O2.- + H+
O2 + H2O2
-
SOD is a regulatory enzyme involved in the degradation of superoxide anions in living organisms
-
-
?
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
-
periplasmic Cu,ZnSOD protects the bacterium from exogenously generated O2.- and contributes to intracellular survival of the bacterium in macrophages
-
-
?
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
B0L421, B2KYC6, B2KYC9
a metalloenzyme that eliminates superoxide radicals by dismutation into hydrogen peroxide and molecular oxygen
-
-
?
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
-
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
A7BI63
SOD is a regulatory enzyme involved in the degradation of superoxide anions in living organisms
-
-
?
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
-
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
-
the enzyme is important in defense of cells against oxidative stress
-
-
?
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
B6QEB3
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
-
-
?
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
?
-
-
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
?
-
-
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
?
-
B0B552
SOD activity is one major defense line against oxidative stress for all of the aerobic organisms
-
-
-
additional information
?
-
B0B552
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
Cu,Zn-dependent enzyme protects photoheterotrophic cells from periplasmic superoxide generated by exposure to low O2 under illuminated conditions
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
copper
Cu
Cu2+
Fe
Fe2+
Iron
Manganese
Mg2+
Mn
Mn2+
Zinc
Zn
Zn2+
additional information
Ca2+
-
study on affinity for enzyme-DNA complex and binding parameters. Enzyme-DNA complex shows at least two binding sites for divalent metal ions
copper
-
peculiar axial geometry of copper active sitewith low accessibility to external chelating agents
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
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+
-
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+
-
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 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+
a Cu,Zn-superoxide dismutase; a Cu,Zn-superoxide dismutase
Cu2+
a Cu,Zn-superoxide dismutase; a Cu,Zn-superoxide dismutase
Cu2+
a Cu,Zn-superoxide dismutase, residues H46, H48, H63, and H119 are involved in Cu2+ binding
Cu2+
-
1.63-1.78 mol per mol of isoenzyme I; 1.86-1.97 mol per mol of isoenzyme II
Cu2+
the residues His47, His49, His64, His72, His81, and Asp121 are involved in metal binding
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; 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+
all isozymes in the organism are FeSODs; all isozymes in the organism are FeSODs; all isozymes in the organism are FeSODs
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 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+
-
bound by His33, His84, His174, and Asp170, coordination in the active site, overview
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
Iron
the enzyme is a tetramer with 4 iron centers, one iron per monomer
Iron
-
1.8-1.9 mol (gatoms) per mol of enzyme; each Fe3+ ion has 2 coordination positions available for interaction with solute molecules but only 1 is necessary for catalysis
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
-
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
-
contains one iron atom per dimer, the protein contains a mononuclear iron center
Iron
-
no change in the geometry of the FeII site occurs over a wide pH range
Iron
-
0.35 mol per mol of subunit, required both for activity and stability of enzyme tetramer
Manganese
-
when the Deinococcus radiodurans Mn2+SOD reacts with a substoichiometric amount of superoxide, Deinococcus radiodurans Mn3+SOD is produced
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
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
-
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
0.3 atoms of iron/manganese in ratio 2:1 per subunit
Mg2+
-
study on affinity for enzyme-DNA complex and binding parameters. Enzyme-DNA complex shows at least two binding sites for divalent metal ions
Mn
manganese superoxide dismutase; 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; manganese superoxide dismutase
Mn
cytosolic MnSOD isozymes, Mn binding sequence is DVWHHAYY; mitochondrial MnSOD isozymes, Mn binding sequence is DVWHHAYY
Mn
manganese superoxide dismutase; 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+
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; 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+
-
study on affinity for enzyme-DNA complex and binding parameters. Enzyme-DNA complex shows at least two binding sites for divalent metal ions
Mn2+
-
the enzyme selectively chooses the Mn ion as its native cofactor, although Co and Fe ions can stably substitute the Mn ion
Mn2+
-
MnSOD, the Mn ion is the only metal cofactor, 0.57 atom per polypeptide chain
Mn2+
a Mn-SOD, Mn2+ activates, the manganese-binding site is formed by conserved residues His260, His308, Asp392, and His396
Mn2+
-
a Fe,Mn-SOD, the purified enzyme contains 0.7 g-atom of Mn per mol enzyme
Mn2+
a cambialistic Fe/Mn-superoxide dismutase, 1.12 g-atom 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+
-
0.75 mol per mol of subunit; accepts iron and/or manganese as cofactor
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
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
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+
-
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+
-
a Cu,ZnSOD with 1.18 Zn2+ per enzyme subunit, binding structure, overview
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+
a Cu,Zn-superoxide dismutase; a Cu,Zn-superoxide dismutase
Zn2+
a Cu,Zn-superoxide dismutase; a Cu,Zn-superoxide dismutase
Zn2+
a Cu,Zn-superoxide dismutase, residues H63, H71, H80, and D83 are involved in Zn2+ binding
Zn2+
-
2 mol of Zn2+ per mol of enzyme; mitochondrial cyanide-sensitive enzyme
Zn2+
-
1.34-1.81 mol per mol of isoenzyme I; 1.9-20.0 mol per mol of isoenzyme II
Zn2+
the residues His47, His49, His64, His72, His81, and Asp121 are involved in metal binding
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron; overview: metal content
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron; overview: metal content
additional information
-
relevance of the zinc imidazolate bond to the redox properties
additional information
-
role of copper and zinc in protein conformation and activity
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
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron; 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; 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; no MnSOD and Cu/ZnSOD in Crypthecodinium cohnii; no MnSOD and Cu/ZnSOD in Crypthecodinium cohnii
additional information
no MnSOD and Cu/ZnSOD in Crypthecodinium cohnii; no MnSOD and Cu/ZnSOD in Crypthecodinium cohnii; no MnSOD and Cu/ZnSOD in Crypthecodinium cohnii
additional information
no MnSOD and Cu/ZnSOD in Crypthecodinium cohnii; no MnSOD and Cu/ZnSOD in Crypthecodinium cohnii; no MnSOD and Cu/ZnSOD in Crypthecodinium cohnii
additional information
-
no MnSOD and Cu/ZnSOD in Crypthecodinium cohnii; no MnSOD and Cu/ZnSOD in Crypthecodinium cohnii; 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; overview: metal content
additional information
no enzyme activity with Fe2+-reconstituted enzyme
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron; overview: metal content
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron; overview: metal content
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron; overview: metal content
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron; overview: metal content
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; overview: metal content
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron; overview: metal content
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron; overview: metal content
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron; overview: metal content
additional information
-
no evidence for the presence of either iron or copper/zinc SODs in Phytophthora cinnamomi
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
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron; overview: metal content
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
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; overview: metal content
additional information
iron, manganese, and nickel contents are below the detection level
additional information
binding ligands: His27, His74, Asp157 and His161 in SodB; binding ligands: His27, His82, Asp169 and His173 in SodA
additional information
binding ligands: His27, His74, Asp157 and His161 in SodB; binding ligands: His27, His82, Asp169 and His173 in SodA
additional information
binding ligands: His27, His74, Asp157 and His161 in SodB; binding ligands: His27, His82, Asp169 and His173 in SodA
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
chloroform-ethanol
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
-
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
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)napthalen-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)napthalen-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-ethyl-5-phenylisoxazolium 3'-sulfonate
-
i.e. Woodwards reagent, Kat 50 mM
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
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
-
2-mercaptoethanol
gradual inhibition by increasing concentration of 2-mercaptoethanol, 20% inhibition at 2 mM, 36% at 16 mM
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
cyanide
-
the isoenzyme Cu/Zn-SOD is cyanide-sensitive, while the Mn-SOD is not
diethyldithiocarbamate
-
inhibits recombinant Cu,Zn-SOD, at 0.05-0.1 mM inactivation occurs gradually within 1 h
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
inhibits SodC specifically
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
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
inactivation of FeSOD; inactivation of FeSOD; inactivation of FeSOD
H2O2
gradual inhibition by increasing concentration of H2O2, 36% inhibition at 2 mM, 81% at 16 mM
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
half-life of 22 min both in absence or presence of 2-mercaptoethanol
H2O2
distinguishes Fe-SOD from Mn-SOD, since it inactivates only Fe-SOD
Iodine
-
completely inhibits the cell wall SOD, the inhibition is partly, up to 70%, reversed by 2-mercaptoethanol
N3-
-
Mn-SOD is inhibited by 50%, enzyme reconstituted by Fe3+ shows increased 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
50% inhibition at 6.9 mM in absence, at 9.0 mM in presence of 2-mercaptoethanol
NaN3
-
inhibits the enzyme mutants Y41F and H155Q, but not the wild-type enzyme
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
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
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
additional information
-
no inhibition by hydrogen peroxide or potassium cyanide
-
additional information
no inhibition by hydrogen peroxide or potassium cyanide
-
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
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
-
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
-
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
-
ligand complex synthesis, electrochemical properties, and structure determination, overview
-
additional information
-
no inhibition of Cu/ZnSOD by 10 mM H2O2, 1 mM CaCl2, and 1 mM NaN3
-
additional information
-
the enzyme is not inhibited by cyanide (10 mM)
-
additional information
the enzyme is not inhibited by cyanide (10 mM)
-
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
-
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
-
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 of Cu,Zn-SOD by sodium azide and O-phenanthroline
-
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 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
-
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
not inhibitory: sodium dodecylsulfate
-
additional information
imidazole up to 0.8 M and sodium dodecylsulfate up to 4% are not inhibitory
-
additional information
-
imidazole up to 0.8 M and sodium dodecylsulfate up to 4% are not inhibitory
-
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
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8-Hydroxyquinoline-5-sulfonate
-
Fe-SOD, slightly stimulating, depending on the assay method
corticotrophin
-
enzyme activity in the inner zone mitochondria of adrenal gland is enhaced by corticotrophin and by a low-sodium diet
-
malathion
-
subchronic exposure to malathion increases the enzyme activity in liver by 11%
o-phenanthroline
-
depending on assay method; Fe-SOD, slightly stimulating
sulfhydryl compounds
-
e.g. reduced glutathione, cysteine, 2-mercaptopropionylglycine activate
additional information
-
tributyltin chloride does not affect enzyme expression
-
additional information
tributyltin chloride does not affect enzyme expression
-
additional information
-
rosuvastatin induces the enzyme in aortic extracts and restores the enzyme expression in DKO mice with combined leptin and LDL-receptor deficiency, leading to less oxLDL accumulation within atherosclerotic plaques and inhibition of plaque progression, and restores enzyme expression in THP-1 macrophages and foam cells, overview
-
additional information
-
teneurin carboxy-terminal associated peptide-1, i.e. TCAP-1, upregulates the enzyme expression, shows neuroprotective activity, and is implicated in the regulation of neuron growth and differentiation, the TCAP-teneurin system may be part of a mechanism to protect neurons during trauma, such as hypoxia and ischemia, overview
-
additional information
-
no effect on the enzyme by alpha-tocopherol in absence of diethyldithiocarbamate
-
additional information
-
activation of intermembrane space SOD1 upon oxidation of critical thiols. 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
-
additional information
-
the enzyme is 5fold induced by iron starvation
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
evaluation of catalytic rate constant as a function of ionic strength and copper and zinc content. rate constant increases with ionic strength up to 1500000000 per M and s at an ionic strength of 15 mM, and decreases thereafter
-
additional information
additional information
pH-dependence of KM-value reflects the inhibition of anion binding by ionized Y34
-
additional information
additional information
-
ratio kcat/Km per microM and s: wild-type, 800, mutant C140S, 800, mutant N73S, 470, mutant Q143A, 3.1, mutant N73S/Q143A, 13, mutant N73S/C140S/Q143A, 15
-
additional information
additional information
-
kinetics of recombinant wild-type and mutant enzymes
-
additional information
additional information
-
rate constants and kinetic mechanism
-
additional information
additional information
-
rate constants and kinetics compared to other SODs from other species, overview
-
additional information
additional information
-
steady-state kinetics with artificial substrates, overview
-
additional information
additional information
-
infection with pathogen Puccinia striiformis f.sp. tritici alters the kinetic properties of the cell wall enzyme, kinetics of enzymes from infected and uninfected leaaves with pyrogallol, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Bos taurus
-
determination of catalytic rate constant by pulse irradiation and cytochrome c assay after addition of EDTA to eliminate excess copper. kcat Value is 2820000000 per M and s at low ionic strength and 1300000000 per M and s in presence of 50 mM phosphate, pH 7.8
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
17.3
-
purified extracellular enzyme, pyrogallol autoxidation inhibition assay method
151.9
purified recombinant enzyme, pH and temperature not specified in the publication
178.7
recombinant wild-type SOD1, pH not specified in the publication, temperature not specified in the publication
289
pH 8.0, apoprotein reconstitued in presence of manganese and iron
434
recombinant Fe2+-reconstituted enzyme, pH and temperature not specified in the publication
500
purified native enzyme, pH not specified in the publication, temperature not specified in the publication
800
-
isoform FeSOD, pH not specified in the publication, temperature not specified in the publication
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
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
3788
recombinant SOD1 mutant P143S/P145L, pH not specified in the publication, temperature not specified in the publication
4200
purified recombinant enzyme, pH and temperature not specified in the publication
8600
-
isoform MnSOD, pH not specified in the publication, temperature not specified in the publication
additional information
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
-
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
dimeric form shows 65% higher activity than monomeric form
additional information
-
Fe-SOD and Mn-SOD activity in Flavobacteria
additional information
-
activity in egg white and yolk during storage, overveiw
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
Cu/Zn-SOD activity in overexpressing cells from different culture conditions, overview
additional information
-
Fe-SOD and Mn-SOD activity in Flavobacteria
additional information
-
development of a 96-well-plate mircoassay for enzyme activity
additional information
-
Fe-SOD and Mn-SOD activity in Flavobacteria
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
-
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+
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
7 - 11
7.4
7.5
7.8
8.2
8.5
8.9
10.2
additional information
6
-
both wild-type and fusion protein with the N-terminal domain of superoxide dismutase from Geobacillus thermodenitrificans NG80-2
7 - 11
native and recombinant Cu,Zn-SOD, activity is pH-independent
additional information
-
the inaccessibility of a direct activity assay also excludes determination of a pH- or temperature-optimum
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 9
-
activity range, the enzyme shows 30% of maximal activity at pH 10.0 and is inactive at pH 11.0
3 - 11
-
pH-profile, overview. Outside the range of 5.0-7.0, activity is rapidly lost
4 - 12
-
90% of maximal activity at pH 5.6-pH 7.5, 15% at pH 4.0, 60% at pH 12.0, 25°C, pH profile, overview
4 - 12
Rhodothermus sp.
-
inactivation at pH 2.0, shrap drop of activity below pH 4.0, high activity at pH 4.0-pH 5.0, about 70% of maximal activity at pH 6.0-12.0
5 - 10
6 - 11
6 - 10.6
7 - 11
native and recombinant Cu,Zn-SOD, activity is pH-independent
7 - 10
maximal activity at pH 7.6, 50% of miximal activity at pH 8.5, inactivation above pH 10.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
21
22
25
37
55
60
70
95
-
stable, the inaccessibility of a direct activity assay also excludes determination of a pH- or temperature-optimum
60
-
fusion protein with the N-terminal domain of superoxide dismutase from Geobacillus thermodenitrificans NG80-2
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 90
40°C: about 50% of maximal activity, 90°C: 75% of maximal activity; activity range, profile overview
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.8
4.55
-
isoform with molecular weight of 130 kDa, CuZn-type, induction by exposure of mussels to copper
5.31
5.33
5.9
6.2
6.8
additional information
isoelectric focusing reveals four isoelectric variants in the recombinant JcCu/Zn-SOD, with pI values of 7.04, 7.33, 8.62, and 8.77
5.31
SOD1, sequence calculation; SOD1, sequence calculation; SOD1, sequence calculation
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
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
accumulation of sodA mRNA in conidia, semi-quantitative expression analysis
-
germinated cyst, isoform MnSOD2 and low levels of isoform MnSOD1
-
Cu/Zn-superoxide dismutase isozymes; plasma, isozyme pattern, overview
-
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
-
changes in SOD activity in boar sperm during preservation at 16°C, overview
-
dogs with unilateral testicular tumor or unilateral cryptorchid testis, and with or without Sertoli cell tumor, seminoma and/or Leydig cell tumor
-
in rats with hepatic necrosis after treatment with tetrachlorcarbon
additional information
-
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
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
-
Cu,Zn-SOD, in vessels, including endothelium; Mn-SOD, endothelium
-
Cu,Zn-SOD, in vessels, including endothelium; Mn-SOD, endothelium
-
real time quantitative PCR expression analysis of cytoplasmic Cu,Zn-SOD
-
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
-
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
semi-quantitative expression analysis, the expression is down regulates in the mycelium phase
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; 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
enzyme overexpression; enzyme overexpression
additional information
-
optimal conditions for growth of this organism are 82-92°C, pH 3.0-4.0
additional information
optimal conditions for growth of this organism are 82-92°C, pH 3.0-4.0
additional information
tissue specific expression of SOD, no activity in gonad and mantle
additional information
bamboo SODs show developmental and tissue-specific regulation, unique fast-growth phenotype of green bamboo; bamboo SODs show developmental and tissue-specific regulation, unique fast-growth phenotype of green bamboo
additional information
bamboo SODs show developmental and tissue-specific regulation, unique fast-growth phenotype of green bamboo; bamboo SODs show developmental and tissue-specific regulation, unique fast-growth phenotype of green bamboo
additional information
-
quantitative determination of an isotopically enriched metalloenzyme containing two different metal isotopes, method development, overview
additional information
-
MnSOD-2 is constitutively expressed, while synthesis of MnSOD-3 is inducible
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
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
-
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
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
additional information
-
measurement of serum and urinary PC-SOD concentrations after application of exogenous recombinant human isozyme to male and female humans, overview
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
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
additional information
-
cultivation on bean seeds of Phaseolus vulgaris, root colonization and growth of wild-type and mutant strains, overview
additional information
-
overview: content of Cu,Zn-SOD and Mn-SOD in rat tissues
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
additional information
-
overview: content of Cu,Zn-SOD and Mn-SOD in rat tissues
-
additional information
-
overview: content of Cu,Zn-SOD and Mn-SOD in rat tissues
-
additional information
-
quantitative real-time PCR enzyme expresion analysis
additional information
constant expression in plerocercoid larvae and adult worms
additional information
-
constant expression in plerocercoid larvae and adult worms
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
additional information
the enzyme expression is upregulated in the yeast phase
additional information
-
the enzyme expression is upregulated in the yeast phase
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
intermediate form between Fe- and Mn-SOD, contains Zn2+, associated with outer cell wall and selectively secreted into the medium
-
intermediate form between Fe- and Mn-SOD, contains Zn2+, associated with outer cell wall and selectively secreted into the medium
-
-
extracellular Fe-SOD, associated with cell-surface
-
-
one copper chaperone gene for superoxide dismutase is responsible for the activation of cytosolic, peroxisomal and chloroplast enzyme
determined from amino acid sequence and structure analysis; determined from amino acid sequence and structure analysis; determined from amino acid sequence and structure analysis
-
one copper chaperone gene for superoxide dismutase is responsible for the activation of cytosolic, peroxisomal and chloroplast enzyme
-
of vegetative cells and heterocysts, i.e. nitrogenase containing specialized cells formed during nitrogen-limiting conditions
-
; it comprises at least 11% of the cytosolic protein
-
enzyme SOD3 is secreted; enzyme SOD3 is secreted
-
enzyme SOD3 is secreted; enzyme SOD3 is secreted
-
-
MnSOD is translated in the cytoplasm and then imported into the mitochondria via a mitochondrial targeting signal
two potential distinct mMnSOD isoforms presenting particular peptide signals
the enzyme contains an N-terminal mitochondrial targeting sequence
two potential distinct mMnSOD isoforms presenting particular peptide signals
the enzyme contains a highly conserved mitochondria-targeting signal
two potential distinct mMnSOD isoforms presenting particular peptide signals
the enzyme possesses a unique 35 amino acid mitochondrial targeting sequence at the N-terminus
-
Cu,Zn-dependent enzyme, occurence together with light-harvesting complexes, post-transcriptional regulation
-
-
one copper chaperone gene for superoxide dismutase is responsible for the activation of cytosolic, peroxisomal and chloroplast enzyme
additional information
-
cytosolic Mn-SOD resembles the chloroplast enzyme of higher plants
-
additional information
-
cytosolic Mn-SOD resembles the chloroplast enzyme of higher plants
-
-
additional information
-
subcellular localization study of SOD1, overview
-
additional information
-
subcellular localization study of SOD1, overview
-
-
additional information
-
SODI and SODII also occur in low mass organelles
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Acidilobus saccharovorans (strain DSM 16705 / JCM 18335 / VKM B-2471 / 345-15)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Haemophilus ducreyi (strain 35000HP / ATCC 700724)
Haemophilus ducreyi (strain 35000HP / ATCC 700724)
Helicobacter pylori (strain ATCC 700392 / 26695)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Pseudoalteromonas haloplanktis (strain TAC 125)
Pseudoalteromonas haloplanktis (strain TAC 125)
Pseudoalteromonas haloplanktis (strain TAC 125)
Pseudoalteromonas haloplanktis (strain TAC 125)
Pseudoalteromonas haloplanktis (strain TAC 125)
Pseudoalteromonas haloplanktis (strain TAC 125)
Pseudoalteromonas haloplanktis (strain TAC 125)
Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Yersinia pseudotuberculosis serotype I (strain IP32953)
Yersinia pseudotuberculosis serotype I (strain IP32953)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15000
15700
x * 15700, about, cytoplasmic CuZn-SOD, sequence calculation
15800
15960
2 * 15960, sequence calculation, 2 * 17000, recombinant enzyme, SDS-PAGE
16000
16385
1 * 16385, sequence calculation, 1 * 16400, about, recombinant His6-and thioredoxin-tagged enzyme, mass spectrometry and SDS-PAGE
16400
16500
16800
17000
18000
18300
18500
19500
20000
21000
21251
2 * 21251, mass spectrometry, 2 * 22000, SDS-PAGE
21500
21700
22000
22321
-
4 * 22321, MALDI-TOF, 4 * 24000-25000, SDS-PAGE in absence, 4 * 25000, in presence of 2-mercaptoethanol
22400
23000
23500
23600
Rhodothermus sp.
-
2 * 23600, about, recombinant enzyme, sequence calcualtion, 2 * 25000, recombinant enzyme, SDS-PAGE
23652
2 * 23652, SOD1, sequence calculation; 2 * 23652, SOD1, sequence calculation; 2 * 23652, SOD1, sequence calculation
24000
24270
-
2 * 24270, calculated from sequence; 2 * 24270, sequence calculation
24577
-
in crystals, 4 * 24577, sequence calculation and gel filtration; in solution, 2 * 24577, sequence calculation and gel filtration
24800
25000
25400
26000
27000
28000
30000
30500
30800 - 31600
-
mitochondrial cyanide-sensitive enzyme, gel filtration, sedimentation equilibrium analysis
31000 - 33000
31000
31200
32000 - 32500
32000
33000
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
35000
36000
37400
38500
39800
40000
41500
42000 - 43000
42000
43000
44000
45000
46000
47000
48000
50000
52000
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
56000
59000
60000
61000
69000
80000
82000
85000
87900
88000
91000
96000
97000
x * 106000, or x * 97000, SDS-PAGE, differently glycosylated protein forms
100000
106000
x * 106000, or x * 97000, SDS-PAGE, differently glycosylated protein forms
additional information
15800
2 * 42000, recombinant GST-tagged SeCuZnSOD, SDS-PAGE, 2 * 15800, untagged enzyme, SDS-PAGE
16400
about, recombinant His6-and thioredoxin-tagged enzyme, mass spectrometry
17000
2 * 15960, sequence calculation, 2 * 17000, recombinant enzyme, SDS-PAGE
19500
amino acid sequence determination, SDS-PAGE; native Cu,Zn-SOD
21500
amino acid sequence determination; recombinant Cu,Zn-SOD; SDS-PAGE
22000
2 * 21251, mass spectrometry, 2 * 22000, SDS-PAGE
22400
-
2 * 22400, calculated from sequence; 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
25000
-
4 * 22321, MALDI-TOF, 4 * 24000-25000, SDS-PAGE in absence, 4 * 25000, in presence of 2-mercaptoethanol
25000
Rhodothermus sp.
-
2 * 23600, about, recombinant enzyme, sequence calcualtion, 2 * 25000, recombinant enzyme, SDS-PAGE
27000
-
and dimer and octamer, 4 * 27000, SDS-PAGE; and dimer and tetramer, 8 * 27000, SDS-PAGE; and tetramer and octamer, 2 * 27000, SDS-PAGE
30000
-
Cu,Zn-SOD isoenzyme I, gel filtration, sedimentation equilibrium centrifugation
31200
-
Cu,Zn-SOD, sedimentation equilibrium centrifugation analysis
33000
-
Cu,Zn-SOD isoenzyme II, gel filtration, sedimentation equilibrium analysis
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
42000
2 * 42000, recombinant GST-tagged SeCuZnSOD, SDS-PAGE, 2 * 15800, untagged enzyme, SDS-PAGE
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
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
homotetramer
monomer
monomer or dimer
tetramer
trimer or tetramer
additional information
?
x *17000, recombinant SOD1, SDS-PAGE, x * 45000, recombinant SOD1-Lys7, SDS-PAGE
?
Beauveria bassiana 2860
-
x *17000, recombinant SOD1, SDS-PAGE, x * 45000, recombinant SOD1-Lys7, SDS-PAGE
-
?
x * 15500, calculated, x * 16000, SDS-PAGE; x * 25400, calculated, x * 28000, 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 * 15764-15809, Cu,Zn-SOD wild-type and mutant D90A, electrospray mass spectroscopy
-
?
x * 45000, SDS-PAGE of native protein, x * 34000-38000 and x * 29000-33000, SDS-PAGE of deglycosylated protein
?
-
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 * 22000, SDS-PAGE; x * 24000, SDS-PAGE; x * 26873, calculated; x * 36031, calculated
dimer
Anas platyrhynchos domestica CuZn-SOD
-
2 * 16000, Cu,Zn-SOD, SDS-PAGE
-
dimer
-
2 * 16000, Cu,Zn-SOD, SDS-PAGE; 2 * 22000, Mn-SOD, SDS-PAGE
-
dimer
2 * 23652, SOD1, sequence calculation; 2 * 23652, SOD1, sequence calculation; 2 * 23652, SOD1, sequence calculation
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
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 * 21251, mass spectrometry, 2 * 22000, SDS-PAGE
dimer
Rhodothermus sp.
-
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
-
; 2 * 16000, Cu,Zn-SOD, SDS-PAGE; 2 * 18300, Cu,Zn-SOD, SDS-PAGE; cytoplasmic enzyme
-
dimer
-
2 * 24270, calculated from sequence; 2 * 24270, sequence calculation
dimer
-
2 * 22400, calculated from sequence; 2 * 24270, calculated from sequence
-
homodimer
-
2 * 34034, sequence calculation and mass spectrometry
-
homodimer
2 * 42000, recombinant GST-tagged SeCuZnSOD, SDS-PAGE, 2 * 15800, untagged enzyme, SDS-PAGE
homodimer
2 * 15960, sequence calculation, 2 * 17000, recombinant enzyme, SDS-PAGE
homotetramer
-
in crystals, 4 * 24577, sequence calculation and gel filtration
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 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
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 * 24000, SDS-PAGE; 4 * 24204, calculated from sequence
tetramer
-
4 * 25000, Mn-SOD, reducing SDS-PAGE; mitochondrial enzyme
-
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
-
additional information
-
three-dimensional structure modelling, overview
additional information
three-dimensional structure modelling, overview
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
homology structure modeling of PgCuZnSOD, overview
additional information
-
the enzyme contains the sequence TLPDLKYD at the N-terminus
additional information
-
the enzyme contains the sequence TLPDLKYD at the N-terminus
-
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; SOD1 possesses a short amino-terminal extension which could represent, in this heterotrophic dinoflagellate lacking a chloroplast, a putative mitochondrial targeting signal; 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; SOD1 possesses a short amino-terminal extension which could represent, in this heterotrophic dinoflagellate lacking a chloroplast, a putative mitochondrial targeting signal; 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; SOD1 possesses a short amino-terminal extension which could represent, in this heterotrophic dinoflagellate lacking a chloroplast, a putative mitochondrial targeting signal; 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; SOD1 possesses a short amino-terminal extension which could represent, in this heterotrophic dinoflagellate lacking a chloroplast, a putative mitochondrial targeting signal; 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
modelling of the three-dimensional structure of SOD monomer, overview
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
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; 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; 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; 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
-
immunoblot analysis shows isoforms of 25 and 75 kDa with increased expression of the 75 kDa isoform after treatment with corticotrophin
additional information
-
secondary, quarternary and three-dimensional structure
additional information
-
secondary, quarternary and three-dimensional structure
-
additional information
-
secondary structure analysis by CD spectroscopy, the enzyme has a high alpha-helical content of 70%, overview
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; 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; 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; 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; 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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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
no glycoprotein
the enzyme sequence lacks any putative glycosylation sites
phosphoprotein
the enzyme sequence shows the presence of putative sites of phosphorylation
proteolytic modification
additional information
glycoprotein
-
Cu/Zn-SOD from mitochondrial intermembrane space and cytosol is glycosylated
glycoprotein
-
Cu/Zn-SOD from mitochondrial intermembrane space and cytosol is glycosylated
-
glycoprotein
-
the enzyme contains carbohydrate at 1200 kDa, it is associated with carbohydrate components comprising at least 4 monosugars, D-xylose, D-mannose, D-galactose and N-acetyl-D-glucosamine
glycoprotein
-
the enzyme contains carbohydrate at 1200 kDa, it is associated with carbohydrate components comprising at least 4 monosugars, D-xylose, D-mannose, D-galactose and N-acetyl-D-glucosamine
-
glycoprotein
sequence contains four potential N-glycosylation sites. Three of them, N43, N115, N172, are modified
glycoprotein
-
biantennary nonasaccharide with composition (GlnNAc)4:Man3:Xyl:Fuc; nectarin I: Mn-SOD
proteolytic modification
sequence codes for a protein of 245 amino acids with potential precursor cleavage site between Y20-L21
proteolytic modification
precursor protein with seven additional N-terminal amino acids
additional information
-
resistant to proteolysis by trypsin and chymotrypsin
additional information
resistant to proteolysis by trypsin and chymotrypsin
additional information
disulfide bridges are homogenous and identical to human active extracellular enzyme. Rabbit enzyme exists only in enzymatically active form
additional information
sequence contains an amino terminal extension of 35 residues; sequence contains an amino terminal extension of 97 residues
additional information
sequence contains an amino terminal extension of 35 residues; sequence contains an amino terminal extension of 97 residues
additional information
sequence contains an amino terminal extension of 35 residues; sequence contains an amino terminal extension of 97 residues
additional information
sequence contains an amino terminal extension of 35 residues; sequence contains an amino terminal extension of 97 residues
additional information
the enzyme sequence shows the presence of putative sites of disulphide bonds
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
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
purified recombinant Mn-SOD enzyme, X-ray diffraction structure determination and analysis at 2.0 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 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
-
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
-
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
-
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 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
-
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
-
extracellular enzyme, tetraborate crystallization of ethanolic enzyme extract, then recrystallization from buffer than from water
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 9
-
the pH stability of the enzyme is enhanced by the polysialylation, after 1 h at pH 2-3, the residual enzyme activity of polysialylated SOD is 64-74%, while the native SOD shows quickly decreased activity to 20-38%
714572
2.2 - 10.2
purified recombinant enzyme, 10 min, 87% activity within this range remaining, rapid loss above pH 10.2
728279
3 - 10.8
-
30 min, pH 3.0: about 30% loss of activity, pH 10.8: rapid inactivation above
438166
3 - 8
-
fusion protein with the N-terminal domain of superoxide dismutase from Geobacillus thermodenitrificans NG80-2, more than 90% of initial activity
737269
4 - 9
-
the purified native enzyme exhibits high thermal stability at 70°C over the pH range from pH 4.0 to pH 9.0
714399
5 - 9
the purified recombinant enzyme is relatively stable at pH 5.0-9.0, and retains more than 70% of full activity at pH 5.5-8.0
714576
5 - 11
5.5 - 9.5
purified recombinant His-tagged enzyme, 25°C, 1 h, good stability
727206
6 - 9
Radix lethospermi
-
25°C
659568
6
-
purified enzyme, after 45 min 80% activity is remaining, after 120 min 60% activity is remaining
728648
6.5 - 8
-
rapid inactivation below pH 6.5 and above pH 8.0, 60% remaiining activity at pH 7.8 after 10 min at 25°C
704820
7 - 8
-
purified enzyme, after 60 min 80% activity is remaining, after 120 min 70% activity is remaining
728648
additional information
4
-
purified enzyme, after 10 min 80% activity is remaining, after 120 min less than 40% activity is remaining
728648
additional information
-
the recombinant purified enzyme is highly stable at neutral and alkaline pHs but is relatively unstable in acidic condition
706067
additional information
the recombinant purified enzyme is highly stable at neutral and alkaline pHs but is relatively unstable in acidic condition
706067
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
10 - 50
purified recombinant enzyme, 10 min, 83% activity within this range remaining
20 - 90
secondary structure of SOD_ASAC is stable within this temperature range
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
37
40 - 90
over 50% activity within this range, most stable at 70°C, profile overview
40
44.5
purified recombinant His-tagged enzyme, 60 min, loss of 50% activity
45
50
50 - 60
50
50 - 60
purified recombinant His-tagged enzyme, 60 min, over 80% activity remaining
50
50
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
55
60
60
65
half-life of 14.7 min, thermal inactivation rate constant Kd of 0.0321 per min
70
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 nezyme is almost inactivated after incubation for 3 h, while the polysialylated SOD still has 49-61% residual activities
70
71 - 73
-
half-inactivation occurring after 10 min exposure at 71-73°C, depending on the bound metal
75
80
80
85
90
95
100
105
110
additional information
37
purified recombinant His-tagged enzyme, 48 h, over 80% activity remaining
40
-
purified enzyme, completely stable after 20 min, after 1 h, 98% remaining activity of the leaf enzyme, 88% of the rhizome enzyme
40
-
purified enzyme, 90 min, completely stable, 90% activity remaining after 120 min
45
purified recombinant His-tagged enzyme, 40 min, 50% activity remaining
50
purified recombinant His-tagged enzyme, completely stable for 6 h, after 48 h 30% activity remaining
60
-
5 min, complete inactivation of isoenzyme B, 50% loss of isoenzyme A activity
60
the puurified recombinant enzyme retains 93% of maximal activity after 60 min
60
-
purified enzyme, completely stable after 20 min, after 1 h, 90% remaining activity of the leaf enzyme, 70% of the rhizome enzyme
60
purified native enzyme, 95% remaining activity after 60 min
70
Anas platyrhynchos domestica
-
recombinant Cu,Zn-SOD, after 2 h 20% activity remaining, after 3 h all activity is lost
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
purified recombinant enzyme, retains 65% of the maximum activity at 70°C for 60 min
70
purified recombinant enzyme, 60 min, 75% activity remaining
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 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 native enzyme, 55% remaining activity after 60 min
70
purified recombinant enzyme, 65% remaining activity after 60 min
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
80
purified recombinant enzyme, 66 h, 50% activity remaining
80
purified recombinant enzyme, 25 min, 50% activity remaining
80
-
purified enzyme, completely stable after 20 min, after 1 h, 80% remaining activity of the leaf enzyme, 52% of the rhizome enzyme
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
Rhodothermus sp.
-
purified recombinant enzyme, 40% remaining activity after 30 min, complete inactivation after 4 h
90
purified recombinant enzyme, 30 min, 20% activity remaining
90
dimer: half-life 99 min, dimeric form is more stable than monomeric form
90
-
purified native enzyme, with 67.8% activity remaining after 10 min at pH 7.4
90
purified recombinant enzyme, 20% remaining activity after 50 min
95
2 h, purified recombinant enzyme, 96% remaining activity, half-life is 33 h, inactivation according to first order kinetics
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
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, 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
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
-
purified recombinant enzyme, 20% activity remaining activity after 30 min
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
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
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
-
comparison of thermostability of various Gluconobacter strains
additional information
-
activation energy for enzyme thermal denaturation, 143.5 kJ per mol
additional information
-
thermal stability of Mn-SOD at several temperatures, enzyme is more labile at higher temperatures
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
-
phenylmethanesulfonyl fluoride attachment to the active site Tyr41 increases the heat stability of the enzyme, overview
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
3 cycles of freezing and thawing cause less than 20% loss of activity, Mn-SOD
-
activity of the SOD remains intact both in crude and purified forms after autoclaving at 6-20 bars up to 10 min and microwaving at a frequency of 2450 MHz or million cycles per second for 1-3 min
-
dimethyl sulfoxide: Spirulina enzyme is stable up to 55%, Rhodopseudomonas enzyme up to 70% v/v
due to high salt requirement for enzyme stability purification is performed in presence of 2 M NaCl
-
incubation with proteases (e.g. trypsin, V8 Staphylococcus aureus protease) has no effect on this enzyme
-
SDS decreases the stability of SOD and accelerates enzyme inactivation
-
the enzyme is remarkably stable at high temperatures and even under denaturing conditions
-
the purified enzyme is stable in 6 M guanidinium chloride for 72 h loosing only 33% activity
-
urea: 8 M, 0°C, isoenzyme I unfolds immediately, isoenzyme II stays folded
-
dimethyl sulfoxide: Spirulina enzyme is stable up to 55%, Rhodopseudomonas enzyme up to 70% v/v
-
dimethyl sulfoxide: Spirulina enzyme is stable up to 55%, Rhodopseudomonas enzyme up to 70% v/v
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
chloroform
dimethyl sulfoxide
guanidine-HCl
SDS
additional information
guanidine-HCl
-
6 M, incubation for 72 h, 67% of the initial activity is retained
guanidine-HCl
-
after 72 h incubation with 6 M guanidinium hydrochloride at 2O°C, 67% of its enzymatic activity is retaine
guanidine-HCl
-
6 M, incubation for 72 h, 67% of the initial activity is retained; after 72 h incubation with 6 M guanidinium hydrochloride at 2O°C, 67% of its enzymatic activity is retaine
-
SDS
-
incubation with 0.1% SDS shows no effect on the enzyme. Simultaneous treatment with low SDS concentrations and heat results in an almost quantitative conversion into a second form of the enzyme with a molecular mass of 87000 Da. It is most likely a tetramer. The specific activity of the tetrameric form is 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
SDS
-
incubation with 0.1% SDS shows no effect on the enzyme. Simultaneous treatment with low SDS concentrations and heat results in an almost quantitative conversion into a second form of the enzyme with a molecular mass of 87000 Da. It is most likely a tetramer. The specific activity of the tetrameric form is 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
-
additional information
-
chloroform/ethanol is used during purification of Fe-SOD and for detection of Cu,Zn-SOD, acetone precipitation
additional information
-
Mn-SOD and Fe-SOD: not stable to organic solvents, Cu,Zn-SOD: stable to organic solvents
additional information
-
Mn-SOD and Fe-SOD: not stable to organic solvents, Cu,Zn-SOD: stable to organic solvents
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
DNA binding protein-like protein, superoxide dismutase, and peroxiredoxin interact and likely form a supramolecular complex for mitigating oxidative damage
-
726264
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, loss of 50% of activity during one cycle of freezing and thawing, addition of 50% ethylene glycol preserve activity at -20°C
-
16°C, changes in superoxide dismutase activity in boar sperm during preservation, overview
-
isolated CuZnSOD shows activity that is stable under a broad range of pH and temperature treatments, even at room temperature for more than 3 days
isolated MnSOD shows activity that is stable under a broad range of pH and temperature treatments, even at room temperature for more than 3 days
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
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 forms, 1 dimer and 1 monomer; recombinant His-tagged Cu,Zn-SOD from Escherichia coli
; overview: purification of extracellular superoxide dismutases
; recombinant His-tagged enzyme by nickel affinity chromatography from Escherichia coli strain Rosetta-gami(DE3)
analytical isolation of the enzyme in a 2D electrophoresis from strains KT2440 and PAO1, overview
-
Cu,Zn-SOD
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
-
extracellular enzyme
Fe-SOD
Fe-SOD; native extracellular enzyme to homogeneity from the culture medium by ultrafiltration, gel filtration, dialysis, and anion exchange chromatography
-
four isozymes by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration. SODI is purified 424fold, SODII 635fold, SODIII 336fold, and SODIV 489fold
-
Mn-SOD
Mn-SOD from liver
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 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
-
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 mitochondrial intermembrane space of livber microsomes
-
native enzyme from post-ribosomal supernatant by anion exchange, hydrophobic interaction, and hydroxyapatite chromatography, followed by gel filtration, to homogeneity
-
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 to homogeneity by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography
native enzyme, and recombinant enzyme from Escherichia coli strain JM109(DE3)
-
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
partially
recombinant Cu, ZnSOD from Pichia pastoris strain GS115 by anion exchange chromatography
recombinant Cu,ZnSOD from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, cleavage of the GST fusion protein; recombinant MnSOD 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 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 Pichia pastoris strain GS115 by anion exchange chromatography
recombinant enzyme from Pichia pastoris strain GS115 by dialysis and anion exchange chromatography
recombinant GST-tagged SeCuZnSOD from Escherichia coli by glutathione 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 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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 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 wild-type and mutant enzymes and His-tagged SOD1-Lys7 from Escherichia coli 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 Mn-SOD from Escherichia coli strain QC774 by anion exchange chromatography
-
recombinant SOD1 from Leishmania tarentolae strain P10 to 90% purity by ultracentrifugation, hydrophobic interaction chromatography and dialysis
-
recombinant soluble enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
soluble recombinant enzyme from Escherichia coli by ammonium sulfate fractionation and anion exchange chromatography to homogeneity
recombinant enzyme from Pichia pastoris strain GS115 by anion exchange chromatography
recombinant enzyme from Pichia pastoris strain GS115 by anion exchange chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Rhodothermus sp.
-
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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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
atypical SOD, functional and structural intermediate between Fe-SOD and Mn-SOD, expression in Escherichia coli
-
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, overexpression in Escherichia coli
Cu,Zn-SOD, overexpression of wild-type and mutants in Spodoptera frugiperda cells Sf21 via baculovirus infection
-
cytosolic MnSOD isozyme, DNA and amino acid sequence determination and analysis, phylogenetic analysis, sequence comparison, quantitative real-time RT-PCR expression analysis; mitochondrial 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, 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, 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 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)
Rhodothermus sp.
-
EC-SOD, overexpression in Escherichia coli as His-tagged protein and in Tn-5B1-4 cells of Trichoplusia ni via baculovirus infection
-
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; expression analysis in homozygous LDL-receptor-knockout mice, heterozygous ob/+, and wild-type C57BL6 mice
-
expression in Escherichia coli
expression in Escherichia coli; 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)
expression in Pichia pastoris, DNA and amino acid sequence determination and comparison
expression of recombinant chimera MnSOD-VHb in Escherichia coli strain BL21(DE3)
-
expression of wild-type and mutant enzymes in Escherichia coli strain JM109(DE3)
-
Fe-SOD, expression in Escherichia coli, DNA and amino acid sequence determination
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 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 MSD1, DNA and amino acid sequence determination and analysis, expression as GST-tagged protein in Escherichia coli strain BL21(DE3)
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
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
-
gene cz1, expression of Cu,ZnSOD in Pichia pastoris strain GS115
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 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
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, 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 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 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 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
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
-
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
-
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 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 sodC, SodC cannot be expressed in Escherichia coli strain BL21(DE3)
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, overexpression of the His6-tagged type A isozyme 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
-
Mn-SOD, expression in Escherichia coli as His-tagged protein, DNA sequence analysis; overexpression in Saccharomyces cerevisiae mutant lacking Cu,Zn-SOD, restores activity of the mutant
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; 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; 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 of wild-type and mutant enzymes in hind limb muscle of transgenic mice
-
single copy gene, DNA and amino acid sequence determination and analysis
SOD, DNA and amino acid sequence determination and analysis, promoter analysis, phylogentic tree
subcloning in Escherichia coli, expression of iron-SOD or manganese-SOD in and complementation of an enzyme-deficient double mutant strain
-
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; 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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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
4 constitutive isozymes, 3 cold-inducible isozymes in bulbs, at 4°C, overview
-
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
-
challenge with Vibrio anguillarum increases Mm-icCu/Zn-SOD expression
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
-
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
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 expression of the enzyme is increased in plerocercoid larvae after treated with paraquat and significantly induced under oxidative stress
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
P143S/P145L
Y34F
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
D90A
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
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
G85R
G93A
G93R
-
an amyotrophic lateral sclerosis-associated naturally occuring SOD mutant, misfolding/aggregation mechanism with folding and unfolding kinetics, overview
H43R
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
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
-
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
-
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
additional information
P143S/P145L
site-directed mutagenesis, gain-of-function, the mutant shows increased activirty compared to the wild-type SOD1
P143S/P145L
Beauveria bassiana 2860
-
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
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
additional information
construction of two mutant strains KO1 and KOS, lacking either sodA-1 or both sodA-1 and sodA-2, through homologous recombination; 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; 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; 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; 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 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
Beauveria bassiana 2860
-
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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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; 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; 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
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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; naturally occuring hybrids between Fe-SOD and Mn-SOD, altered metal content
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additional information
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naturally occuring hybrids between Fe-SOD and Mn-SOD, altered metal content; naturally occuring hybrids between Fe-SOD and Mn-SOD, altered metal content
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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
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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
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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
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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
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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
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additional information
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phenotype of homozygous LDL-receptor-knockout mice, heterozygous ob/+, and wild-type C57BL6 mice, 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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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
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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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naturally occuring exchange of Arg-189 for Lys in the active site of Mn-SOD, sensitivity to lysine-modifying agents
additional information
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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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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
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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
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
after reconstitution with Fe3+ instead of Mn2+, the enzyme shows properties similar to Fe-SODs; Zn2+ inhibits reconstitution with Mn2+ or Fe3+
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apoprotein expressed in insect cells can be restored by addition of Cu2+, fully active
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enzyme folding and unfolding kinetic mechanism of wild-type and mutant enzymes at pH 7.8 and 25°C, role of metal ions, overview
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incubation of purified apoprotein with metal salts at ambient temperatures, no restauration of activity. Reactivation by heating apoprotein with manganese salts at elevated temperatures, both manganese and iron bind to protein, but only manganese restores activity. Mechanism of metallation
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reconstitution of active enzyme after withdrawal of metal by either Mn or Fe yielding an active enzyme irrespective of the metal ion initially present
reconstitution of active enzyme after withdrawal of metal either with the native metal or with cadmium, chromium or iron
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reconstitution of active enzyme after withdrawal of Mn2+ by addition of Mn2+ to apoprotein in 8 M urea at acid pH
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reconstitution of active protein after withdrawal of metal, higher activity with Mn2+, lower activity with Fe3+
reconstitution of Fe-SOD from purified recombinant apo-enzyme, apo-enzyme preparation: purified recombiant enzyme is denatured in buffer containing 50 mM acetate buffer, pH 3.8, 6 M guanidine hydrochloride, and 10 mM EDTA for 16 h at 50°C, followed by dialysis against the same buffer containing MnSO4 instead of EDTA, and removal of guanidine hydrochloride in a second dialysis step, followed by gel filtration, overview
reconstitution of active enzyme after withdrawal of metal by either Mn or Fe yielding an active enzyme irrespective of the metal ion initially present
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reconstitution of active enzyme after withdrawal of metal by either Mn or Fe yielding an active enzyme irrespective of the metal ion initially present
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reconstitution of active protein after withdrawal of metal, higher activity with Mn2+, lower activity with Fe3+
reconstitution of active protein after withdrawal of metal, higher activity with Mn2+, lower activity with Fe3+
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
biotechnology
diagnostics
drug development
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the enzyme is a target for development of antiangiogenic and antitumour drugs
environmental protection
Cu/Zn superoxide dismutase might be used as a bioindicator of the aquatic environmental pollution and cellular stress in pearl oyster
medicine
synthesis
agriculture
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soaking fish larva in enzyme solution protects fish from 100 ppm paraquat-induced oxidative injury
agriculture
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enzyme is a biochemical marker sufficient to identify a trypanosomatid isolated from a plant as belonging to the genus Phytomonas
agriculture
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concomitant expression of superoxide dismutase and ascorbate peroxidase in potato chloroplast results in enhanced tolerance of plants to 0.25 mM methyl viologen, and visible damage in transgenic plants is one-fourth that of control. In addition, transgenic plants are more resistant to elevated temperatures
biotechnology
transfection of the Ctsod gene may have great potential for the genetic improvement of salt tolerance in plants
biotechnology
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transfection of the Ctsod gene may have great potential for the genetic improvement of salt tolerance in plants
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diagnostics
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Cu,Zn-SOD is a urinary marker of hepatic necrosis, but not hepatic fibrosis, overview
diagnostics
the enzyme might be used to develop a biosensor for the detection of antioxidants and free radical activity
diagnostics
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the enzyme might be used to develop a biosensor for the detection of antioxidants and free radical activity
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medicine
recombinant protein is useful as serodiagnostic marker for identification of Aspergillus fumigatus infections, crossreactive antibodies
medicine
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investigations with help of mutants to elucidate structure-function relation in familial amyotrophic lateral sclerosis
medicine
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enzyme deletion mutants are avirulent in a murine model of inhaled cryptococcosis
medicine
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patients with idiopathic pulmonary fibrosis/usual interstitial pneumonia show significantly lowered immunoreactivity of extracellular superoxide dismutase in fibrotic compared to non-fibrotic areas of the diseased lung
medicine
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superoxide dismutase enzyme mutations causing familial amyotrophic lateral scerosis FALS cluster in protein regions influencing architectural integrity. FALS mutants H43R and A4V show reduced stability and drastically increased aggregation propensity, promoting the formation of filamentous aggregates. Free-cysteine-independent aggregation of FALS mutant enzyme is an intregral part of pathology
medicine
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differences in oxidative stress between human arteries and veins are unlikely to be caused by superoxide dismutase activity. However enzyme plays an important role in amelioration of oxidative stress in both types of vessels
medicine
pronounced reaction of enzyme with sera from patients infected by Clonorchis sinensis and extensive cross-reactions with sera of patients infected by other trematodes or cestodes; pronounced reaction of enzyme with sera from patients infected by Clonorchis sinensis and extensive cross-reactions with sera of patients infected by other trematodes or cestodes
medicine
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recombinant protein is useful as serodiagnostic marker for identification of Aspergillus fumigatus infections, crossreactive antibodies
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medicine
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investigations with help of mutants to elucidate structure-function relation in familial amyotrophic lateral sclerosis
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synthesis
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coexpression of enzyme and variants with yeast copper chaperone yCCS in Escherichia coli, in medium supplemented with copper and zinc, with high yield and activity
synthesis
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production of extracellular superoxide dismutase in Pichia pastoris. Secretion of enzyme into the culture medium to a concentration of 440 mg/l and an antioxidative activity of 760 U/mg of enzyme. Transformed yeast cells are more resistant to heat shock and H2O2 oxidative stress
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