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Enzyme Nomenclature
Information on EC 1.15.1.1 - superoxide dismutase and Organism(s) Homo sapiens
for references in articles please use BRENDA:EC1.15.1.1
Word Map on EC 1.15.1.1
- 1.15.1.1
- catalase
- malondialdehyde
- injury
- gsh
- dysfunction
- endothelial
- inflammation
- vascular
- gsh-px
- ascorbate
- wistar
- diabetes
-
thiobarbituric
- artery
-
anti-oxidant
- ischemia
-
amyotrophic
- myocardial
-
tbars
-
reperfusion
- cardiac
- lactate
- renal
- sclerosis
- glutathione-s-transferase
- creatinine
-
chemiluminescence
- xanthine
-
sacrificed
- coronary
- myeloperoxidase
-
neuroprotective
- caspase-3
- infarct
- neutrophil
-
mime
-
sham
-
albino
- cerebral
-
sprague-dawley
-
hydroperoxide
- cholesterol
-
ischemia-reperfusion
- peroxynitrite
- drug development
- diagnostics
- biotechnology
- medicine
-
cardioprotective
-
hepatotoxicity
-
hepatoprotective
- agriculture
- analysis
-
endothelium-dependent
- synthesis
- environmental protection
- ceruloplasmin
- alpha-tocopherol
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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The taxonomic range for the selected organisms is: Homo sapiens
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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
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
electrostatic guidance of anionic substrate to the active site, detailed overview. Generation of a model for electrostatic-mediated diffusion, and efficient binding of superoxide for catalysis
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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
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
-
superoxide dismutase (SOD) is a prime antioxidant enzymethat destroys the effects of superoxide, thus limiting the dele-terious effects of reactive oxygen and nitrogen species. SOD is considered an important regulator of oxida-tive/nitrosative stress
additional information
malfunction
-
MnSOD ala16val polymorphism is associated with various diseases including breast cancer
malfunction
-
Role of nitric oxide (NO) modified erythrocytes superoxide dismutase (eSOD) in alopecia areata, a non-scarring hair loss disorder. dysfunctioning of SODis reported in patients with alopecia areata. Protein-A purified IgG of alopecia areata patients (AA-IgG) show strong binding to NO-eSOD in comparison with IgG from controls. In addition, AA-IgG from patients with alopecia universalis recognize NO-eSOD in a greater extentas compared to AA-IgG from patients with patchy persistent alopecia areata. Alopecia universalis patients' sera contain higher levels of NO or carbonyl contents and lower levels of SOD activity compared with patchy persistent alopecia areata patient or control sera
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
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NO-induced damage in eSOD causes alteration in hydrophobic or aromatic amino acids and protein carbonyl contents
additional information
-
the putative binding position of superoxide is determined from the crystal structure of the enzyme in complex with azide, providing a model for binding to the active site. Facilitation of the anionic ligand to the active site pit via a valley of positively-charged surface patches. Surrounding ridges of negative charge help guide the superoxide anion. Within the active site pit, Arg173 and Glu162 further guide and align superoxide for efficient catalysis. Superoxide coordination at the sixth position causes the electrostatic surface of the active site pit to become nearly neutral. Generation of a model for electrostatic-mediated diffusion, and efficient binding of superoxide for catalysis. The active site manganese ion is coordinated by His26, His74, Asp159, His163, and a single oxygen, typically thought to be a water or hydroxide ion. These ligands are referred to as the inner-sphere residues. Outer-sphereresidues surround the inner-sphere and include His30, Tyr34, Phe77, Trp78, Trp123, Gln143, Trp161 and, from across the dimer interface, Glu162. Distorted five-coordinate trigonal bipyramidal active site geometry of native human MnSOD, overview
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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
2 O2.- + 2 H+
O2 + H2O2
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enzyme activity determination by xanthine-xanthine oxidase-nitro blue tetrazolium assay
-
-
ir
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2.- + H+
O2 + H2O2
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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
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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
-
-
?
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
?
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enzyme activity detection by water-soluble tetrazolium (WST-1) assay. This assay is based on the detection of a water-soluble formazan dye that is formed upon reduction of water-soluble tetrazolium salt, WST-1, by the superoxide anion
-
-
-
additional information
?
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the enzyme activity is detected by its ability to inhibit the autoxidation of epinephrine at pH 10.2
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-
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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
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
-
-
?
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
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
copper
Cu2+
Mn2+
Zinc
Zn2+
additional information
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
Cu2+
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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
Zinc
-
wild-type, 1.08 atoms per subunit, mutant H43R, 1.11, mutant A4V, 1.43 atoms per subunit
Zn2+
-
a Cu,ZnSOD with 1.18 Zn2+ per enzyme subunit, binding structure, overview
additional information
added Zn2+ and Cu2+ do not affect the enzyme activity or structure
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-(((2,4-dichlorobenzyl)(propyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 630 nM
5-(((3,5-dichlorobenzyl)(ethyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 420 nM
5-(((3,5-dichlorobenzyl)(isopropyl)amino)methyl)-1H-pyrazol-3(2H)-one
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EC50 value is 0.00108 mM
5-(((3,5-dichlorobenzyl)(methyl)amino)methyl)-1H-pyrazol-3(2H)-one
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EC50 value is 480 nM
5-(((3,5-dichlorobenzyl)(propyl)amino)methyl)-1H-pyrazol-3(2H)-one
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EC50 value is 470 nM
5-(((3,5-dichlorophenethyl)(methyl)amino)methyl)-1H-pyrazol-3(2H)-one
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EC50 value is 0.00164 mM
5-(((3-(3,5-dichlorophenyl)propyl)(methyl)amino)methyl)-1H-pyrazol-3(2H)-one
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EC50 value is 0.00332 mM
5-((benzyl(3,5-dichlorobenzyl)amino)methyl)-1H-pyrazol-3(2H)-one
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EC50 value is 0.00245 mM
5-((cyclopropyl(3,5-dichlorobenzyl)amino)methyl)-1H-pyrazol-3(2H)-one
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EC50 value is 0.00134 mM
5-[(3,5-dichlorophenoxy)methyl]-1,2-dihydro-3H-pyrazol-3-one
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EC50 value is 400 nM
5-[[(3,5-dichlorophenyl)(methyl)amino]methyl]-1,2-dihydro-3H-pyrazol-3-one
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EC50 value is 570 nM
azide
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the azide ion acts as a strong competitive inhibitor for SOD by binding directly to the active site metal. Azide is bound end-on at the sixth coordinate position of the manganese ion. Tetrameric electrostatic surfaces are calculated incorporating accurate partial charges for the active site in three states, including a state with superoxide coordinated to the metal using the position of azide as a model
di-N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium sulfate
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EC50 value is 480 nM
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Mn(Me-Phimp)2(ClO4)
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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)
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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
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i.e. Mn(2-((2-phenyl-2-(pyridin-2-yl)hydazono)methyl)phenol), active as cofactor in superoxide dismutation reaction
Mn(Phimp)2(ClO4)
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i.e. Mn(2-((2-phenyl-2-(pyridin-2-yl)hydazono)methyl)phenol)chlorate, active as cofactor in superoxide dismutation reaction
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium chloride
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EC50 value is 510 nM
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N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium citrate
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EC50 value is 480 nM
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N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium dibasic phosphate
-
EC50 value is 480 nM
-
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium L-tartrate
-
EC50 value is 480 nM
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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
diethyldithiocarbamate
-
inhibits recombinant Cu,Zn-SOD, at 0.05-0.1 mM inactivation occurs gradually within 1 h
additional information
-
the conserved, active-site residue Tyr34 mediates product inhibition
-
additional information
-
ligand complex synthesis, electrochemical properties, and structure determination, overview
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additional information
-
NO-induced damage in eSOD causes alteration in hydrophobic or aromatic amino acids and protein carbonyl contents
-
additional information
-
pyrazolone derivatives are inhibitors of Cu/Zn superoxide dismutase 1 (SOD1)-dependent protein aggregation and are useful as drugs in treatment of amyotrophic lateral sclerosis (ALS). Design and synthesis of a series of tertiary amine-containing pyrazolones and their structure-activity relationships, conjugate salts greatly improved their solubility, overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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additional information
additional information
-
kinetics of recombinant wild-type and mutant enzymes
-
additional information
additional information
-
steady-state kinetics with artificial substrates, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
additional information
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
MnSOD is translated in the cytoplasm and then imported into the mitochondria via a mitochondrial targeting signal
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Homo sapiens;
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22000
88000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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
additional information
?
-
x * 15764-15809, Cu,Zn-SOD wild-type and mutant D90A, electrospray mass spectroscopy
additional information
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isoform SOD1 stabilizes and activates calcineurin in rat brain cytosol by 47%
additional information
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asymmetric structure of the zinc-deficient enzyme, overview
additional information
hEC-SOD is present both as a monomer (33 kDa) and a dimer (66 kDa), enzyme secondary structure determination by circular dichroism, recombinant hEC-SOD purified from Sf9 insect cells is mainly composed of beta-sheet structures
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
recombinant hEC-SOD expressed in Sf9 insect cells is glycosylated at Asn107. The glycosylated form of hEC-SOD is soluble, whereas the unglycosylated form is not, but it can be solubilized by increasing the pH and ionic strength of the solution
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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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
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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
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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
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purified enzyme MnSOD in complex with azide, hanging-drop vapor diffusion, mixing of 0.001 ml of 21 mg/ml protein solution with 0.001 ml of reservoir solution 1.8 M potassium phosphate, pH 7.8, at room temperature for1 day, to obtain the azide complex, 0.002 ml of reservoir containing 200 mM sodium azide are added to drops of 6 day crystals, X-ray diffraction structure determination and analysis at 1.77-1.82 A resolution
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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
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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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
Mn-SOD and Fe-SOD: not stable to organic solvents, Cu,Zn-SOD: stable to organic solvents
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
EC-SOD recombinant from Escherichia coli as His-tagged protein and partially from insect cells
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recombinant SOD1 from Leishmania tarentolae strain P10 to 90% purity by ultracentrifugation, hydrophobic interaction chromatography and dialysis
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recombinant wild-type and truncated mutant FLAG-tagged hEC-SOD enzymes from Spodoptera frugiperda Sf9 cells by affinity chromatography
soluble recombinant enzyme SOD2 from Escherichia coli cell-free extract by dialysis, anion exchange chromatography, again dialysis, and ultrafiltration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cu,Zn-SOD, overexpression of wild-type and mutants in Spodoptera frugiperda cells Sf21 via baculovirus infection
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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
-
EC-SOD, overexpression in Escherichia coli as His-tagged protein and in Tn-5B1-4 cells of Trichoplusia ni via baculovirus infection
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expression of recombinant chimera MnSOD-VHb in Escherichia coli strain BL21(DE3)
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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, cloning of EC-SOD and recombinant expression of wild-type and truncated mutant FLAG-tagged hEC-SOD enzymes in Spodoptera frugiperda Sf9 cells using the baculovirus transfection method, both full length and truncated hEC-SOD proteins are enzymatically active
overexpression of wild-type and mutant enzymes in hind limb muscle of transgenic mice
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
docosahexaenoic acid inhibits enzyme transcription in cancer cells, involvement of hypoxia-inducible factor-2alpha signaling, but not of peroxisome proliferator-activated receptor alpha, overview. Suppression of SOD-1 expression by clofibrate also requires hypoxia-inducible factor-2alpha and the binding element in the SOD-1 promoter
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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site-directed mutagenesis, the mutant has 0.93 copper and 0.03 zinc per subunit
D83S
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site-directed mutagenesis, the mutant has 0.93 copper and 0.08 zinc per subunit
D83S/C111S
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site-directed mutagenesis, the mutant has 0.93 copper and 0.08 zinc per subunit
D90A
E100G
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an amyotrophic lateral sclerosis-associated naturally occuring SOD mutant, misfolding/aggregation mechanism with folding and unfolding kinetics, overview
E93A
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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
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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
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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
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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
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an amyotrophic lateral sclerosis-associated naturally occuring SOD mutant, misfolding/aggregation mechanism with folding and unfolding kinetics, overview
H43R
H46R
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an amyotrophic lateral sclerosis-associated naturally occuring SOD mutant, misfolding/aggregation mechanism with folding and unfolding kinetics, overview
H63C
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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
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site-directed mutagenesis, the mutant has 0.93 copper and 0.08 zinc per subunit
H80S/D83S/C6A/C111S
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site-directed mutagenesis, the mutant has 1.07 copper and 1.18 zinc per subunit
N73S
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ratio kcat/Km about twofold smaller than in wild-type, product inhibition similar to wild-type
N73S/C140S/Q143A
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catalytic efficiency much smaller than wild-type, no appreciable product inhibition
N73S/Q143A
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catalytic efficiency much smaller than wild-type, no appreciable product inhibition
Q143A
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dramatically reduced product inhibition, reduced catalytic activity and efficiency
additional information
D90A
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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
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mutant related to amyothrophic lateral sclerosis, improvement of expression by coexpression with yeast copper chaperone
G85R
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Cu,Zn-SOD, site-directed mutagenesis, analogous to mutant found in familial amyotrophic lateral sclerosis, 99% activity compared to the wild-type
G85R
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an amyotrophic lateral sclerosis-associated naturally occuring SOD mutant, misfolding/aggregation mechanism with folding and unfolding kinetics, overview
G93A
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mutant related to amyothrophic lateral sclerosis, improvement of expression by coexpression with yeast copper chaperone
G93A
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an amyotrophic lateral sclerosis-associated naturally occuring SOD mutant, misfolding/aggregation mechanism with folding and unfolding kinetics, overview
H43R
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Cu,Zn-SOD, site-directed mutagenesis, analogous to mutant found in familial amyotrophic lateral sclerosis, 66% activity compared to the wild-type
H43R
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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
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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
generation of a catalytically active truncated (residues 19-240) mutant form of human EC-SOD (hEC-SOD)
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
apoprotein expressed in insect cells can be restored by addition of Cu2+, fully active
-
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
synthesis
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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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
SOD3 has the potential as a therapeutic drug for various diseases
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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