1.15.1.1: superoxide dismutase
This is an abbreviated version!
For detailed information about superoxide dismutase, go to the full flat file.
Word Map on EC 1.15.1.1
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1.15.1.1
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catalase
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malondialdehyde
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gsh
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necrosis
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endothelial
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tnf
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wistar
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artery
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ascorbate
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gsh-px
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caspase-3
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cholesterol
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cardiac
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reperfusion
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neuroprotective
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sclerosis
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tbars
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anti-oxidant
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ischemia
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thiobarbituric
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myocardial
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triglyceride
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alt
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amyotrophic
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mime
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sacrificed
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chlorophyll
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neurotoxicity
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hippocampus
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myeloperoxidase
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infarct
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cerebral
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xanthine
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hepatotoxicity
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streptozotocin
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albino
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sham
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creatinine
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ischemia-reperfusion
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bcl-2
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s-transferase
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glutathione-s-transferase
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hepatoprotective
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diagnostics
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chemiluminescence
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synthesis
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gavage
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cardioprotective
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ceruloplasmin
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drug development
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oxygenase-1
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endothelium-dependent
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peroxynitrite
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environmental protection
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analysis
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biotechnology
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medicine
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agriculture
- 1.15.1.1
- catalase
- malondialdehyde
- gsh
- necrosis
- endothelial
- tnf
- wistar
- artery
- ascorbate
- gsh-px
- caspase-3
- cholesterol
- cardiac
-
reperfusion
-
neuroprotective
- sclerosis
-
tbars
-
anti-oxidant
- ischemia
-
thiobarbituric
- myocardial
- triglyceride
-
alt
-
amyotrophic
-
mime
-
sacrificed
- chlorophyll
-
neurotoxicity
- hippocampus
- myeloperoxidase
- infarct
- cerebral
- xanthine
-
hepatotoxicity
- streptozotocin
-
albino
-
sham
- creatinine
-
ischemia-reperfusion
- bcl-2
- s-transferase
- glutathione-s-transferase
-
hepatoprotective
- diagnostics
-
chemiluminescence
- synthesis
-
gavage
-
cardioprotective
- ceruloplasmin
- drug development
- oxygenase-1
-
endothelium-dependent
- peroxynitrite
- environmental protection
- analysis
- biotechnology
- medicine
- agriculture
Reaction
2 superoxide
+
2 H+
=
Synonyms
AhSOD, alr2938, AmSOD, APE0743, ApMn-SOD1, ApMn-SOD2, ASAC_0498, Ca-Cu,Zn SOD, cambialistic superoxide dismutase, Cg-EcSOD, chloroplastic Fe-SOD, Cj-Cu, Zn SOD, cMn-SOD, cMnSOD, cold-active superoxide dismutase, copper, zinc superoxide dismutase, copper-zinc superoxide dismutase, copper/zinc superoxide dismutase, copper/zinc-superoxide dismutase, CpSOD, CSD1, CSD2, CtSOD, Cu, Zn SOD, Cu, Zn superoxide dismutase, Cu, Zn-superoxide dismutase, Cu, ZnSOD, Cu,Zn superoxide dismutase, Cu,Zn-SOD, Cu,Zn-superoxide dismutase, Cu,ZnSOD, Cu-Zn SOD, Cu-Zn superoxide dismutase, Cu-Zn-SOD, Cu/Zn SOD, Cu/Zn superoxide dismutase, Cu/Zn superoxide dismutase 1, Cu/Zn-SOD, Cu/Zn-SODI, Cu/Zn-SODII, Cu/Zn-superoxide dismutase, Cu/ZnSOD, cuprein, CuZn superoxide dismutase, CuZn superoxide dismutase 1, CuZn-SOD, CuZn-superoxide dismutase, CuZnSOD, cytMnSOD, cytocuprein, cytoplasmic manganese SOD, cytosolic Cu/Zn superoxide dismutase, cytosolic Cu/Zn-SOD, cytosolic manganese superoxide dismutase, DaSOD, dhsod-1, dismutase, superoxide, EC-SOD, ecCuZnSOD, ECSOD, ElFe-SOD, ElSOD, erythrocuprein, erythrocyte superoxide dismutase, eSOD, extracellular copper-zinc superoxide dismutase, extracellular CuZnSOD, extracellular SOD, extracellular superoxide dismutase, Fe-SOD, Fe-SODe, Fe-SOD_ASAC, Fe-superoxide dismutase, Fe-type SOD, Fe/Mn-SOD, Fe/Mn-type SOD, Fe/MnSOD, ferrisuperoxide dismutase, FeSOD, GTNG_2884, hEC-SOD, hemocuprein, hepatocuprein, high isoelectric point superoxide dismutase, intracellular Cu-Zn superoxide dismutase, iron SOD, iron SOD type, iron superoxide dismutase, iron-containing superoxide dismutase, iron-dependent superoxide dismutase, iron-superoxide dismutase, KmSod1p, LSOD, manganese superoxide dismutase, manganese-containing SOD, manganese-containing superoxide dismutase, MgMnSOD1, MgMnSOD2, mitMn-SOD, mitochondrial manganese superoxide dismutase, mMnSOD, Mn-containing superoxide dismutase, Mn-SOD, Mn-type SOD, Mn/Fe superoxide dismutase, MnSOD, MnSOD-2, MnSOD-3, MnSOD1, MnSOD47, More, mtMnSOD, mtSOD, nectarin I, neelaredoxin, Nlr, Of-cCu/ZnSOD, PASOD, perMn-SOD, pfSOD, PschSOD, PsSOD, PthipI-SODC, PthipI-SODC1, PthipI-SODC2, RmFeSOD, RsrSOD, SaCSD1, SaFe-SOD, sdB, SOD, SOD 1, SOD I, SOD-1, SOD-2, SOD-3, SOD-4, SOD1, SOD2, SOD3, SODA, SodB, SODB1, SODB2, SodC, SODF, SODI, SODII, SODIII, SODIV, SODS, SSO0316, superoxide dismutase, superoxide dismutase 1, superoxide dismutase I, superoxide dismutase II, superoxide dismutase [Cu-Zn]
ECTree
1.15.1.1 superoxide dismutaseAdvanced search results
results (
results (Temperature Stability
Temperature Stability on EC 1.15.1.1 - superoxide dismutase
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TEMPERATURE STABILITY 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
10 - 50
purified recombinant enzyme, 10 min, 83% activity within this range remaining
100
105
110
121
20 - 40
recombinant enzyme, 1 h, about 90% activity remaining, completely stable for 45 min
20 - 90
secondary structure of SOD_ASAC is stable within this temperature range
25 - 75
purified recombinant His-tagged enzyme, no significant change in enzyme activity at 25-45°C for up to 1 h, at 75°C, 60% of enzyme activity is retained after 1 h of treatment, suggesting that the SaCSD1 is relatively thermostable
25 - 90
-
the recombinant enzyme retains more than 80% activity between 10°C and 60°C, but loses activity rapidly, which is reduced to 54% and 40% at 70°C and 80°C, respectively, and it is almost inactive at 90°C
37
4 - 70
the recombinant purified enzyme is fairly stable at 4°C and 37°C, but is rapidly inactivated at 50°C and 70°C
40
40 - 90
over 50% activity within this range, most stable at 70°C, profile overview
44.5
purified recombinant His-tagged enzyme, 60 min, loss of 50% activity
45
50
50 - 60
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 - 70
65
70
70 - 110
-
recombinant N-terminal domain of the enzyme SOD obtained by in vitro reconstitution (Mn-rec ntdSODAp) exhibits improved optimum temperature at 70°C and dramatically enhanced thermostability especially at 110°C with enhanced pH stability from pH 4 to pH 10
70 - 80
71 - 73
-
half-inactivation occurring after 10 min exposure at 71-73°C, depending on the bound metal
75
80
85
90
95
additional information
100
-
recombinant wild-type enzyme SODAp retains 44&% of maximal activity, while recombinant Mn-rec ntdSODAp N-termina domain retains 58% activity
100
purified recombinant His-tagged enzyme, 5% activity remaining after 1 h, inactivation after 2 h
100
-
purified enzyme, loss of 5% activity after 10 min boiling for the chloroplast enzyme and 35% for the cytosolic enzyme, after 1 h, 70% remaining activity, of the leaf enzyme, 20% of the rhizome enzyme
100
-
purified enzyme, strong stability at pH 6.0-7.0, the enzyme survives boiling for 10 min without losing more than 60% of activity
100
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, loss of 80% activity after 10 min, and inactivation after 20 min
110
-
purified recombinant enzyme, 20% activity remaining activity after 30 min
121
Cj-Cu,Zn SOD retains 50% of the maximum activity after autoclaving, autoclaved Ca-Cu,Zn SOD exhibits 40% of maximum activity of unautoclaved enzyme at 20°C and 30°C. Thermal inactivation kinetics of Ca-Cu,Zn SOD, overview
121
Ca-Cu Z- SOD retains 50% of the maximum activity after autoclaving, autoclaved Ca-Cu,Zn SOD exhibits 40% of maximum activity of unautoclaved enzyme at 20°C and 30°C. Thermal inactivation kinetics of Ca-Cu,Zn SOD, overview
37
purified recombinant His-tagged enzyme, 48 h, over 80% activity remaining
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 recombinant His-tagged enzyme, 40 min, 82.2% activity remains
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
50
purified recombinant His-tagged enzyme, 40 min, 59.4% activity remains
50
-
purified native enzyme, more than 85% of its initial activity is retained after 1 h of incubation. The enzyme is highly stable at temperatures below 50°C
50 - 60
purified recombinant His-tagged enzyme, 60 min, over 80% activity remaining
60
-
5 min, complete inactivation of isoenzyme B, 50% loss of isoenzyme A activity
60
-
purified enzyme, completely stable after 20 min, after 1 h, 90% remaining activity of the leaf enzyme, 70% of the rhizome enzyme
60
purified recombinant enzyme, loss of 50% activity after 20 min, of about 85% activity after 100 min, and inactivation after 120 min
60
-
purified native enzyme, 45% of its initial activity is retained after 1 h of incubation
60
purified native enzyme, 95% remaining activity after 60 min
60
Thermochaetoides thermophila
the puurified recombinant enzyme retains 93% of maximal activity after 60 min
60 - 70
purified recombinant His-tagged enzyme, more than 73% activity remains after 30 min. The residual activity declines sharply from 73.07% to 28.75% between 60°C and 70°C, T1/2 is 63°C
65
half-life of 14.7 min, thermal inactivation rate constant Kd of 0.0321 per 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 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 recombinant His-tagged enzyme, 20 min, almost no activity remains
70
-
purified native enzyme, 37% of its initial activity is retained after 1 h of incubation
70
purified native enzyme, 55% remaining activity after 60 min
70
purified recombinant enzyme, 65% remaining activity after 60 min
70
Thermochaetoides thermophila
purified recombinant enzyme, retains 65% of the maximum activity at 70°C for 60 min
70
Thermochaetoides thermophila
purified recombinant enzyme, 60 min, 75% activity remaining
70
purified enzyme mutants H29A and H171A, 30 min, retain 51% and 36.7% activity, respectively, mutant H29A retains 20% activity after 1 h, half-lives of SOD activity for His171Ala and His29Ala mutants are 33 and 15 min
70 - 80
-
the initial activities of the polysialyated enzyme show 35-55% higher than those of the native enzyme after incubation at 70°C, and 31-45% at 80°C, the native enzyme is almost inactivated after incubation for 3 h, while the polysialylated SOD still has 49-61% residual activities
75
-
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
recombinant enzyme SOD Cj-Cu,Zn SOD shows a residual SOD activity of 26.07% after being heated for 160 min
80
-
purified enzyme, completely stable after 20 min, after 1 h, 80% remaining activity of the leaf enzyme, 52% of the rhizome enzyme
80
-
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
-
purified recombinant enzyme, 40% remaining activity after 30 min, complete inactivation after 4 h
80
Thermochaetoides thermophila
purified recombinant enzyme, 25 min, 50% activity remaining
85
the enzyme is stable in aqueous solution at temperatures up to 85°C
90
dimer: half-life 99 min, dimeric form is more stable than monomeric form
90
purified recombinant enzyme, 57% activity remaining after incubation for 1 h
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
90
Thermochaetoides thermophila
purified recombinant enzyme, 30 min, 20% activity remaining
95
2 h, purified recombinant enzyme, 96% remaining activity, half-life is 33 h, inactivation according to first order kinetics
additional information
thermal stability and activity of the enzyme directly depends on the nature of the reconstituted metal and the degree of saturation of binding sites
additional information
-
thermal stability and activity of the enzyme directly depends on the nature of the reconstituted metal and the degree of saturation of binding sites
additional information
an increased net negative charge on the surface of asFeSOD may explain its lower thermostability compared to the enzyme from Escherichia coli, structure-thermostability relationship, overview
additional information
-
an increased net negative charge on the surface of asFeSOD may explain its lower thermostability compared to the enzyme from Escherichia coli, structure-thermostability relationship, overview
additional information
-
a highly thermostable enzyme, occurrence of an additional sulfur-containing hydrogen bond involving the M110 residue and the effect of the A138 residue on the backbone entropy
additional information
-
SODI displays a Tm value of 54°C and therefore its structure is rather labile to temperature
additional information
SODI displays a Tm value of 54°C and therefore its structure is rather labile to temperature
additional information
-
SODII displays a Tm value of 80°C and therefore its structure is rather stable to temperature
additional information
SODII displays a Tm value of 80°C and therefore its structure is rather stable to temperature
additional information
circular dichroic spectroscopy analysis confirms the thermostable nature of Cj-Cu,Zn SOD. Thermal inactivation first-order kinetics
additional information
thermal inactivation kinetics fit the first-order inactivation rate equation, recombinant enzyme
additional information
-
thermal inactivation kinetics fit the first-order inactivation rate equation, recombinant enzyme
additional information
-
two protein denaturation peaks at 65°C and 84°C by differential scanning calorimetry
additional information
-
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
phenylmethanesulfonyl fluoride attachment to the active site Tyr41 increases the heat stability of the enzyme, overview
additional information
-
phenylmethanesulfonyl fluoride attachment to the active site Tyr41 increases the heat stability of the enzyme, overview
additional information
-
due to its extraordinary heat stability, unfolding dynamics of this protein cannot be investigated by conventional physical methods below 100°C
additional information
due to its extraordinary heat stability, unfolding dynamics of this protein cannot be investigated by conventional physical methods below 100°C
