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
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results (Inhibitors
Inhibitors on EC 1.15.1.1 - superoxide dismutase
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INHIBITOR 
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
chloroform:ethanol solution
the Mn- and Fe-SODs of Yérsinia enterocolitica are inhibited by chloroform:ethanol solution; the Mn- and Fe-SODs of Yérsinia enterocolitica are inhibited by chloroform:ethanol solution; the Mn- and Fe-SODs of Yérsinia enterocolitica are inhibited by chloroform:ethanol solution
concanavalin A
-
inhibition in vivo and in vitro, essentially dependent on calcium chloride
-
di-N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium sulfate
Dithiocarbamate
strongly inhibits the activity of the rOf-cCu/ZnSOD
DTPA
-
i.e. diethylenetriamine-N,N,N,N,N-pentaacetic acid, inhibits the reductive decomposition of S-nitroso-L-glutathione catalyzed by superoxide dismutase by binding to the solvent-exposed active-site copper of one subunit without removing it. The resulting conformational change at the second active site inhibits the S-nitroso-L-glutathione reductase but not superoxide dismutase activity
Mn(Me-Phimp)2(ClO4)
-
i.e. Mn(2-(1-(2-phenyl-2-(pyridine-2-yl)hydrazono)ethyl)phenol)chlorate, active as cofactor in superoxide dismutation reaction
Mn(N-Phimp)2
-
i.e. Mn-(2-((2-phenyl-2-(pyridin-2-yl)hydrazono)methyl)naphthalen-1-ol), active as cofactor in superoxide dismutation reaction
Mn(N-Phimp)2(ClO4)
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i.e. Mn(2-((2-phenyl-2-(pyridin-2-yl)hydrazono)methyl)naphthalen-1-ol)chlorate, active as cofactor in superoxide dismutation reaction
Mn(Phimp)2
-
i.e. Mn(2-((2-phenyl-2-(pyridin-2-yl)hydazono)methyl)phenol), active as cofactor in superoxide dismutation reaction
Mn(Phimp)2(ClO4)
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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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N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium citrate
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium dibasic phosphate
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium L-tartrate
N-ethyl-5-phenylisoxazolium 3'-sulfonate
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i.e. Woodwards reagent, Kat 50 mM
Phenylglyoxal
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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
-
25% inhibition of Mn-reconstituted wild-type enzyme at 10 mM, no inhibition at 1 mM
2-mercaptoethanol
gradual inhibition by increasing concentration of 2-mercaptoethanol, 20% inhibition at 2 mM, 36% at 16 mM
5-(((2,4-dichlorobenzyl)(propyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 630 nM
5-(((2,4-dichlorobenzyl)(propyl)amino)methyl)-1H-pyrazol-3(2H)-one
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EC50 value is 630 nM
5-(((3,5-dichlorobenzyl)(ethyl)amino)methyl)-1H-pyrazol-3(2H)-one
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EC50 value is 420 nM
5-(((3,5-dichlorobenzyl)(ethyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 420 nM
5-(((3,5-dichlorobenzyl)(isopropyl)amino)methyl)-1H-pyrazol-3(2H)-one
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EC50 value is 0.00108 mM
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
-
EC50 value is 480 nM
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-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-(((3,5-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-(((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-((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-((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-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
5-[[(3,5-dichlorophenyl)(methyl)amino]methyl]-1,2-dihydro-3H-pyrazol-3-one
-
EC50 value is 570 nM
azide
the azide ion acts as a strong competitive inhibitor for SOD by binding directly to the active site metal. Azide is bound end-on at the sixth coordinate position of the manganese ion. Tetrameric electrostatic surfaces are calculated incorporating accurate partial charges for the active site in three states, including a state with superoxide coordinated to the metal using the position of azide as a model
azide
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
recombinant PsSOD is sensitive to a mixture of chloroform and ethanol in the ratio 3:5. Mixing the recombinant PsSOD enzyme and the solvent mixture by 2:1 and 1:1, the relative activity is 36.4 and 13.6%, respectively. In addition, no enzymatic activity remains after incubation at 1:2 mixture
CN-
-
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
di-N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium sulfate
-
EC50 value is 480 nM
di-N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium sulfate
-
EC50 value is 480 nM
diethyldithiocarbamate
-
inhibits recombinant Cu,Zn-SOD, at 0.05-0.1 mM inactivation occurs gradually within 1 h
diethyldithiocarbamate
complete inhibition at 1.4 mM, a specific inhibitor for CuZn-SODs
diethyldithiocarbamate
-
causes decline of the enzyme in various tissues after intraperitoneal injection, alpha-tocopherol feeding prior to application of diethyldithiocarbamate leads to reduced inhibition of the enzyme
diethyldithiocarbamate
inhibits SodC specifically
EDTA
-
60% inhibition of Mn-reconstituted wild-type enzyme at 10 mM, 20% at 1 mM
EDTA
-
i.e. diethylenediamine-N,N,N,N-tetraacetic acid, inhibits the reductive decomposition of S-nitroso-L-glutathione catalyzed by superoxide dismutase by binding to the solvent-exposed active-site copper of one subunit without removing it. The resulting conformational change at the second active site inhibits the S-nitroso-L-glutathione reductase but not superoxide dismutase activity
ethanol
recombinant PsSOD is sensitive to a mixture of chloroform and ethanol in the ratio 3:5. Mixing the recombinant PsSOD enzyme and the solvent mixture by 2:1 and 1:1, the relative activity is 36.4 and 13.6%, respectively. In addition, no enzymatic activity remains after incubation at 1:2 mixture
guanidinium hydrochloride
-
25% inhibition of Mn-reconstituted wild-type enzyme at 10 mM
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
addition of 5 mM of hydrogen peroxide (H2O2) completely inhibits of the enzyme
H2O2
half-life of 22 min both in absence or presence of 2-mercaptoethanol
H2O2
preincubation in 5 mM H2O2 for 30 min results in a loss of 91% activity
H2O2
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
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium chloride
-
EC50 value is 510 nM
-
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium chloride
-
EC50 value is 510 nM
-
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium citrate
-
EC50 value is 480 nM
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium citrate
-
EC50 value is 480 nM
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium dibasic phosphate
-
EC50 value is 480 nM
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium dibasic phosphate
-
EC50 value is 480 nM
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium L-tartrate
-
EC50 value is 480 nM
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium L-tartrate
-
EC50 value is 480 nM
N3-
-
Mn-SOD is inhibited by 50%, enzyme reconstituted by Fe3+ shows increased inhibition
NaCl
activity of SaCSD1 decreases with the increase of salt concentration
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
-
60% inhibition of Mn-reconstituted wild-type enzyme at 1%, and 40% inhibition of the Mn-reconstituted N-terminal domain
SDS
-
recombinant Cp-icCuZnSOD is active and retains more than 80% activity under treatment with 1-6% SDS. It retains 70% activity after treatment with 8% SDS but activity is rapidly lowered to 52% after treatment with 10% SDS
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
the enzyme is resistant to denaturation by sodium dodecyl sulfate (SDS) and urea
-
additional information
not inhibitory: sodium dodecylsulfate
-
additional information
imidazole up to 0.8 M and sodium dodecylsulfate up to 4% are not inhibitory
-
additional information
no inhibition by CN; no inhibition by CN; no inhibition by CN
-
additional information
no inhibition by CN; no inhibition by CN; no inhibition by CN
-
additional information
no inhibition by CN; no inhibition by CN; no inhibition by CN
-
additional information
-
no inhibition by CN; no inhibition by CN; no inhibition by CN
-
additional information
-
UV-B radiation decreases the SOD activity
-
additional information
not inhibitory: sodium dodecylsulfate up to 2.5%
-
additional information
-
not inhibitory: sodium dodecylsulfate up to 2.5%
-
additional information
-
no inhibition by dithiothreitol and beta-mercaptoethanol
-
additional information
insensitivity of the recombinant enzyme to both KCN and H2O2
-
additional information
the enzyme shows good tolerance to some inhibitors, detergents, and denaturants
-
additional information
insensitivity of the recombinant enzyme to both KCN and H2O2. The enzyme shows a relatively good tolerance to some inhibitors, detergents, and denaturants, such as 2-mercaptoethanol, dithiothreitol, phenylmethylsulfonyl fluoride, Chaps, Triton X-100, urea, and guanidine hydrochloride
-
additional information
tributyltin chloride does not affect enzyme expression
-
additional information
-
tributyltin chloride does not affect enzyme expression
-
additional information
the conserved, active-site residue Tyr34 mediates product inhibition
-
additional information
-
the conserved, active-site residue Tyr34 mediates product inhibition
-
additional information
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ligand complex synthesis, electrochemical properties, and structure determination, overview
-
additional information
NO-induced damage in eSOD causes alteration in hydrophobic or aromatic amino acids and protein carbonyl contents
-
additional information
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NO-induced damage in eSOD causes alteration in hydrophobic or aromatic amino acids and protein carbonyl contents
-
additional information
-
pyrazolone derivatives are inhibitors of Cu/Zn superoxide dismutase 1 (SOD1)-dependent protein aggregation and are useful as drugs in treatment of amyotrophic lateral sclerosis (ALS). Design and synthesis of a series of tertiary amine-containing pyrazolones and their structure-activity relationships, conjugate salts greatly improved their solubility, overview
-
additional information
-
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
-
compound 2-[(3-iodophenyl)methylsulfanyl]-5-pyridin-4-yl-1,3,4-oxadiazole, a known protein kinase inhibitor, decreases enzyme mutant G93A-SOD1 expression in vitro and in the brain and spinal cord in vivo, but this compound has a biphasic dose response curve and a likely toxophore which limit its therapeutic window for chronic disease such as amyotrophic lateral sclerosis (ALS). Therefore, a focused library of analogues are tested for the ability to decrease SOD1 expression in vitro. This exercise results in the identification of a lead compound with improved drug-like characteristics and activity. Development of small molecules that reduce the expression of etiologically relevant toxic proteins, structureactivity relationships, overview. Compounds 3-[1-(3-hydroxypropyl)-1H-pyrrolo[2,3-b]pyridin-3-yl]-4-(pyrazin-2-yl)-1H-pyrrole-2,5-dione, 2-chloro-1-(4,5-dibromothiophen-2-yl)ethan-1-one, 2-bromo-1-(4-bromophenyl)ethan-1-one, 4-(5-[[(3-iodophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(3-methoxyphenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(3-fluorophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-[5-([[4-(trifluoromethyl)phenyl]methyl]sulfanyl)-1,3,4-oxadiazol-2-yl]pyridine, 4-(5-[[(3-chlorophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(3-nitrophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(3-bromophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(4-methoxyphenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(4-chlorophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(4-bromophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(4-iodophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(4-fluorophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(4-methylphenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(4-nitrophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine, 4-(5-[[(4-nitrophenyl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)pyridine suppress the enzyme expression
-
additional information
-
pyrazolone derivatives are inhibitors of Cu/Zn superoxide dismutase 1 (SOD1)-dependent protein aggregation and toxicity, and are useful as drugs in treatment of amyotrophic lateral sclerosis (ALS). Design and synthesis of a series of tertiary amine-containing pyrazolones and their structure-activity relationships, conjugate salts greatly improve their solubility, overview. Identification of several neuron-protection scaffolds based on mitigating protein aggregation and toxicity. A tertiary amine fragment is incorporated into the linker between the pyrazolone and the aryl group on the basis of principles of optimal brain exposure in CNS drug molecule design, the tertiary amine pyrazolone scaffolds exhibited superior properties for potential neuronal activity and in metabolic studies, such as microsomal stability, plasma stability, and Caco-2 permeability
-
additional information
poor inhibition by KCN, no inhibition by EDTA and cuprizone
-
additional information
-
poor inhibition by KCN, no inhibition by EDTA and cuprizone
-
additional information
no inhibition by EDTA and poor inhibition by NaN3
-
additional information
-
no inhibition by EDTA and poor inhibition by NaN3
-
additional information
-
not inhibitory: cyanide, hydrogen peroxide, ditiothreitol, sodium azide, Triton X-100, and 2-mercaptoethanol
-
additional information
-
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
-
cyanide at 5 mM and H2O2 at 3 mM have no effect on the activity of the enzyme
-
additional information
-
no effect: Cu2+, Co2+, Ca2+, sodium dodecylsulfate, 2-mercaptoethanol
-
additional information
Radix lethospermi
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not inhibitory: dithiothreitol, sodium azide, 2-mercaptoethanol
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additional information
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no effect on the enzyme by alpha-tocopherol in absence of diethyldithiocarbamate
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additional information
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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
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additional information
no inhibition by DTT. Ba2+, Ca2+, Ni2+, and Fe2+ have no obvious impact to enzyme activity at 1 mM
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additional information
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no inhibition by DTT. Ba2+, Ca2+, Ni2+, and Fe2+ have no obvious impact to enzyme activity at 1 mM
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additional information
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the enzyme is insensitive to cyanide inhibition
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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
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additional information
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recombinant Fe-reconstituted SOD is not inhibited by azide, steric hindrance in the substrate funnel of the enzyme prevents the access of N3- but allows O2- and F- access to the active site
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additional information
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no inhibition of Cu,Zn-SOD by sodium azide and O-phenanthroline
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additional information
the SaCSD1 protein is very susceptive to pepsin digestion
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additional information
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the SaCSD1 protein is very susceptive to pepsin digestion
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additional information
the enzyme is insensitive to malondialdehyde (MDA) or 4-hydroxy-2-nonenal (HNE); the enzyme is insensitive to malondialdehyde (MDA) or 4-hydroxy-2-nonenal (HNE). Enzyme Mn-SOD is insensitive to cyanide
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additional information
the enzyme is insensitive to malondialdehyde (MDA) or 4-hydroxy-2-nonenal (HNE); the enzyme is insensitive to malondialdehyde (MDA) or 4-hydroxy-2-nonenal (HNE). Enzyme Mn-SOD is insensitive to cyanide
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additional information
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no inhibition of the purified enzyme by 6 M guanidinium chloride or by proteases trypsin and Staphylococcus aureus V8 protease
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additional information
no inhibition of the purified enzyme by 6 M guanidinium chloride or by proteases trypsin and Staphylococcus aureus V8 protease
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additional information
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the native enzyme is degraded by pepsin and trypsin, while the polysialylated SOD is resistant to pepsin and trypsin
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additional information
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urea and iodoacetamide do not affect the enzymatic activity
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additional information
the purified recombinant enzyme shows a high degree of resistance to detergent, ethanol and protease digestion
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additional information
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the purified recombinant enzyme shows a high degree of resistance to detergent, ethanol and protease digestion
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additional information
no inhibition by diethyldithiocarbamate; no inhibition by diethyldithiocarbamate
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additional information
no inhibition by diethyldithiocarbamate; no inhibition by diethyldithiocarbamate
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additional information
no inhibition by diethyldithiocarbamate; no inhibition by diethyldithiocarbamate
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additional information
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no inhibition by diethyldithiocarbamate; no inhibition by diethyldithiocarbamate
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