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Information on EC 1.15.1.1 - superoxide dismutase and Organism(s) Saccharolobus solfataricus and UniProt Accession P80857
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1.15.1.1 superoxide dismutaseIUBMB Comments
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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- 1.15.1.1
- catalase
- malondialdehyde
- gsh
- necrosis
- endothelial
- tnf
- wistar
- artery
- ascorbate
- gsh-px
- caspase-3
- cholesterol
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reperfusion
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neuroprotective
- sclerosis
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tbars
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anti-oxidant
- ischemia
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thiobarbituric
- myocardial
- triglyceride
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alt
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amyotrophic
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mime
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sacrificed
- chlorophyll
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neurotoxicity
- hippocampus
- myeloperoxidase
- infarct
- cerebral
- xanthine
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hepatotoxicity
- streptozotocin
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albino
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sham
- creatinine
-
ischemia-reperfusion
- bcl-2
- s-transferase
- glutathione-s-transferase
-
hepatoprotective
- diagnostics
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chemiluminescence
- synthesis
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gavage
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cardioprotective
- ceruloplasmin
- drug development
- oxygenase-1
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endothelium-dependent
- peroxynitrite
- environmental protection
- analysis
- biotechnology
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- agriculture
The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
superoxide dismutase, sod, mnsod, manganese superoxide dismutase, mn-sod, ec-sod, cuznsod, superoxide dismutase 1, cu/zn superoxide dismutase, sod-1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
copper-zinc superoxide dismutase
-
-
-
-
Cu,Zn-SOD
-
-
-
-
Cu-Zn superoxide dismutase
-
-
-
-
cuprein
-
-
-
-
cytocuprein
-
-
-
-
dismutase, superoxide
-
-
-
-
erythrocuprein
-
-
-
-
Fe-SOD
ferrisuperoxide dismutase
-
-
-
-
hemocuprein
-
-
-
-
hepatocuprein
-
-
-
-
Mn-SOD
-
-
-
-
SOD
SOD-1
-
-
-
-
SOD-2
-
-
-
-
SOD-3
-
-
-
-
SOD-4
-
-
-
-
SODF
-
-
-
-
SODS
-
-
-
-
superoxide dismutase
-
-
-
-
superoxide dismutase I
-
-
-
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superoxide dismutase II
-
-
-
-
Fe-SOD
-
-
-
-
SOD
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
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oxidation
-
-
-
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reduction
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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.
CAS REGISTRY NUMBER
COMMENTARY
9054-89-1
-
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
-
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
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dismutation of superoxide in a two-step reaction: 1. O2.- + Fe3+-SOD = O2 + Fe2+-SOD, 2. O2.- + Fe2+-SOD + 2 H+ = H2O2 + Fe3+-SOD
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-
?
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
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-
?
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
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-
?
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
?
-
-
unusual covalent modification of the conserved Tyr41 in the active site, interactions Tyr41-His155, overview
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-
?
NATURAL SUBSTRATE
NATURAL 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
-
superoxide dismutase is a key enzyme for the protection of aerobic organisms against toxic radicals produced during oxidative processes
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
additional information
Fe2+
-
Fe-type SOD, helices alpha1 and alpha2 contribute one metal ligand each, i.e. His33 and His84, binding structure, the iron is ligated by Nepsilon2 of His33, His84 and His174, by Odelta1 of Asp170, and a solvent molecule forming a distorted trigonal bipyramidal coordination sphere, overview
Fe2+
-
the homodimeric enzyme contains 0.7 atom of iron per subunit
additional information
metal content analysis of the recombinant enzyme
additional information
-
metal content analysis of the recombinant enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
H2O2
distinguishes Fe-SOD from Mn-SOD, since it inactivates only Fe-SOD
phenylmethanesulfonyl fluoride
irreversible inactivation by attachment of a molecule phenylmethanesulfonyl fluoride to the active site Tyr41 reinforcing the heat stability of the enzyme, overview
NaN3
-
inhibits the enzyme mutants Y41F and H155Q, but not the wild-type enzyme
additional information
recombinant Fe-reconstituted SOD is not inhibited by azide, steric hindrance in the substrate funnel of the enzyme prevents the access of N3- but allows O2- and F- access to the active site
-
additional information
-
recombinant Fe-reconstituted SOD is not inhibited by azide, steric hindrance in the substrate funnel of the enzyme prevents the access of N3- but allows O2- and F- access to the active site
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additional information
-
the enzyme is insensitive to cyanide inhibition
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
17.3
-
purified extracellular enzyme, pyrogallol autoxidation inhibition assay method
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
both wild-type and fusion protein with the N-terminal domain of superoxide dismutase from Geobacillus thermodenitrificans NG80-2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
fusion protein with the N-terminal domain of superoxide dismutase from Geobacillus thermodenitrificans NG80-2
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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
-
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
extracellular Fe-SOD, associated with cell-surface
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24000
63000
87900
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y88F
site-directed mutagenesis, substitution of Tyr88 to Phe does not affect the metal specificity of the enzyme
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
additional information
additional information
construction of a fusion protein with the N-terminal domain of superoxide dismutase from Geobacillus thermodenitrificans NG80-2. The recombinant protein exhibits improved thermophilicity, higher working temperature, improved thermostability, broader pH stability, and enhanced tolerance to inhibitors and organic media without any alterations in its oligomerization state
additional information
-
construction of a fusion protein with the N-terminal domain of superoxide dismutase from Geobacillus thermodenitrificans NG80-2. The recombinant protein exhibits improved thermophilicity, higher working temperature, improved thermostability, broader pH stability, and enhanced tolerance to inhibitors and organic media without any alterations in its oligomerization state
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 8
fusion protein with the N-terminal domain of superoxide dismutase from Geobacillus thermodenitrificans NG80-2, more than 90% of initial activity
737269
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
105
95
2 h, purified recombinant enzyme, 96% remaining activity, half-life is 33 h, inactivation according to first order kinetics
additional information
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
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
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
SDS decreases the stability of SOD and accelerates enzyme inactivation
-
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme, and recombinant enzyme from Escherichia coli strain JM109(DE3)
native enzyme from post-ribosomal supernatant by anion exchange, hydrophobic interaction, and hydroxyapatite chromatography, followed by gel filtration, to homogeneity
-
native extracellular enzyme to homogeneity from the culture medium by ultrafiltration, gel filtration, dialysis, and anion exchange chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and anaylsis, expression of wild-type and mutant in Escherichia coli
gene sod, cloning from genomic DNA, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain JM109(DE3)
expression of wild-type and mutant enzymes in Escherichia coli strain JM109(DE3)
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of Fe-SOD from purified recombinant apo-enzyme, apo-enzyme preparation: purified recombinant 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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cannio, R.; D'Angelo, A.; Rossi, M.; Bartolucci, S.
A superoxide dismutase from the archaeon Sulfolobus solfataricus is an extracellular enzyme and prevents the deactivation by superoxide of cell-bound proteins
Eur. J. Biochem.
267
235-243
2000
Saccharolobus solfataricus, Saccharolobus solfataricus Gtheta
Gogliettino, M.A.; Tanfani, F.; Scire, A.; Ursby, T.; Adinolfi, B.S.; Cacciamani, T.; De Vendittis, E.
The role of Tyr41 and His155 in the functional properties of superoxide dismutase from the archaeon Sulfolobus solfataricus
Biochemistry
43
2199-2208
2004
Saccharolobus solfataricus
Dello Russo, A.; Rullo, R.; Nitti, G.; Masullo, M.; Bocchini, V.
Iron superoxide dismutase from the archaeon Sulfolobus solfataricus: average hydrophobicity and amino acid weight are involved in the adaptation of proteins to extreme environments
Biochim. Biophys. Acta
1343
23-30
1997
Saccharolobus solfataricus, Saccharolobus solfataricus MT-4 / DSM 5833
De Vendittis, E.; Ursby, T.; Rullo, R.; Gogliettino, M.A.; Masullo, M.; Bocchini, V.
Phenylmethanesulfonyl fluoride inactivates an archaeal superoxide dismutase by chemical modification of a specific tyrosine residue. Cloning, sequencing and expression of the gene coding for Sulfolobus solfataricus superoxide dismutase
Eur. J. Biochem.
268
1794-1801
2001
Saccharolobus solfataricus (P80857), Saccharolobus solfataricus
Yamano, S.; Maruyama, T.
An azide-insensitive superoxide dismutase from a hyperthermophilic archaeon, Sulfolobus solfataricus
J. Biochem.
125
186-193
1999
Saccharolobus solfataricus (P80857), Saccharolobus solfataricus
Ursby, T.; Adinolfi, B.S.; Al-Karadaghi, S.; De Vendittis, E.; Bocchini, V.
Iron superoxide dismutase from the archaeon Sulfolobus solfataricus: analysis of structure and thermostability
J. Mol. Biol.
286
189-205
1999
Saccharolobus solfataricus
Maaty, W.S.; Wiedenheft, B.; Tarlykov, P.; Schaff, N.; Heinemann, J.; Robison-Cox, J.; Valenzuela, J.; Dougherty, A.; Blum, P.; Lawrence, C.M.; Douglas, T.; Young, M.J.; Bothner, B.
Something old, something new, something borrowed; how the thermoacidophilic archaeon Sulfolobus solfataricus responds to oxidative stress
PLoS One
4
e6964
2009
Saccharolobus solfataricus (P80857), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (P80857)
Li, M.; Zhu, L.; Wang, W.
Improving the thermostability and stress tolerance of an archaeon hyperthermophilic superoxide dismutase by fusion with a unique N-terminal domain
Springerplus
5
241
2016
Geobacillus thermodenitrificans (A4ISC5), Saccharolobus solfataricus (P80857), Saccharolobus solfataricus, Saccharolobus solfataricus DSM 1617 (P80857), Geobacillus thermodenitrificans NG80-2 (A4ISC5), Geobacillus thermodenitrificans NG80-2
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