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Information on EC 1.15.1.1 - superoxide dismutase and Organism(s) Rattus norvegicus and UniProt Accession P07632
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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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Word Map
- 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
The taxonomic range for the selected organisms is: Rattus norvegicus
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
-
-
-
-
superoxide dismutase II
-
-
-
-
copper-zinc superoxide dismutase
-
-
-
-
Cu-Zn superoxide dismutase
-
-
-
-
Mn-SOD
-
-
-
-
SOD
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 superoxide + 2 H+ = O2 + H2O2
amino acid sequence alignment and comparison
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
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
O2- + H+
O2 + H2O2
-
-
Fe-SODs are inhibited by H2O2, but Mn-SODs are not
?
O2.- + H+
O2 + H2O2
-
Cu,ZnSOD is a urinary marker of hepatic necrosis, but not hepatic fibrosis, overview
-
-
?
O2.- + H+
O2 + H2O2
-
SOD1 induces Ca2+ in the cell and inhibits ERK phosphorylation in the P-ERK1/2 pathway by muscarinic receptor M1 modulation in rat pituitary GH3 cells, the effect is enhanced by oxotremorine and partially reverted by pyrenzepine, and independent from increased intracellular calcium concentration, overview
-
-
?
O2.- + H+
O2 + H2O2
-
the enzyme is involved in hypoxic pulmonary vasoconstriction, HPV, an important physiological mechanism, which is regulated by changes in the production of and interactions among reactive oxygen species, mechanism, overview, the superoxide dismutase mimetic tempol inhibits HPV, overview
-
-
?
O2.- + H+
O2 + H2O2
-
the enzyme prevents the inhibition of human CYP3A4, UGT1A6, and P-glycoprotein with halogenated xanthene food dyes, overview
-
-
?
additional information
?
-
-
dismutation of superoxide anions is promoted by reduction of Cu2+ to Cu+
-
-
?
additional information
?
-
-
MnSOD may have a specific role in the steroidogenic function of the fasciulata/reticularis of the rat adrenal, but not on that of the glomerulosa
-
-
?
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
additional information
?
-
-
MnSOD may have a specific role in the steroidogenic function of the fasciulata/reticularis of the rat adrenal, but not on that of the glomerulosa
-
-
?
O2.- + H+
O2 + H2O2
-
Cu,ZnSOD is a urinary marker of hepatic necrosis, but not hepatic fibrosis, overview
-
-
?
O2.- + H+
O2 + H2O2
-
SOD1 induces Ca2+ in the cell and inhibits ERK phosphorylation in the P-ERK1/2 pathway by muscarinic receptor M1 modulation in rat pituitary GH3 cells, the effect is enhanced by oxotremorine and partially reverted by pyrenzepine, and independent from increased intracellular calcium concentration, overview
-
-
?
O2.- + H+
O2 + H2O2
-
the enzyme is involved in hypoxic pulmonary vasoconstriction, HPV, an important physiological mechanism, which is regulated by changes in the production of and interactions among reactive oxygen species, mechanism, overview, the superoxide dismutase mimetic tempol inhibits HPV, overview
-
-
?
O2.- + H+
O2 + H2O2
-
the enzyme prevents the inhibition of human CYP3A4, UGT1A6, and P-glycoprotein with halogenated xanthene food dyes, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu2+
Mn2+
Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
additional information
-
no effect on the enzyme by alpha-tocopherol in absence of diethyldithiocarbamate
-
additional information
-
melatonin, testosterone, dihydrotestosterone, estradiol, and vitamin D induce activation of SOD1 in mitochondria. Enzyme activation is not affected by furafylline, a selective inhibitor of the P450 1A2 isoform, but is inhibited by omeprazole and ketoconazole, and by tiron, a superoxide radical specific scavenger
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
corticotrophin
-
enzyme activity in the inner zone mitochondria of adrenal gland is enhaced by corticotrophin and by a low-sodium diet
-
malathion
-
subchronic exposure to malathion increases the enzyme activity in liver by 11%
sulfhydryl compounds
-
e.g. reduced glutathione, cysteine, 2-mercaptopropionylglycine activate
additional information
-
no effect on the enzyme by alpha-tocopherol in absence of diethyldithiocarbamate
-
additional information
-
activation of intermembrane space SOD1 upon oxidation of critical thiols. Melatonin, testosterone, dihydrotestosterone, estradiol, and vitamin D induce activation of SOD1 in mitochondria. Enzyme activation is not affected by furafylline, a selective inhibitor of the P450 1A2 isoform, but is inhibited by omeprazole and ketoconazole
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
enzyme mRNA is only found in the inner zones of adrenal cortex, not the glomerulosa. Enzyme activity in the inner zone mitochondria is enhaced by corticotrophin and by a low-sodium diet, but suppressed by betamethasone
-
peritoneal macrophages exposed to He-Ne laser radiation. Changes in the activity of superoxide dismutase as well as the formation of nitric oxide and peroxynitrite depend to a large extent on the laser radiation dose. Activation of enzyme at low radiation doses is accompanied by nitric oxide level increase without changes in peroxynitrite. Enhanced laser radiation doses inhibit the enzyme
-
in rats with hepatic necrosis after treatment with tetrachlorcarbon
additional information
additional information
-
overview: content of Cu,Zn-SOD and Mn-SOD in rat tissues
additional information
-
the enzyme is secreted by many cellular lines and it is also released trough a calcium-dependent depolarization mechanism involving SNARE protein SNAP 25
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
-
subcellular localization study of SOD1, overview
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
superoxide dismutases (SODs) are key enzymes functioning as the first line of antioxidant defense by virtue of the ability to convert highly reactive superoxide radicals to hydrogen peroxide and molecular oxygen. The expression of the SOD genes from animals is related to hormone levels and cytokines in the body. A study suggested that removal of estradiol by ovariectomy decreases the activity of Cu/Zn-SOD and Mn-SOD in the intra-abdominal tissue of female rats compared with rats treated with ovariectomy but with added estradiol. In addition, a variety of cytokines such as growthfactor, tumor necrosis factor, and interleukin regulate response to oxidative stress via regulation of SOD expression
physiological function
additional information
physiological function
-
expression and activity of the mitochondrial P450 system along with substrate availability may contribute to mitochondrial function regulation via activation of IMS SOD1. Activation of intermembrane space SOD1 after incubation of rat liver intact mitochondria with P450 substrates significantly prevents the loss of aconitase activity in the mitochondrial matrix, general mechanism for the SOD1 activation mediated by P450 enzymes, overview
physiological function
superoxide dismutases (SODs) are key enzymes functioning as the first line of antioxidant defense by virtue of the ability to convert highly reactive superoxide radicals to hydrogen peroxide and molecular oxygen. The expression of the SOD genes from animals is related to hormone levels and cytokines in the body. A study suggested that removal of estradiol by ovariectomy decreases the activity of Cu/Zn-SOD and Mn-SOD in the intra-abdominal tissue of female rats compared with rats treated with ovariectomy but with added estradiol. In addition, a variety of cytokines such as growth factor, tumor necrosis factor, and interleukin regulate response to oxidative stress via regulation of SOD expression
additional information
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SODC_RAT
154
0
15912
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
additional information
-
immunoblot analysis shows isoforms of 25 and 75 kDa with increased expression of the 75 kDa isoform after treatment with corticotrophin
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
posttranscriptional regulation of SODs, overview
additional information
posttranscriptional regulation of SODs, overview
additional information
posttranscriptional regulation of SODs, overview
additional information
posttranscriptional regulation of SODs, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
3 cycles of freezing and thawing cause less than 20% loss of activity, Mn-SOD
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from mitochondrial intermembrane space of livber microsomes
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
effects of abiotic and biotic stresses on SOD expression, overview
effects of abiotic and biotic stresses on SOD expression, overview
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
-
Cu,Zn-SOD is a urinary marker of hepatic necrosis, but not hepatic fibrosis, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Beyer, W.; Imlay, J.; Fridovich, I.
SODs: varieties and distributions. X-ray crystallography of Mn-SODs and Fe-SODs
Prog. Nucleic Acid Res. Mol. Biol.
40
221-253
1991
Synechococcus elongatus PCC 7942 = FACHB-805, Geobacillus stearothermophilus, Bacteroides thetaiotaomicron, Bacteroides fragilis, Saccharomyces cerevisiae, Caulobacter vibrioides, Escherichia coli, Thermus thermophilus, Ginkgo biloba, Halobacterium salinarum, Homo sapiens, Methanobacterium bryantii, Paracoccus denitrificans, Mus musculus, Mycolicibacterium phlei, Nocardia asteroides, Photobacterium leiognathi, Leptolyngbya boryana, Propionibacterium freudenreichii subsp. shermanii, Pseudomonas putida, Rattus norvegicus, Gordonia bronchialis, Streptococcus mutans, Thermoplasma acidophilum, Zea mays, Thermus thermophilus Mn-SOD, Photobacterium leiognathi CuZn-SOD, Caulobacter vibrioides CuZn-SOD, Pseudomonas putida Fe-SOD, Escherichia coli Mn-SOD, Escherichia coli Fe-SOD, Paracoccus denitrificans CuZn-SOD, Geobacillus stearothermophilus Mn-SOD, Thermoplasma acidophilum Fe-SOD
Geller, B.L.; Winge, D.R.
Subcellular distribution of superoxide dismutases in rat liver
Methods Enzymol.
105
105-121
1984
Rattus norvegicus
Ishikawa, T.; Hunaiti, A.R.; Piechot, G.; Wolf, B.
Isolation and characterization of basic superoxide dismutase consisting of Mr-25,000 subunits in rat liver
Eur. J. Biochem.
170
317-323
1987
Rattus norvegicus, Rattus norvegicus Mn-SOD
Asayama, K.; Burr, I.M.
Rat superoxide dismutases. Purification, labeling, immunoassay, and tissue concentration
J. Biol. Chem.
260
2212-2217
1985
Rattus norvegicus, Rattus norvegicus CuZn-SOD, Rattus norvegicus Mn-SOD
Hoshino, T.; Ohta, Y.; Ishiguro, I.
The effect of sulfhydryl compounds on the catalytic activity of Cu, Zn-superoxide dismutase purified from rat liver
Experientia
41
1416-1419
1985
Rattus norvegicus, Rattus norvegicus CuZn-SOD
Salin, M.L.; Day, E.D.; Crapo, J.D.
Isolation and characterization of a manganese-containing superoxide dismutase from rat liver
Arch. Biochem. Biophys.
187
223-228
1978
Rattus norvegicus, Rattus norvegicus Mn-SOD
Klebanov, G.I.; Poltanov, E.A.; Chichuk, T.V.; Osipov, A.N.; Vladimirov, Y.A.
Changes in superoxide dismutase activity and peroxynitrite content in rat peritoneal macrophages exposed to He-Ne laser radiation
Biochemistry (Moscow)
70
1335-1340
2005
Rattus norvegicus
Raza, F.S.; Okamoto, M.; Takemori, H.; Vinson, G.P.
Manganese superoxide dismutase activity in the rat adrenal
J. Endocrinol.
184
77-84
2005
Rattus norvegicus
Secondo, A.; De Mizio, M.; Zirpoli, L.; Santillo, M.; Mondola, P.
The Cu-Zn superoxide dismutase (SOD1) inhibits ERK phosphorylation by muscarinic receptor modulation in rat pituitary GH3 cells
Biochem. Biophys. Res. Commun.
376
143-147
2008
Rattus norvegicus
Rezg, R.; Mornagui, B.; El-Fazaa, S.; Gharbi, N.
Biochemical evaluation of hepatic damage in subchronic exposure to malathion in rats: effect on superoxide dismutase and catalase activities using native PAGE
C. R. Biol.
331
655-662
2008
Rattus norvegicus
Hodyc, D.; Snorek, M.; Brtnicky, T.; Herget, J.
Superoxide dismutase mimetic tempol inhibits hypoxic pulmonary vasoconstriction in rats independently of nitric oxide production
Exp. Physiol.
92
945-951
2007
Rattus norvegicus
Prabhu, H.R.; Nandini, M.
Inhibition of selenium dependent glutathione peroxidase and superoxide dismutase in rats by diethyldithiocarbamate: effect of pre-administration of alpha-tocopherol
Indian J. Exp. Biol.
45
465-468
2007
Rattus norvegicus
Smyth, R.; Munday, M.R.; York, M.J.; Clarke, C.J.; Dare, T.; Turton, J.A.
Comprehensive characterization of serum clinical chemistry parameters and the identification of urinary superoxide dismutase in a carbon tetrachloride-induced model of hepatic fibrosis in the female Hanover Wistar rat
Int. J. Exp. Pathol.
88
361-376
2007
Rattus norvegicus
Inarrea, P.; Casanova, A.; Alava, M.A.; Iturralde, M.; Cadenas, E.
Melatonin and steroid hormones activate intermembrane Cu,Zn-superoxide dismutase by means of mitochondrial cytochrome P450
Free Radic. Biol. Med.
50
1575-1581
2011
Rattus norvegicus, Rattus norvegicus Wistar
Wang, W.; Xia, M.X.; Chen, J.; Yuan, R.; Deng, F.N.; Shen, F.F.
Gene expression characteristics and regulation mechanisms of superoxide dismutase and its physiological roles in plants under stress
Biochemistry (Moscow)
81
465-480
2016
Arabidopsis thaliana, Arabidopsis thaliana (O78310), Arabidopsis thaliana (P24704), Glycine max, Nicotiana tabacum, Pleurotus ostreatus, Populus trichocarpa, Zea mays, Nicotiana benthamiana, Raphanus sativus var. raphanistroides, Gypsophila oblanceolata, Rhodobacter capsulatus (O30970), Rattus norvegicus (P07632), Rattus norvegicus (P07895), Pseudomonas putida (P09223), Nicotiana plumbaginifolia (P11796), Nicotiana plumbaginifolia (P22302), Nicotiana plumbaginifolia (P27082), Nostoc sp. PCC 7120 = FACHB-418 (Q8YSZ1)
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