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Information on EC 1.15.1.1 - superoxide dismutase and Organism(s) Bos taurus and UniProt Accession P00442
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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
- cardiac
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reperfusion
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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
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chemiluminescence
- synthesis
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gavage
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cardioprotective
- ceruloplasmin
- drug development
- oxygenase-1
-
endothelium-dependent
- peroxynitrite
- environmental protection
- analysis
- biotechnology
- medicine
- agriculture
The taxonomic range for the selected organisms is: Bos taurus
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
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-
-
-
Cu,Zn-SOD
Cu-Zn superoxide dismutase
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-
-
-
cuprein
-
-
-
-
cytocuprein
-
-
-
-
dismutase, superoxide
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-
-
-
erythrocuprein
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-
-
-
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
-
-
-
-
Cu,Zn-SOD
-
-
-
-
SOD
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 superoxide + 2 H+ = O2 + H2O2
presence of a general acid and a general base in catalysis. Catalytic model requires histidine residues, metal-bound water molecules and two hydrated metal ions to operate in concert
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
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-
-
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reduction
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-
-
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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
O2.- + H+
O2 + H2O2
-
the enzyme catalyzes the disproportionation of superoxide via its Cu ion redox cycle [Cu-(II)/Cu(I)], protecting the organism from oxidative stress, while the neighboring Zn ion plays a structural role
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-
?
additional information
?
-
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enzyme can reduce ferrocyanide to ferricyanide at pH 5.0-8.7
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-
?
additional information
?
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addition of hexacyanoferrate results in reduction of Cu(II) to Cu(I)
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-
?
additional information
?
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coupled assay method using inhibition of the autooxidation of pyrogallol
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-
?
additional information
?
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superoxide dismutase inhibits pyrogallol autoxidation in alkaline medium characterized by increases in oxygen consumption. The primary products of pyrogallol autoxidation are H2O2 by reduction of O2 and pyrogallol-orthoquinone by oxidation of pyrogallol. SOD is catalyzing a reaction that annuls the forward electron transfer step that produces superoxide and pyrogallol-semiquinone, both oxygen radicals. By dismutating these oxygen radicals, SOD can reverse autoxidation. Analysis of reaction parameters, 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
O2.- + H+
O2 + H2O2
-
the enzyme catalyzes the disproportionation of superoxide via its Cu ion redox cycle [Cu-(II)/Cu(I)], protecting the organism from oxidative stress, while the neighboring Zn ion plays a structural role
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
study on affinity for enzyme-DNA complex and binding parameters. Enzyme-DNA complex shows at least two binding sites for divalent metal ions
Cu2+
Mg2+
-
study on affinity for enzyme-DNA complex and binding parameters. Enzyme-DNA complex shows at least two binding sites for divalent metal ions
Mn2+
Zn2+
additional information
Cu2+
-
heart: 1.64 mol of Cu per mol of enzyme, erythrocyte: 1.84 mol of Cu per mol of enzyme
Cu2+
-
the concentration of enzyme bound Cu2+ is 1.63 mg/l, the enzyme catalyzes the disproportionation of superoxide via its Cu ion redox cycle [Cu-(II)/Cu(I)], replacement of natural cofactor Cu2+ by isotopically enriched 65Cu, method, overview
Mn2+
-
study on affinity for enzyme-DNA complex and binding parameters. Enzyme-DNA complex shows at least two binding sites for divalent metal ions
Zn2+
-
the concentration of enzyme bound Zn2+ is 1.68 mg/l, the Zn ion plays a structural role, replacement of natural cofactor Zn2+ by isotopically enriched 68Zn, method, overview
additional information
-
enzyme from eukaryotes contains both copper and zinc, enzymes from most prokaryotes contain manganese or iron
additional information
-
relevance of the zinc imidazolate bond to the redox properties
additional information
-
role of copper and zinc in protein conformation and activity
additional information
-
quantitative determination of an isotopically enriched metalloenzyme containing two different metal isotopes, method development, overview
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DTPA
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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
EDTA
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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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
evaluation of catalytic rate constant as a function of ionic strength and copper and zinc content. rate constant increases with ionic strength up to 1500000000 per M and s at an ionic strength of 15 mM, and decreases thereafter
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
determination of catalytic rate constant by pulse irradiation and cytochrome c assay after addition of EDTA to eliminate excess copper. kcat Value is 2820000000 per M and s at low ionic strength and 1300000000 per M and s in presence of 50 mM phosphate, pH 7.8
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
activities of the native metalloenzyme and isotopically enriched metalloenzyme containing two different metal isotopes, measurement of SOD inhibition of the autoxidation of pyrogallol, method development, overview
additional information
-
activity of native enzyme and modified, fatty acid-conjugated enzyme, overview, coupled assay method using inhibition of the autooxidation of pyrogallol
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme has a divalent-metal dependent nucleolytic activity, DNA-cleavage obeys Michaelis-Menten kinetics
Uniprot
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
quantitative determination of an isotopically enriched metalloenzyme containing two different metal isotopes, method development, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
SOD saves catechols from autoxidation and extends their bioavailability
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_BOVIN
152
0
15683
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32500
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
-
isoform SOD1 stabilizes and activates calcineurin in rat brain cytosol via a nearly 90fold decrease in the KM for p-nitrophenylphosphate. SOD1 prevents the loss of iron and Zn from the active site of calcineurin, possibly by a conformation-dependent interaction. SOD1 also activates human calcineurin by 74%
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
extracellular enzyme, tetraborate crystallization of ethanolic enzyme extract, then recrystallization from buffer than from water
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
chemical modification of the enzyme with linoleic and alpha-linolenic acids using two different methods leads to higher retained enzymatic activity compared with SOD modified by macromolecular substances. Enhanced heat stability, acid and alkali resistance, and anti-pepsin/trypsin ability of the modified SOD are observed and compared to those of the natural enzyme, the apparent oil-water partition coefficient of the modified enzyme is especially increased, overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is remarkably stable at high temperatures and even under denaturing conditions
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Keele, B.B.; McCord, J.M.; Fridovich, I.
Further characterization of bovine superoxide dismutase and its isolation from bovine heart
J. Biol. Chem.
246
2875-2880
1971
Bos taurus
Cass, A.E.G.
Superoxide dismutases
Top. Mol. Struct. Biol.
6
121-156
1985
Geobacillus stearothermophilus, Bos taurus, Saccharomyces cerevisiae, Caulobacter vibrioides, Escherichia coli, Photobacterium leiognathi, Propionibacterium freudenreichii subsp. shermanii, Bos taurus CuZn-SOD, Photobacterium leiognathi CuZn-SOD, Caulobacter vibrioides CuZn-SOD, Caulobacter vibrioides CB15, Escherichia coli Mn-SOD, Escherichia coli Fe-SOD, Saccharomyces cerevisiae CuZn-SOD, Geobacillus stearothermophilus Mn-SOD, Saccharomyces cerevisiae Mn-SOD
-
Flohe, L.; tting, F.
Superoxide dismutase assays
Methods Enzymol.
105
93-104
1984
Bos taurus, Homo sapiens, Homo sapiens CuZn-SOD
Munkres, K.D.
Purification of exocellular superoxide dismutases
Methods Enzymol.
186
249-260
1990
Bacillus subtilis, Bos taurus, Escherichia coli, Saccharomyces cerevisiae, Triticum aestivum
Rigo, A.; Viglino, P.; Rotilio, G.
Kinetic study of o2-dismutation by bovine superoxide dismutase. Evidence for saturation of the catalytic sites by O-2
Biochem. Biophys. Res. Commun.
63
1013-1018
1975
Bos taurus, Bos taurus CuZn-SOD
Rigo, A.; Terenzi, M.; Viglino, P.; Calabrese, L.; Cocco, D.; Rotilio, G.
The binding of copper ions to copper-free bovine superoxide dismutase. Properties of the protein recombined with increasing amounts of copper ions
Biochem. J.
161
31-35
1977
Bos taurus
Morpurgo, L.; Mavelli, I.; Calabrese, L.; Agro, A.F.; Rotilio, G.
A ferrocyanide charge-transfer complex of bovine superoxide dismutase. Relevance of the zinc imidazolate bond to the redox properties of the enzyme
Biochem. Biophys. Res. Commun.
70
607-614
1976
Bos taurus, Bos taurus CuZn-SOD
Fee, J.A.; DeCorleto, P.E.
Observations on the oxidation-reduction properties of bovine erythrocyte superoxide dismutase
Biochemistry
12
4893-4899
1973
Bos taurus, Bos taurus CuZn-SOD
Rotilio, G.; Calabrese, L.; Bossa, F.; Barra, D.; Agro, A.F.; Mondovi, B.
Properties of the apoprotein and role of copper and zinc in protein conformation and enzyme activity of bovine superoxide dismutase
Biochemistry
11
2182-2187
1972
Bos taurus, Bos taurus CuZn-SOD
Weser, U.; Prinz, R.; Schallies, A.; Fretzdorff, A.; Krauss, P.; Voelter, W.; Voetsch, W.
Microbial and hepatic cuprein (superoxide dismutase). Isolation and characterisation of cuprein (superoxide dismutase) from Saccharomyces cerevisiae and bovine liver
Hoppe-Seyler's Z. Physiol. Chem.
353
1821-1831
1972
Bos taurus, Saccharomyces cerevisiae, Bos taurus CuZn-SOD, Saccharomyces cerevisiae CuZn-SOD
Calabrese, L.; Rotilio, G.; Mondovi, B.
Cobalt erythrocuprein: preparation and properties
Biochim. Biophys. Acta
263
827-829
1972
Bos taurus, Bos taurus CuZn-SOD
Michel, E.; Nauser, T.; Sutter, B.; Bounds, P.L.; Koppenol, W.H.
Kinetics properties of Cu,Zn-superoxide dismutase as a function of metal content
Arch. Biochem. Biophys.
439
234-240
2005
Bos taurus
Agbas, A.; Hui, D.; Wang, X.; Tek, V.; Zaidi, A.; Michaelis, E.K.
Activation of brain calcineurin (Cn) by Cu-Zn superoxide dismutase (SOD1) depends on direct SOD1-Cn protein interactions occurring in vitro and in vivo
Biochem. J.
405
51-59
2007
Bos taurus, Homo sapiens
Ye, M.; English, A.M.
Binding of polyaminocarboxylate chelators to the active-site copper inhibits the GSNO-reductase activity but not the superoxide dismutase activity of Cu,Zn-superoxide dismutase
Biochemistry
45
12723-12732
2006
Bos taurus
Goldstein, S.; Fridovich, I.; Czapski, G.
Kinetic properties of Cu,Zn-superoxide dismutase as a function of metal content-order restored
Free Radic. Biol. Med.
41
937-941
2006
Bos taurus
Jiang, W.; Shen, T.; Han, Y.; Pan, Q.; Liu, C.
Divalent-metal-dependent nucleolytic activity of Cu, Zn superoxide dismutase
J. Biol. Inorg. Chem.
11
835-848
2006
Bos taurus (P00442), Bos taurus
Jiang, W.; Han, Y.; Pan, Q.; Shen, T.; Liu, C.
Roles of exogenous divalent metals in the nucleolytic activity of Cu,Zn superoxide dismutase
J. Inorg. Biochem.
101
667-677
2007
Bos taurus
Deitrich, C.L.; Raab, A.; Pioselli, B.; Thomas-Oates, J.E.; Feldmann, J.
Chemical preparation of an isotopically enriched superoxide dismutase and its characterization as a standard for species-specific isotope dilution analysis
Anal. Chem.
79
8381-8390
2007
Bos taurus
Zhan, Z.J.; Zhou, Z.G.; Shan, W.G.
Preparation and characterization of Cu,Zn-superoxide dismutase covalently modified by polyunsaturated fatty acids
Biochemistry (Moscow)
74
1266-1269
2009
Bos taurus
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