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EC Tree
IUBMB 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.
The taxonomic range for the selected organisms is: Sulfolobus acidocaldarius 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,
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Fe-superoxide dismutase
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copper-zinc superoxide dismutase
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Cu-Zn superoxide dismutase
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dismutase, superoxide
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ferrisuperoxide dismutase
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superoxide dismutase
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superoxide dismutase I
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superoxide dismutase II
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SOD
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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.
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2 O2.- + 2 H+
O2 + H2O2
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additional information
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Fe2+-containing active site structure, overview
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Fe2+
Fe/Mn-type SOD, the Fe-type enzyme contains Gln85
Iron
contains one iron atom per dimer, the protein contains a mononuclear iron center
Mn2+
Fe/Mn-type SOD, the Mn-type enzyme contains Gly85
Fe2+
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bound by His33, His84, His174, and Asp170, coordination in the active site, overview
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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 inaccessibility of a direct activity assay also excludes determination of a pH- or temperature-optimum
additional information
the inaccessibility of a direct activity assay also excludes determination of a pH- or temperature-optimum
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95
stable, the inaccessibility of a direct activity assay also excludes determination of a pH- or temperature-optimum
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SwissProt
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gene sod
SwissProt
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the organism has a very high enzyme content
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it comprises at least 11% of the cytosolic protein
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24270
2 * 24270, calculated from sequence
45000
dimeric form, gel filtration
87000
tetrameric form, gel filtration
24270
2 * 24270, sequence calculation
22400
2 * 22400, calculated from sequence
22400
2 * 22400, simultaneous treatment with low SDS concentrations and heat results in an almost quantitative conversion into a tetrameric form of the enzyme with a specific activity of about 2.5 times higher than the activity of the dimer, suggesting that even though the protein is stable and active in a dimeric state, its physiological form may be tetrameric
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tetramer
2 * 22400, simultaneous treatment with low SDS concentrations and heat results in an almost quantitative conversion into a tetrameric form of the enzyme with a specific activity of about 2.5 times higher than the activity of the dimer, suggesting that even though the protein is stable and active in a dimeric state, its physiological form may be tetrameric
dimer
2 * 24270, sequence calculation
additional information
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secondary, quarternary and three-dimensional structure
dimer
2 * 22400, calculated from sequence
dimer
2 * 24270, calculated from sequence
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purified enzyme, hanging drop vapor diffusion method, 20°C, mixing of 0.003 ml of the concentrated protein solution with 0.003 ml of the reservoir solution containing 16.25% PEG 4000, 0.2 M ammonium sulfate, 5% w/v 2-propanole, 0.1 M HEPES, pH 7.5, X-ray diffraction structure determination and analysis at 2.5 A resolution
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95
purified enzyme, half-life is 48 h or above
additional information
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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
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incubation with proteases (e.g. trypsin, V8 Staphylococcus aureus protease) has no effect on this enzyme
treatment with the proteases V8 shows no effect on the enzyme
treatment with trypsin shows little effect on the enzyme
the purified enzyme is stable in 6 M guanidinium chloride for 72 h loosing only 33% activity
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SDS
incubation with 0.1% SDS shows no effect on the enzyme. Simultaneous treatment with low SDS concentrations and heat results in an almost quantitative conversion into a second form of the enzyme with a molecular mass of 87000 Da. It is most likely a tetramer. The specific activity of the tetrameric form is about 2.5 times higher than the activity of the dimer, suggesting that even though the protein is stable and active in a dimeric state, its physiological form may be tetrameric
guanidine-HCl
after 72 h incubation with 6 M guanidinium hydrochloride at 2O°C, 67% of its enzymatic activity is retaine
guanidine-HCl
6 M, incubation for 72 h, 67% of the initial activity is retained
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gene sod, DNA and amino acid sequence determination and analysis
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Klenk, H.P.; Schleper, C.; Schwass, V.; Brudler, R.
Nucleotide sequence, transcription and phylogeny of the gene encoding the superoxide dismutase of Sulfolobus acidocaldarius
Biochim. Biophys. Acta
1174
95-98
1993
Sulfolobus acidocaldarius (Q08713), Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639 (Q08713)
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Schaefer, T.; Boenisch, H.; Kardinahl, S.; Schmidt, C.; Schaefer, G.
Three extremely thermostable proteins from Sulfolobuc and a reappraisal of the 'traffic rules'
Biol. Chem.
377
505-512
1996
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius (Q08713), Sulfolobus acidocaldarius DSM 639 (Q08713)
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Knapp, S.; Kardinahl, S.; Hellgren, N.; Tibbelin, G.; Schfer, G.; Ladenstein, R.
Refined crystal structure of a superoxide dismutase from the hyperthermophilic archaeon Sulfolobus acidocaldarius at 2.2 A resolution.
J. Mol. Biol.
285
689-702
1999
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639
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Kardinahl, S.; Schmidt, C.L.; Petersen, A.; Schaefer, G.
Isolation, characterization and crystallization of an iron-superoxide dismutase from the crenarchaeon Sulfolobus acidocaldarius
FEMS Microbiol. Lett.
138
65-70
1996
Sulfolobus acidocaldarius (Q08713), Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639 (Q08713)
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