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Literature summary extracted from

  • Kardinahl, S.; Schmidt, C.L.; Petersen, A.; Schaefer, G.
    Isolation, characterization and crystallization of an iron-superoxide dismutase from the crenarchaeon Sulfolobus acidocaldarius (1996), FEMS Microbiol. Lett., 138, 65-70.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.15.1.1
-
 Sulfolobus acidocaldarius

General Stability

EC Number General Stability Organism
1.15.1.1 treatment with the proteases V8 shows no effect on the enzyme Sulfolobus acidocaldarius
1.15.1.1 treatment with trypsin shows little effect on the enzyme Sulfolobus acidocaldarius

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.15.1.1 cytosol it comprises at least 11% of the cytosolic protein Sulfolobus acidocaldarius 5829
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.15.1.1 Iron contains one iron atom per dimer, the protein contains a mononuclear iron center Sulfolobus acidocaldarius

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.15.1.1 22400
-
 2 * 22400, calculated from sequence Sulfolobus acidocaldarius
1.15.1.1 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 Sulfolobus acidocaldarius
1.15.1.1 45000
-
 dimeric form, gel filtration Sulfolobus acidocaldarius
1.15.1.1 87000
-
 tetrameric form, gel filtration Sulfolobus acidocaldarius

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
1.15.1.1 guanidine-HCl after 72 h incubation with 6 M guanidinium hydrochloride at 2O°C, 67% of its enzymatic activity is retaine Sulfolobus acidocaldarius
1.15.1.1 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 Sulfolobus acidocaldarius

Organism

EC Number Organism UniProt Comment Textmining
1.15.1.1 Sulfolobus acidocaldarius Q08713
-
-
1.15.1.1 Sulfolobus acidocaldarius DSM 639 Q08713
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.15.1.1
-
 Sulfolobus acidocaldarius

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.15.1.1 2 O2.- + 2 H+
-
 Sulfolobus acidocaldarius O2 + H2O2
-
 ?
1.15.1.1 2 O2.- + 2 H+
-
 Sulfolobus acidocaldarius DSM 639 O2 + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.15.1.1 dimer 2 * 22400, calculated from sequence Sulfolobus acidocaldarius
1.15.1.1 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 Sulfolobus acidocaldarius

Synonyms

EC Number Synonyms Comment Organism
1.15.1.1 Fe-superoxide dismutase
-
 Sulfolobus acidocaldarius