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Literature summary for 1.15.1.1 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)

Crystallization (Comment) Organism
-
Sulfolobus acidocaldarius

General Stability

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

Localization

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

Metals/Ions

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

Molecular Weight [Da]

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

Organic Solvent Stability

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

Organism UniProt Comment Textmining
Sulfolobus acidocaldarius Q08713
-
-
Sulfolobus acidocaldarius DSM 639 Q08713
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Sulfolobus acidocaldarius

Substrates and Products (Substrate)

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

Subunits

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

Synonyms Comment Organism
Fe-superoxide dismutase
-
Sulfolobus acidocaldarius