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Literature summary extracted from

  • Nakamura, T.; Torikai, K.; Uegaki, K.; Morita, J.; Machida, K.; Suzuki, A.; Kawata, Y.
    Crystal structure of the cambialistic superoxide dismutase from Aeropyrum pernix K1 - insights into the enzyme mechanism and stability (2011), FEBS J., 278, 598-609.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.15.1.1 expression in Escherichia coli Aeropyrum pernix

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.15.1.1 purified recombinant apo, Mn-bound and Fe-bound enzyme, in presence of PEG, 2-3 days, X-ray diffraction structure determination and analysis at 1.56 A, 1.35 A, and 1.48 A, respectively Aeropyrum pernix

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.15.1.1 Fe2+ the SOD is active with Fe2+ and Mn2+, Fe2+ activates 6fold, binding structure, overview Aeropyrum pernix
1.15.1.1 Mn2+ the SOD is active with Fe2+ and Mn2+, Mn2+ activates 20fold, binding structure, overview Aeropyrum pernix

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.15.1.1 24577
-
 in crystals, 4 * 24577, sequence calculation and gel filtration Aeropyrum pernix
1.15.1.1 24577
-
 in solution, 2 * 24577, sequence calculation and gel filtration Aeropyrum pernix
1.15.1.1 57000
-
 in solution, gel filtration Aeropyrum pernix

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.15.1.1 2 O2.- + 2 H+ + Aeropyrum pernix the SOD-catalyzed reaction proceeds through a redox cycle of metal ions, active site geometry, overview O2 + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.15.1.1 Aeropyrum pernix Q9Y8H8
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.15.1.1 27.5
-
 apoenzyme, pH not specified in the publication, 37°C Aeropyrum pernix
1.15.1.1 160
-
 Fe2+-bound enzyme, pH not specified in the publication, 37°C Aeropyrum pernix
1.15.1.1 230
-
 Fe2+-bound enzyme, pH not specified in the publication, 70°C Aeropyrum pernix
1.15.1.1 550
-
 Mn2+-bound enzyme, pH not specified in the publication, 37°C Aeropyrum pernix
1.15.1.1 2700
-
 Mn2+-bound enzyme, pH not specified in the publication, 70°C Aeropyrum pernix

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.15.1.1 2 O2.- + 2 H+ +
-
 Aeropyrum pernix O2 + H2O2
-
 ?
1.15.1.1 2 O2.- + 2 H+ + the SOD-catalyzed reaction proceeds through a redox cycle of metal ions, active site geometry, overview Aeropyrum pernix O2 + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.15.1.1 homodimer in solution, 2 * 24577, sequence calculation and gel filtration Aeropyrum pernix
1.15.1.1 homotetramer in crystals, 4 * 24577, sequence calculation and gel filtration Aeropyrum pernix

Synonyms

EC Number Synonyms Comment Organism
1.15.1.1 cambialistic superoxide dismutase
-
 Aeropyrum pernix
1.15.1.1 SOD
-
 Aeropyrum pernix

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.15.1.1 70
-
-
 Aeropyrum pernix

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.15.1.1 85
-
 the enzyme is stable in aqueous solution at temperatures up to 85°C Aeropyrum pernix

General Information

EC Number General Information Comment Organism
1.15.1.1 physiological function superoxide dismutases play a protective role against oxidative stress by catalyzing disproportionation of the superoxide anion radical to hydrogen peroxide and dioxygen Aeropyrum pernix