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Literature summary for 1.15.1.1 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
Search for more literature for 1.15.1.1

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Aeropyrum pernix

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Aeropyrum pernix Q9Y8H8
-
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 O2.- + 2 H+ +
-
 Aeropyrum pernix O2 + H2O2
-
 ?
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

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

Synonyms

Synonyms Comment Organism
cambialistic superoxide dismutase
-
 Aeropyrum pernix
SOD
-
 Aeropyrum pernix

Temperature Optimum [°C]

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

Temperature Stability [°C]

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

General Information

General Information Comment Organism
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