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Literature summary for 1.15.1.1 extracted from

  • Lee, H.J.; Kwon, H.W.; Koh, J.U.; Lee, D.K.; Moon, J.Y.; Kong, K.H.
    An efficient method for the expression and reconstitution of thermostable Mn/Fe superoxide dismutase from Aeropyrum pernix K1 (2011), J. Microbiol. Biotechnol., 20, 727-731.
    View publication on PubMed
Search for more literature for 1.15.1.1

Cloned(Commentary)

Cloned (Comment) Organism
overexpressed as a GST fusion protein at a high level in Escherichia coli Aeropyrum pernix

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ the enzyme is active with either Fe(II) or Mn(II) as a cofactor. The recombinant enzyme is produced in Escherichia coli expressed as an apoprotein. This apoprotein shows no SOD activity. The recombinant is activated with Fe(NH4)2(SO4)2 and MnSO4 salts at elevated temperature. The Fe-reconstituted enzyme contains 0.79 atom of iron per subunit Aeropyrum pernix
Mn2+ the enzyme is active with either Fe(II) or Mn(II) as a cofactor. The recombinant enzyme is produced in Escherichia coli expressed as an apoprotein. This apoprotein shows no SOD activity. The recombinant is activated with Fe(NH4)2(SO4)2 and MnSO4 salts at elevated temperature. The Mn-reconstituted enzyme contains 0.82 atom of manganese per subunit Aeropyrum pernix

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
25000
-
 2 * 25000, SDS-PAGE Aeropyrum pernix
56000
-
 gel filtration Aeropyrum pernix

Organism

Organism UniProt Comment Textmining
Aeropyrum pernix Q9YE27
-
-
Aeropyrum pernix DSM 11879 Q9YE27
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Aeropyrum pernix

Subunits

Subunits Comment Organism
homodimer 2 * 25000, SDS-PAGE Aeropyrum pernix

Synonyms

Synonyms Comment Organism
APE0743
-
 Aeropyrum pernix