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Literature summary extracted from

  • Lee, Y.M.; Ayala, F.J.; Misra, H.P.
    Purification and properties of superoxide dismutase from Drosophila melanogaster (1981), J. Biol. Chem., 256, 8506-8509.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.15.1.1 CN- at 1-3 mM, complete inhibition; Cu,Zn-SOD Drosophila melanogaster
1.15.1.1 N3- Fe-SOD, slightly Drosophila melanogaster

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.15.1.1 Cu2+ 2 mol of Cu per mol of enzyme Drosophila melanogaster
1.15.1.1 Zn2+ 2 mol of Zn2+ per mol of enzyme Drosophila melanogaster

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.15.1.1 32000 32500 gel filtration Drosophila melanogaster

Organism

EC Number Organism UniProt Comment Textmining
1.15.1.1 Drosophila melanogaster
-
 Cu,Zn-SOD
-
1.15.1.1 Drosophila melanogaster CuZn-SOD
-
 Cu,Zn-SOD
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.15.1.1 Cu,Zn-SOD Drosophila melanogaster

Source Tissue

EC Number Source Tissue Comment Organism Textmining

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 additional information
-
-
 Drosophila melanogaster

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.15.1.1 O2- + H+
-
 Drosophila melanogaster O2 + H2O2
-
 ?
1.15.1.1 O2- + H+
-
 Drosophila melanogaster CuZn-SOD O2 + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.15.1.1 dimer
-
 Drosophila melanogaster