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Literature summary for 1.15.1.1 extracted from

  • Goscin, S.A.; Fridovich, I.
    The purification and properties of superoxide dismutase from Saccharomyces cerevisiae (1972), Biochim. Biophys. Acta, 289, 276-283.
    View publication on PubMed
Search for more literature for 1.15.1.1

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ 2 mol of Cu per mol of enzyme Saccharomyces cerevisiae
Zn2+ 1.8 mol of Zn per mol of enzyme Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
18300
-
 2 * 18300, Cu,Zn-SOD, SDS-PAGE Saccharomyces cerevisiae
32700
-
 Cu,Zn-SOD, sedimentation equilibrium analysis Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
 Cu,Zn-SOD
-
Saccharomyces cerevisiae CuZn-SOD
-
 Cu,Zn-SOD
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein no carbohydrate-containing enzyme Saccharomyces cerevisiae

Purification (Commentary)

Purification (Comment) Organism
Cu,Zn-SOD Saccharomyces cerevisiae

Reaction

Reaction Comment Organism Reaction ID
2 superoxide + 2 H+ = O2 + H2O2 amino acid composition, comparison Saccharomyces cerevisiae
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
O2- + H+
-
 Saccharomyces cerevisiae O2 + H2O2
-
 ?
O2- + H+
-
 Saccharomyces cerevisiae CuZn-SOD O2 + H2O2
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 18300, Cu,Zn-SOD, SDS-PAGE Saccharomyces cerevisiae