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Literature summary for 1.15.1.1 extracted from

  • Rigo, A.; Viglino, P.; Rotilio, G.
    Kinetic study of o2-dismutation by bovine superoxide dismutase. Evidence for saturation of the catalytic sites by O-2 (1975), Biochem. Biophys. Res. Commun., 63, 1013-1018.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
CN- Cu,Zn-SOD Bos taurus
OH- Cu,Zn-SOD, competitively Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.355
-
O2-
-
Bos taurus

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+
-
Bos taurus
Zn2+
-
Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
Cu,Zn-SOD
-
Bos taurus CuZn-SOD
-
Cu,Zn-SOD
-

Reaction

Reaction Comment Organism Reaction ID
2 superoxide + 2 H+ = O2 + H2O2 mechanism Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
-
Bos taurus
-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
100000
-
O2.-
-
Bos taurus