Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Fee, J.A.; DeCorleto, P.E.
    Observations on the oxidation-reduction properties of bovine erythrocyte superoxide dismutase (1973), Biochemistry, 12, 4893-4899.
    View publication on PubMed

Metals/Ions

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

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
1.15.1.1 2 superoxide + 2 H+ = O2 + H2O2 mechanism Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.15.1.1 erythrocyte
-
Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.15.1.1 additional information addition of hexacyanoferrate results in reduction of Cu(II) to Cu(I) Bos taurus ?
-
?
1.15.1.1 additional information addition of hexacyanoferrate results in reduction of Cu(II) to Cu(I) Bos taurus CuZn-SOD ?
-
?
1.15.1.1 O2- + H+
-
Bos taurus O2 + H2O2
-
?
1.15.1.1 O2- + H+
-
Bos taurus CuZn-SOD O2 + H2O2
-
?