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

BRENDA support

Literature summary extracted from

  • Lee, Y.M.; Misra, H.P.; Ayala, F.J.
    Superoxide dismutase in Drosophila melanogaster: biochemical and structural characterization of allozyme variants (1981), Proc. Natl. Acad. Sci. USA, 78, 7052-7055.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.15.1.1 Cu2+
-
 Drosophila melanogaster
1.15.1.1 Zn2+
-
 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 allozyme variants: DSDS and DSDF Drosophila melanogaster

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
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.15.1.1 50
-
 several h, stable Drosophila melanogaster
1.15.1.1 70
-
 5 min, complete loss of activity Drosophila melanogaster