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Literature summary extracted from

  • Banci, L.; Bertini, I.; Borsari, M.; Viezzoli, M.S.; Hallewell, R.A.
    Mutation of the metal-bridging proton-donor His63 residue in human copper, zinc superoxide dismutase. Biochemical and biophysical analysis of the His63-Cys mutant (1995), Eur. J. Biochem., 232, 220-225.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.15.1.1 expression of H63C mutant in Escherichia coli Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.15.1.1 H63C Cu,Zn-SOD, mutant with exchange of metal-bridging proton-donor His63 for Cys, binds Cu2+, but not Zn2+, 1% remaining activity compared to wild-type Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.15.1.1 Co2+ Co2+ binds at zinc site Homo sapiens
1.15.1.1 Cu2+ Cu,Zn-SOD mutant H63C Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.15.1.1 Homo sapiens
-
 Cu,Zn-SOD
-
1.15.1.1 Homo sapiens CuZn-SOD
-
 Cu,Zn-SOD
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.15.1.1 2 superoxide + 2 H+ = O2 + H2O2 A metalloprotein. Enzymes from most eukaryotes contain both copper and zinc, those from mitochondria and most prokaryotes contain manganese or iron. ligand binding site and structure Homo sapiens
a

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
-
-
 Homo sapiens

Substrates and Products (Substrate)

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