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Literature summary for 1.15.1.1 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)

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

Protein Variants

Protein Variants Comment Organism
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

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

Organism

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

Reaction

Reaction Comment Organism Reaction ID
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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Homo sapiens

Substrates and Products (Substrate)

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