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Literature summary for 1.15.1.1 extracted from

  • Slykhouse, T.O.; Fee, J.A.
    Physical and chemical studies on bacterial superoxide dismutases. Purification and some anion binding properties of the iron-containing protein of Escherichia coli B (1976), J. Biol. Chem., 251, 5472-5477.
    View publication on PubMed
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Inhibitors

Inhibitors Comment Organism Structure
fluoride Fe-SOD Escherichia coli
N3- binds to Fe3+, but has no effect on activity Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Iron each Fe3+ ion has 2 coordination positions available for interaction with solute molecules but only 1 is necessary for catalysis Escherichia coli
Iron 1.8-1.9 mol (gatoms) per mol of enzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli
-
 Fe-SOD
-
Escherichia coli B / ATCC 11303
-
-
-
Escherichia coli Fe-SOD
-
 Fe-SOD
-

Purification (Commentary)

Purification (Comment) Organism
Fe-SOD Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
O2- + H+
-
 Escherichia coli O2 + H2O2
-
 ?
O2- + H+
-
 Escherichia coli B / ATCC 11303 O2 + H2O2
-
 ?
O2- + H+
-
 Escherichia coli Fe-SOD O2 + H2O2
-
 ?