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Literature summary for 1.15.1.1 extracted from

  • Pinto, A.F.; Romao, C.V.; Pinto, L.C.; Huber, H.; Saraiva, L.M.; Todorovic, S.; Cabelli, D.; Teixeira, M.
    Superoxide reduction by a superoxide reductase lacking the highly conserved lysine residue (2015), J. Biol. Inorg. Chem., 20, 155-164.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Ignicoccus hospitalis

Protein Variants

Protein Variants Comment Organism
additional information the mutant enzymes lacking the glutamate and lysine residues close to the active site can be a competent superoxide reductase Ignicoccus hospitalis

Metals/Ions

Metals/Ions Comment Organism Structure
Iron contains 0.95 atoms of Fe per monomer Ignicoccus hospitalis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
14000
-
4 * 14000, SDS-PAGE Ignicoccus hospitalis

Organism

Organism UniProt Comment Textmining
Ignicoccus hospitalis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Ignicoccus hospitalis

Subunits

Subunits Comment Organism
homotetramer 4 * 14000, SDS-PAGE Ignicoccus hospitalis