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Literature summary for 1.15.1.1 extracted from

  • Whittaker, M.M.; Whittaker, J.W.
    Recombinant superoxide dismutase from a hyperthermophilic archaeon, Pyrobaculum aerophilium (2000), J. Biol. Inorg. Chem., 5, 402-408.
    View publication on PubMed
Search for more literature for 1.15.1.1

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pyrobaculum aerophilum

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ the purified apoprotein can be reconstituted with either Mn2+ or Fe2+ by heating the protein with the appropriate metal salt at 95°C. Both Mn- and Fe-reconstituted enzyme exhibits superoxide dismutase activity, with the Mn-containing enzyme having the higher activity Pyrobaculum aerophilum
Mn2+ the purified apoprotein can be reconstituted with either Mn2+ or Fe2+ by heating the protein with the appropriate metal salt at 95°C. Both Mn- and Fe-reconstituted enzyme exhibits superoxide dismutase activity, with the Mn-containing enzyme having the higher activity Pyrobaculum aerophilum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
24000
-
 4 * 24000, SDS-PAGE Pyrobaculum aerophilum
24204
-
 4 * 24204, calculated from sequence Pyrobaculum aerophilum
61000
-
 gel filtration Pyrobaculum aerophilum

Organism

Organism UniProt Comment Textmining
Pyrobaculum aerophilum O93724
-
-
Pyrobaculum aerophilum IM2 O93724
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pyrobaculum aerophilum

Subunits

Subunits Comment Organism
tetramer 4 * 24000, SDS-PAGE Pyrobaculum aerophilum
tetramer 4 * 24204, calculated from sequence Pyrobaculum aerophilum

Synonyms

Synonyms Comment Organism
PASOD
-
 Pyrobaculum aerophilum