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Literature summary extracted from

  • Jovanovic, T.; Ascenso, C.; Hazlett, K.R.O.; Sikkink, R.; Krebs, C.; Litwiller, R.; Benson, L.M.; Moura, I.; Moura, J.J.G.; Radolf, J.D.; Huynh, B.H.; Naylor, S.; Rusnak, F.
    Neelaredoxin, an iron-binding protein from the syphilis spirochete, Treponema pallidum, is a superoxide reductase (2000), J. Biol. Chem., 275, 28439-28448.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.15.1.2 expression in Escherichia coli Treponema pallidum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.15.1.2 Fe2+/Fe3+ 0.67 iron atoms/subunit, iron atom exists as a mononuclear center in a mixture of high spin ferrous and ferric oxidation states Treponema pallidum
1.15.1.2 Zn2+ approx. 0.25 atoms/subunit Treponema pallidum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.15.1.2 13670
-
 1 * 13800 + 1 * 13670, ESI-MS Treponema pallidum
1.15.1.2 13800
-
 1 * 13800 + 1 * 13670, ESI-MS Treponema pallidum
1.15.1.2 14000
-
 2 * 14000, SDS-PAGE Treponema pallidum
1.15.1.2 26000
-
 gel filtration Treponema pallidum

Organism

EC Number Organism UniProt Comment Textmining
1.15.1.2 Treponema pallidum
-
 microaerophilic obligate human pathogen
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.15.1.2 recombinant enzyme Treponema pallidum

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.15.1.2 reduced cytochrome c + superoxide + H+ enzyme shows only very weak superoxide dismutase activity Treponema pallidum cytochrome c + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.15.1.2 dimer 2 * 14000, SDS-PAGE Treponema pallidum
1.15.1.2 dimer 1 * 13800 + 1 * 13670, ESI-MS Treponema pallidum

Synonyms

EC Number Synonyms Comment Organism
1.15.1.2 neelaredoxin
-
 Treponema pallidum