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Literature summary for 1.15.1.2 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)

Cloned (Comment) Organism
expression in Escherichia coli Treponema pallidum

Metals/Ions

Metals/Ions Comment Organism Structure
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
Zn2+ approx. 0.25 atoms/subunit Treponema pallidum

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Treponema pallidum
-
microaerophilic obligate human pathogen
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Treponema pallidum

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
neelaredoxin
-
Treponema pallidum