AF019: Cu/Zn Superoxide dismutase

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Include only IUIS approved allergens.

Biochemical properties

Superoxide dismutases (SODs) are ubiquitous metalloproteins that prevent damage by oxygen-mediated free radicals by catalyzing the dismutation of superoxide into molecular oxygen and hydrogen peroxide [1]. There are three families of SODs differing in their metal cofactor and their species distribution. CU/Zn-SODs are found mostly in eukaryotes, Fe/Mn-SODs in prokaryotes, mitochondria and protists and Ni-SODs in prokaryotes. The Cu/Zn SOD folds into an eight-stranded β-sandwich, similar to the immunoglobulin fold [2].

Allergens from this family

The minor olive pollen allergen Ole e 5 belongs to this family [3].

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References

  1. Fridovich I:
    Superoxide anion radical (O2-.), superoxide dismutases, and related matters.
    J Biol Chem 1997, 272, 18515-7. [PubMed]
  2. Tainer JA, Getzoff ED, Beem KM, Richardson JS, Richardson DC:
    Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase.
    J Mol Biol 1982, 160, 181-217. [PubMed]
  3. Butteroni C, Afferni C, Barletta B, Iacovacci P, Corinti S, Brunetto B, Tinghino R, Ariano R, Panzani RC, Pini C, Di Felice G:
    Cloning and Expression of the Olea europaea allergen Ole e 5, the pollen Cu/Zn superoxide dismutase.
    Int Arch Allergy Immunol 2005, 137, 9-17. [PubMed] [Full Text]

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Links to Pfam

Family-defining Pfam domains (at least one of these domains is present in each family member):

Pfam domain Pfam clan
PF00080 Copper/zinc superoxide dismutase (SODC) -

Links to Wikipedia

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