AllFam - Database of allergen families Department of Pathophysiology and Allergy Research Medical University of Vienna

AF073: Pectate lyase

Pfam domains
PF00544: Pectate lyase

Biochemical properties

Pectate lyases are enzymes from plants and plant pathogens involved in the maceration and soft rotting of plant tissue [1]. They catalyze the eliminative cleavage of pectate, yielding oligosaccharides with 4-deoxy-α-D-mann-4-enuronosyl groups at their non-reducing ends. Pectate lyases are maximally expressed late in pollen development where they are involved in pectin degradation during pollen tube growth.

Allergological significance

Two groups of allergens belong to this family. The group 1 Cupressaceae pollen allergens are major allergens identified in cedars, junipers, and cypresses [2]. The major ragweed pollen allergens Amb a 1 and Amb a 2 show no IgE cross-reactivity to homologues from Cupressaceae [3]. In addition, an IgE binding pectate lyase (Pen c 32) was identified in the mould Penicillium citrinum [4].

References

  1. Marin-Rodriguez MC, Orchard J, Seymour GB.
    Pectate lyases, cell wall degradation and fruit softening.
    J Exp Bot 2002, 53, 2115-9. [PubMed]
  2. Di Felice G, Barletta B, Tinghino R, Pini C.
    Cupressaceae pollinosis: identification, purification and cloning of relevant allergens.
    Int Arch Allergy Immunol 2001, 125, 280-9. [PubMed]
  3. Wopfner N, Gadermaier G, Egger M, Asero R, Ebner C, Jahn-Schmid B, Ferreira F.
    The spectrum of allergens in ragweed and mugwort pollen.
    Int Arch Allergy Immunol 2005, 138, 337-46. [PubMed]
  4. Chiu LL, Lee KL, Lin YF, Chu CY, Su SN, Chow LP.
    Secretome analysis of novel IgE-binding proteins from Penicillium citrinum.
    Proteomics Clin Appl 2008, 2, 33-45.

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