. Allergopedia

Λεξικό .. Acid phosphatase

Enzyme isolated from bee venom in 1977. It has molecular weight around 49000 and in solution exhibits a tendency to aggregate[1]. The acid phosphatase Api m 3 is the major allergen of the honeybee venom. Georgieva D, et al, (2009) applied homology modeling to assign the three-dimensional structure of Api m 3.

The structure of the homodimeric human prostatic acid phosphatase was used to model the Api m 3 tertiary structure. IgE epitopes and antigenic sites were predicted using programs based on the structure of known epitopes and analysis of the 3-D model. The model of Api m 3 revealed an active site similar to those of the histidine-type acid phosphatases with conservation of the catalytically important residues. The observed substitutions in the phosphate ion binding site suggest differences in the substrate specificity in comparison to other acid phosphatases. The analysis of the Api m 3 three-dimensional model revealed a very likely mechanism of enzyme action [2]..


Hoffman, D.R.: Allergens in bee venom III. Identification of allergen B of bee venom as acid phosphatase. J. Allergy Clin. Immunol. 1977:59:364-366.

Georgieva D, Greunke K, Genov N, Betzel C. 3-D Model of the bee venom acid phosphatase: insights into allergenicity. Biochem Biophys Res Commun. 2009 Jan 23;378(4):711-5.

Γκέλης Ν.Δ. - Λεξικό Αλλεργίας - Εκδόσεις ΒΕΛΛΕΡOΦΟΝΤΗΣ - Κόρινθος 2013

Gelis Ν.D. - Dictionary of Allergies - VELLEROFONTIS Publications - Corinth 2013