AF099: Berberine bridge enzyme
- Pfam domains
- PF01565: FAD binding domain
- PF08031: Berberine and berberine like
Berberine bridge and berberine bridge-like enzymes are plant enzymes involved in the biosynthesis of numerous isoquinoline alkaloids. Berberine bridge enzymes catalyze the transformation of the N-methyl group of (S)-reticuline into the C-8 berberine bridge carbon of (S)-scoulerine . Members of this family are flavoproteins that contain a conserved FAD-binding domain.
The first allergen from this family was BG60 from Bermuda grass pollen . Homology to BBEs was also found for Phl p 4 from timothy grass , Api g 5 from celery tuber , and a high molecular weight allergen from Brassica napus pollen . These allergens are glycoproteins and were orginally thought to bind human IgE exclusively via their N-liked glycan moieties . However, recombinant Phl p 4 expressed in Escherichia coli bound IgE of nearly all sera of nPhl p 4-sensitized patients .
Molecular characterization of berberine bridge enzyme genes from opium poppy.
Plant Physiol 1996, 112, 1669-77. [PubMed]
Immunologic and physicochemical studies of Bermuda grass pollen antigen BG60.
J Allergy Clin Immunol 1996, 98, 486-94. [PubMed]
Cloning, expression and immunological characterization of full-length timothy grass pollen allergen Phl p 4, a berberine bridge enzyme-like protein with homology to celery allergen Api g 5.
Clin Exp Allergy 2006, 36, 77-86. [PubMed]
Cross-reactive N-glycans of Api g 5, a high molecular weight glycoprotein allergen from celery, are required for immunoglobulin E binding and activation of effector cells from allergic patients.
FASEB J 2003, 17, 1697-9. [PubMed]
Characterization of high-molecular-mass allergens in oilseed rape pollen.
Int Arch Allergy Immunol 2001, 125, 128-34. [PubMed]
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