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 identified 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 originally 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 .
Family-defining Pfam domains (at least one of these domains is present in each family member):
|Pfam domain||Pfam clan|
|PF01565||FAD binding domain||CL0077||PCMH-like FAD binding|
|PF08031||Berberine and berberine like||CL0277||FAD-linked oxidase C-terminal domain superfamily|
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