[2] BBE-like enzymes family form a large subgroup that have a special C-terminal structural element adjacent to the substrate binding region.
An homonym of this family is the (S)-reticuline oxidase or berberine bridge enzyme from California poppy (Eschscholzia californica), the responsible of catalyzing the conversion of (S)-reticuline to (S)-scoulerine.
Regarding the structure of this particular family, they have a FAD binding module formed by the N- and C- terminal parts of the protein.
In order to eliminate most of these interfering cationic substances, the enzyme solution was treated first with carboxymethyl-Sepharose and subsequently with dextrancoated charcoal.
After that, the resulting solution was fractionated using standard procedures and generated, after isoelectric focusing, a single protein band in SDS gel electrophoresis.
The mechanism through which reactions are catalyzed by these BBE-like enzymes has not been found yet, but the resulting conformation of the products suggests that a similar coupling of substrate oxidation and ring formation occurs in these processes.
A member of these enzymes is hexose oxidase (HOX) from Chondrus crispus, a red algae that belongs to the division of Rhodophyta.
Berberine has been known to influence weight loss, and this antiobesity effect may benefit all conditions related to increased body mass such as hypertension, dyslipidemia or pre-diabetes.
Overall, this alkaloid might be useful in the treatment and study of diseases like polycystic ovary syndrome (PCOS), some types of cancer, heart problems or dyslipidemia.