page_title: BBE-like enzymes
section_title: Properties
hierarchical_section_title: BBE-like enzymes / Properties
caption_attribution_description: English: pH scale showing the BBE-like enzymes' optimum pH, and their isoelectric point.
context_page_description: Berberine bridge enzyme-like form a subgroup of the superfamily of FAD-linked oxidases, structurally characterized by a typical fold observed initially for vanillyl-alcohol oxidase. This proteins are part of a multigene family that can be found in plants, fungi and bacteria.
  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-reticuline oxidase or berberine bridge enzyme from California poppy, the responsible of catalyzing the conversion of-reticuline to-scoulerine. This conversion is made by an oxidative ring closure reaction. The product of this reaction is the C-C bond and is referred to as the berberine bridge. Also, marks a branch point in the biosynthesis of benzylisoquinoline alkaloids.
  As mentioned above, BBE-like enzymes are in the large family of FAD-linked oxidases. Regarding the structure of this particular family, they have a FAD binding module formed by the N- and C- terminal parts of the protein.
context_section_description: The BBE-like enzyme's optimum pH is 8.9, this means it works in an alkaline medium, but the isoelectric point of the homogeneous enzyme is located at pH 4.9, which is a rather an acid medium. This value was obtained with isoelectric focusing and chromatofocusing techniques.
  The enzyme broad temperature range is between 40-50 degrees Celsius. The molecular weight of the protein was determined by two processes that show two different results: by SDS gel electrophoresis comes to be 54 kD, and by gel filtration on AcA 54 the enzyme corresponds to a molecular weight of 49 kD, adopting globular shape. A purification study shows that the true molecular weight is in the range of 52 ±4 kD.
  On the other hand, total activity decreases drastically during the stationary phase.
caption: pH scale showing the BBE-like enzyme's optimum pH and isoelectric point.
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