2017/07/01 by Bastian Daniel, Barbara Konrad, Marina Toplak +4 · 3 citations
Agricultural and Biological Sciences · Biochemistry, Genetics and Molecular Biology · Environmental Science · #Enzyme-mediated dye degradation #Microbial bioremediation and biosurfactants #Polyamine Metabolism and Applications
paper · pdf · doi:10.1016/j.abb.2017.06.023
openalex publication_date 2017/07/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/01
Biological oxidations form the basis of life on earth by utilizing organic compounds as electron donors to drive the generation of metabolic energy carriers, such as ATP. Oxidative reactions are also important for the biosynthesis of complex compounds, i.e. natural products such as alkaloids that provide vital benefits for organisms in all kingdoms of life. The vitamin B 2 -derived cofactors flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) enable an astonishingly diverse array of oxidative reactions that is based on the versatility of the redox-active isoalloxazine ring. The family of FAD-linked oxidases can be divided into subgroups depending on specific sequence features in an otherwise very similar structural context. The sub-family of berberine bridge enzyme (BBE)-like enzymes has recently attracted a lot of attention due to the challenging chemistry catalyzed by its members and the unique and unusual bi-covalent attachment of the FAD cofactor. This family is the focus of the present review highlighting recent advancements into the structural and functional aspects of members from bacteria, fungi and plants. In view of the unprecedented reaction catalyzed by the family's namesake, BBE from the California poppy, recent studies have provided further insights into nature's treasure chest of oxidative reactions.