Dehydrogenases in the Flavoprotein Amine Oxidoreductase Superfamily.

ABSTRACT: Enzymes of the ubiquitous flavoprotein amine oxidoreductase (FAO) superfamily catalyze C-N bond oxidation of amine-containing substrates using flavin adenine dinucleotide (FAD) as a prosthetic group. Their reaction proceeds via a two-step mechanism involving hydride transfer from the substrate to the bound FAD cofactor, and the reduced flavin is subsequently reoxidized by a physiological electron acceptor. For nearly a century, it has been generally accepted that all enzymes in the FAO superfamily are oxidases, i.e., donating the electrons from substrate oxidation to dioxygen (O₂). However, we recently showed that the FAO family enzymes nicotine oxidoreductase and pseudooxynicotine amine oxidase are not oxidases because they do not utilize oxygen efficiently, and instead are cyt

SUBMITTER: Akram J 

PROVIDER: S-EPMC12224317 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature