ArticleBiochemistry2025
Dehydrogenases in the Flavoprotein Amine Oxidoreductase Superfamily.
Article in Biochemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Whole genome insights into hydrocarbon degradation and antimicrobial resistance in Staphylococcus epidermidis CSR1 isolated from oil-contaminated soil.Archives of microbiology · 2026Article
- Combined transcriptomic and proteomic analysis reveals the response mechanisms of alfalfa to freezing stress.Frontiers in plant science · 2025Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
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 (O
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