Recombinant Human FLAD1 protein

FLAD1 (Flavin Adenine Dinucleotide Synthase 1) is a critical enzyme involved in the biosynthesis of flavin adenine dinucleotide (FAD), an essential cofactor for numerous metabolic reactions, including energy production, redox homeostasis, and DNA repair. Encoded by the *FLAD1* gene in humans, this protein catalyzes the final step of FAD synthesis by transferring an AMP moiety from ATP to flavin mononucleotide (FMN). FAD-dependent enzymes, such as dehydrogenases and oxidases, rely on this cofactor for electron transport and oxidative phosphorylation, highlighting FLAD1's central role in cellular metabolism.

Recombinant FLAD1 protein is produced through genetic engineering techniques, typically by expressing the *FLAD1* gene in bacterial, yeast, or mammalian cell systems. This allows large-scale production of the purified enzyme for functional and structural studies. Researchers often utilize recombinant FLAD1 to investigate its catalytic mechanisms, substrate specificity, and interactions with other metabolic components. Structural analyses, including X-ray crystallography and cryo-EM, have provided insights into its bifunctional domains: an N-terminal FMN-binding region and a C-terminal ATP-binding site.

Mutations in *FLAD1* are linked to mitochondrial disorders, such as lipid storage myopathy and respiratory chain deficiencies, underscoring its biomedical relevance. Recombinant FLAD1 serves as a tool to study these pathologies, enabling the development of enzyme replacement therapies or small-molecule modulators. Additionally, its role in FAD-dependent processes connects it to cancer metabolism and neurodegenerative diseases, where altered redox states are common. By elucidating FLAD1's molecular dynamics and regulatory networks, recombinant protein studies contribute to therapeutic strategies targeting FAD-related metabolic dysfunctions.