flavinadeninidinukleotidin

Flavinadeninidinukleotidin (FAD) is a coenzyme derived from riboflavin, a water-soluble B vitamin. It plays a crucial role in various biochemical reactions within living organisms. FAD is composed of a ribityl group, an adenine base, and a flavin moiety. The flavin moiety consists of an isoalloxazine ring system, which is responsible for FAD's ability to accept and donate electrons, making it an essential component in redox reactions.

FAD is involved in numerous enzymatic reactions, including those catalyzed by oxidoreductases, dehydrogenases, and oxygenases. It acts as a cofactor for enzymes such as succinate dehydrogenase, which is part of the electron transport chain in cellular respiration, and glyceraldehyde-3-phosphate dehydrogenase, which plays a key role in glycolysis. FAD also participates in the synthesis of nucleotides and the metabolism of various compounds.

FAD exists in two forms: oxidized (FAD) and reduced (FADH2). The reduced form, FADH2, is generated during electron transfer processes and can be reoxidized to FAD, releasing energy that can be used by the cell. This redox cycle is vital for maintaining cellular energy balance and supporting various metabolic pathways.

FAD is found in all living organisms, from bacteria to humans. It is synthesized in the body from riboflavin and is also obtained through the diet. Adequate intake of riboflavin is essential for maintaining optimal levels of FAD and supporting overall health. Deficiencies in riboflavin can lead to various health issues, including anemia, dermatitis, and neurological problems.