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In biochemistry, flavin adenine dinucleotide (FAD) is a redox-active coenzyme associated with various proteins, which is involved with several enzymatic reactions in metabolism. A flavoprotein is a protein that contains a flavin group , which may be in the form of FAD or flavin mononucleotide (FMN).
About 5-10% of flavoproteins have a covalently linked FAD. [2] Based on the available structural data, FAD-binding sites can be divided into more than 200 different types. [3] 90 flavoproteins are encoded in the human genome; about 84% require FAD and around 16% require FMN, whereas 5 proteins require both. [4]
The oxidized and reduced forms are in fast equilibrium with the semiquinone form, shifted against the formation of the radical: [2] Fl ox + Fl red H 2 ⇌ FlH • where Fl ox is the oxidized flavin, Fl red H 2 the reduced flavin (upon addition of two hydrogen atoms) and FlH • the semiquinone form (addition of one hydrogen atom).
In enzymology, a FMN adenylyltransferase (EC 2.7.7.2) is an enzyme that catalyzes the chemical reaction. ATP + FMN diphosphate + FAD. Thus, the two substrates of this enzyme are ATP and FMN, whereas its two products are diphosphate and FAD.
In enzymology, a FAD diphosphatase (EC 3.6.1.18) is an enzyme that catalyzes the chemical reaction FAD + H 2 O ⇌ {\displaystyle \rightleftharpoons } AMP + FMN Thus, the two substrates of this enzyme are FAD and H 2 O , whereas its two products are AMP and FMN .
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In molecular biology FAD-oxidases are a family of FAD-dependent oxidoreductases. They are flavoproteins that contain a covalently bound FAD group which is attached to a histidine via an 8-alpha-(N3-histidyl)-riboflavin linkage. The region around the histidine that binds the FAD group is conserved in these enzymes. [1]
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