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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).
FMOs have a tightly bound FAD prosthetic group and a binding NADPH cofactor. [11] Both dinucleotide binding motifs form Rossmann folds. The yeast FMO and bacterial FMO are dimers, with each monomer consisting of two structural domains: the smaller NADPH binding domain and the larger FAD-binding domain. The two domains are connected by a double ...
Oxygen is used to restore the reduced FADH2 cofactor back to the active FAD form. Monoamine oxidases contain the covalently bound cofactor FAD and are, thus, classified as flavoproteins. Monoamine oxidase A and B share roughly 70% of their structure and both have substrate binding sites that are predominantly hydrophobic.
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This gives a total of four FAD molecules and four acyl-CoA substrate binding sites per enzyme. FAD is bound between the three domains of the monomer, where only the nucleotide portion is accessible. FAD binding contributes significantly to overall enzyme stability. The acyl-CoA substrate is bound completely within each monomer of the enzyme ...
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