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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).
Structure of the medium-chain acyl-CoA dehydrogenase tetramer. FAD molecules are shown in yellow. The medium chain acyl-CoA dehydrogenase (MCAD) is the best known structure of all ACADs, and is the most commonly deficient enzyme within the class that leads to metabolic disorders in animals. [1]
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]
Flavin adenine dinucleotide is a group bound to many enzymes including ferredoxin-NADP+ reductase, monoamine oxidase, D-amino acid oxidase, glucose oxidase, xanthine oxidase, and acyl CoA dehydrogenase.
Flavin Adenine Dinucleotide. FAD, or flavin adenine dinucleotide, is a prosthetic group (a non-polypeptide unit bound to a protein that is required for function) that consists of an adenine nucleotide and a flavin mononucleotide. [10] FAD is a unique electron acceptor.
Riboflavin is reversibly converted to FMN and then FAD. From riboflavin to FMN is the function of zinc-requiring riboflavin kinase; the reverse is accomplished by a phosphatase. From FMN to FAD is the function of magnesium-requiring FAD synthase; the reverse is accomplished by a pyrophosphatase. FAD appears to be an inhibitory end-product that ...
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 ...
The Rossmann fold is a tertiary fold found in proteins that bind nucleotides, such as enzyme cofactors FAD, NAD +, and NADP +.This fold is composed of alternating beta strands and alpha helical segments where the beta strands are hydrogen bonded to each other forming an extended beta sheet and the alpha helices surround both faces of the sheet to produce a three-layered sandwich.