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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]
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]
There are 18 key atoms in isoalloxazine that make up its characteristic three-ring structure. The R-group varies and differentiates various flavins. Riboflavin. Flavins (from Latin flavus, "yellow") refers generally to the class of organic compounds containing the tricyclic heterocycle isoalloxazine or its isomer alloxazine, and derivatives thereof.
Therefore, SDHA is a flavoprotein (Fp) due to the prosthetic group flavin adenine dinucleotide (FAD). Crystal structure suggests that FAD is covalently bound to a histidine residue (His99) and further coordinated by hydrogen bonds with number of other amino acid residues within the FAD-binding domain. FAD which is derived from riboflavin ...
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.
The succinate dehydrogenase complex showing several cofactors, including flavin, iron–sulfur centers, and heme.. A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst (a catalyst is a substance that increases the rate of a chemical reaction).
The glutamate residue is highly conserved because it both stabilizes the semiquinone form of FAD and is a proton donor/acceptor in the reaction. [5] The rate limiting step of the electron transfer reaction is the release of the first oxidized ferredoxin molecule after the reduction of FAD with one electron. [3]