Flavin adenine dinudeotide

Another characteristic of enzymes is their frequent need for cofactors. A cofactor is a nonprotein compound that combines with the otherwise inactive enzyme to give the active enzyme. Examples of cofactors are metal ions such as Ca2+, Cu2+, Co2+, Fe2+, and Mg2+, and organic molecules such as nicotinamide adenine dinucleotide (NAD) and flavin adenine dinudeotide (FAD). 

Flavin adenine dinudeotide, see FAD Flavin miinirmucLecitide. iee FMN Flavins, 609,612 Flavoprotelns, 609,611 Fluoride, bone and, 778-780 Fluomapatile. 779 Flufimsis, 77 ... 

Hustad S, McKinley MC, McNulty H, Schneede J, Strain fJ, Scott JM, Ueland PM. Riboflavin, flavin mononucleotide, and flavin adenine dinudeotide in human plasma and erythrocytes at baseline and after low-dose riboflavin supplementation. Clin Chem 2002 48 1571-7. 

Figure 8.27 Mechanism-based (suicide) inhibition. Monoamine oxidase, an enzyme important for neurotransmitter synthesis, requires the cofactor FAD (flavin adenine dinudeotide). N./V-Dimethylpropargylamine inhibits monoamine oxidase by covalently modifying the flavin prosthetic group only after the inhibitor has been oxidized. The N-5 flavin adduct is stabilized by the addition of a proton.

Riboflavin (Bj) Flavin adenine dinudeotide (FAD) Oxidation-reduction Cheliosis and angular stomatitis (lesions of the mouth), dermatitis... 

Fig. 1.1Z Schemalic dkBwing of the glucose oxidase molecule, showing the electron-transfer dslances involved in the various steps of moving an electron from its two flavin adenine dinudeotide/reduced flavin adenine dnudeotide (FAD/FADHg) centers to a metal electrode. Left The enzyme before modfication. Right The modified enzyme, after chemical attachment of an array of electron transfer relays ( R ). (Reprinted from Y. Degani and A. Heller, J. Phys. Chem. 91 1286, 1987.)...

Flavine adenine dinudeotide, flavine mononucleotide see riboflavin(e). 

The first committed step in the biosynthetic pathway of the branched chain amino acids is catalyzed by the enzyme acetohydroxyacid synthase (AHAS, EC 2.2.1.6), which is also referred to as acetolactate synthase (ALS). As depicted in Fig. 2.1.1, the pathway leading to valine and leucine begins with the condensation of two molecules of pyruvate accompanied by loss of carbon dioxide to give (S)-2-acetolactate. A parallel reaction leading to isoleucine involves the condensation of pyruvate with 2-ketobutyrate to afford (S)-2-aceto-2-hydroxybutyrate after loss of carbon dioxide. Both reactions are catalyzed by AHAS, which requires the cofactors thiamin diphosphate (ThDP) and flavin adenine dinudeotide (FAD). A divalent metal ion, most commonly is also required. Several excellent reviews... 

Flavin adenine dinudeotide (FAD) A biological oxidizing agent. When acting as an oxidizing agent, FAD is rednced to FADHj. 

Abb. HSCoA = Coenzyme A GSH = Glutathione AM(D)(T)P = Adenosine mono (di)(tri)phosphate TPP = Thiamin pyrophosphate LipSj = Lipoic acid amide GD(T)P = Guanosine di(tri)phosphate K = Inorganic phosphate FAD(H2) = Enzyme-bound oxidized (reduced) Flavin-adenine-dinudeotide NAD (H) = Oxidized (reduced) Nicotinamide-adenine-dinucleotide. Compounds with are competitive inhibitors. 

In biological systems the iwo-dectron reduction may be accomplished by NADH and flavin adenine dinudeotide (FAD). The methyl donor is N -melhylielrahydrofolale (CH]-THF). The C lll) corrinoid (melbylcobalamin) can then paitake in biomelhyla-tion reactions ... 

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