Adenine, dinucleotide with nicotinamide

Hendrickson CM, Bowden JA. 1976. In vitro inhibition of lactate dehydrogenase by insecticidal polychlorinated hydrocarbons I. Mechanism of inhibition Possible association of reduced nicotinamide adenine dinucleotide with mirex. J Agric Food Chem 24(2) 241-244. 

Nucleotides are stmctural units of deoxyribonucleic acid (DNA), ribonucleic acid (RNA) and cofactors such as coenzyme A (CoA), flavin adenine dinucleotide (FAD), nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP), with important roles in energy transfer, metabolism and intracellular signalling. 

Enzymatic cofactors, such as nicotinamide adenine dinucleotide (NADH), nicotinamide adenine dinucleotide phosphate (NADPH), flavin adenine dinucleotide (EAD), flavin mononucleotide (EMN), and pyridoxal phosphate, are fluorescent and commonly found associated with various proteins where they are responsible for electron transport (see Fig. lb and Table 1). NADH and NADPH in the oxidized form are nonfluorescent, whereas conversely the flavins, FAD and EMN, are fluorescent only in the oxidized form. Both NADH and FAD fluorescence is quenched by the adenine found within their cofactor structures, whereas NADH-based cofactors generally remain fluorescent when interacting with protein structures. The fluorescence of these cofactors is often used to study the cofactors interaction with proteins as well as with related enzymatic kinetics (1, 9-12). However, their complex fluorescent characteristics have not led to widespread applications beyond their own intrinsic function. 

M. Masoom and A. Townshend, Cyclic Regeneration of Nicotinamide Adenine Dinucleotide with Immobilized Enzymes. Flow-Injection Spectro-fluorimetric Determination of Ethanol. Anal. Chim. Acta, 185 (1986) 49. 

FIGURE 10.5 Extracted ion chromatogram of the analytes and system control standard (A thiamine, B riboflavin, C flavin adenine dinucleotide, D nicotinamide, E pyridoxal, F -caffeine). (Adapted from Hampel, D., York, E., and Allen, L. 2012. J. Chromatogr. B. 903 7-13. With permission.)... 

This 584 page monograph contains a comprehensive discussion on the determination of the electrochemical potentials of organic systems with emphasis both on theory and experimental practice. Included are approximately 100 tables of critically evaluated oxidation and reduction potentials for organic and biochemical systems through about 1960. Included are the quinones, phenols, anilines, porphyrins, nicotinamide-adenine dinucleotide, and nicotinamide-adenine dinucleotide phosphate systems, and several others. The author has, in most cases, specified the conditions to which the data refer. 

Using a CNT-coated graphite electrode, Wang et al. have demonstrated a good voltammetric resolution for DA and AA with an anodic potential difference of 270 mV in a pH 5.0 phosphate buffer, which indicates a high selectivity for DA over AA. The observed difference in electrocatalysis toward DA and AA was attributed to a three-dimensional (3D) porous interfacial layer associated with the CNT-modified electrode. The CNT-modified electrodes were also found to exhibit a strong and stable electrocatalytic response to NADH (reduced nicotinamide adenine dinucleotide) with a... 

The 2,3-butanediol cycle in bacteria, as proposed by Juni and Heym (1956). The boxed area represents 2,3-BD formation in bacteria. BDL butanediol TPP thiamine pyrophosphate AACS acetyiacetoin synthase AACR acetyiacetoin reductase NAD nicotinamide adenine dinucleotide NADH reduced nicotinamide adenine dinucleotide NADP nicotinamide adenine dinucleotide phosphate NADPH reduced nicotinamide adenine dinucleotide phosphate (Redrawn from Syu (2001), with permission)... 

Oxidoreductase enzymes include dehydrogenases, reductases, and oxidases that typically contain flavin adenine dinucleotide (FAD), nicotinamide adenine dinucleotide phosphate (NAD(P)" ), or pyrroloquinohne quinone (PQQ) as redox cofactors. Although some specific enzymes possess cofactors with theoretically low redox potentials, this does not always translate to efficient performance when immobilized onto electrodes for BFCs. The caveat provides a need to study... 

Dehydrogenases and reductases require a coenz5mie such as nicotinamide adenine dinucleotide (NADH), nicotinamide adenine dinucleotide phosphate (NADPH), flavin, etc. The reduction of a carbonyl compoxmd with NAD(P)H with auxiliary substance proceeds as follows (Figure 11.1a). 

Insects poisoned with rotenone exhibit a steady decline ia oxygen consumption and the iasecticide has been shown to have a specific action ia interfering with the electron transport iavolved ia the oxidation of reduced nicotinamide adenine dinucleotide (NADH) to nicotinamide adenine dinucleotide (NAD) by cytochrome b. Poisoning, therefore, inhibits the mitochondrial oxidation of Krebs-cycle iatermediates which is catalysed by NAD. 

Nicotinamide, (S)-N-(a-methylbenzyl)-hydrogen bonding, 2, 111 Nicotinamide, N-phenyl-hydrogen bonding, 2, 111 Nicotinamide adenine dinucleotide in biochemical pathways, 1, 248 coenzyme system with NADH, 2, 121 reactions, 2, 382 reduction, 2, 281, 283... 

Nicotinamide adenine dinucleotide phosphate (NADP, TPN) [53-59-8] M 743.4, pK] 1.1 (PO4H2), pK 4.0 (adenine NH ), pKa 6.1 (P04 ). Purified by anion-exchange chromatography in much the same way as for NAD [Dalziel and Dickinson Biochem J 95 311 7965 Biochemical Preparations 11 87 7966]. Finally it is purified by dissolving in H2O and precipitating with 4 volumes of Me2CO and dried in... 

The first step in the biological degradation of lysine is reductive animation with a-ketoglutarate to give saccharopine. Nicotinamide adenine dinucleotide phosphate (NADPH), a relative of NADH, is the reducing agent. Show the mechanism. 

Newman, Melvin S., 93 Newman projection, 93 molecular model of, 93 Nicotinamide adenine dinucleotide, biological oxidations with, 625-626 reactions of, 725 structure of, 725, 1044 Nicotinamide adenine dinucleotide (reduced), biological reductions with, 610-611... 

Ethanol Electrodes The reliable sensing of ethanol is of great significance in various disciplines. The enzymatic reaction of ethanol with the cofactor nicotinamide-adenine dinucleotide (NAD+), in the presence of alcohol dehydrogenase (ADH)... 

Reduced nicotinamide-adenine dinucleotide (NADH) plays a vital role in the reduction of oxygen in the respiratory chain [139]. The biological activity of NADH and oxidized nicotinamideadenine dinucleotide (NAD ) is based on the ability of the nicotinamide group to undergo reversible oxidation-reduction reactions, where a hydride equivalent transfers between a pyridine nucleus in the coenzymes and a substrate (Scheme 29a). The prototype of the reaction is formulated by a simple process where a hydride equivalent transfers from an allylic position to an unsaturated bond (Scheme 29b). No bonds form between the n bonds where electrons delocalize or where the frontier orbitals localize. The simplified formula can be compared with the ene reaction of propene (Scheme 29c), where a bond forms between the n bonds. 

The samples of l,6-T2-DBpD and l,6-T2-2,3,7,8-Cl4-DBpD are useful in metabolism and mode of action studies. For example, when incubated with rabbit liver microsomes, l,6-T.>-DBpD is extensively metabolized to polar product(s) but only when these preparations are fortified with reduced nicotinamide-adenine dinucleotide phosphate. Under the same conditions l,6-T2-2,3,7,8-Cl4-DBpD is completely resistant to metabolic attack. In some types of studies, a higher specific activity possibly is desirable i.e., >1 Ci/mmole), and this can be achieved, with the methodology already developed, by using larger amounts of tritium gas or working on a larger synthetic scale so that it is not necessary to add unlabeled materials to assist in crystallization steps where a certain minimum amount of compound is necessary. 

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