NADPH—See Nicotinamide adenine dinucleotide phosphate

NAD" — see Nicotinamide adenine dinucleotide NADP" — see Nicotinamide adenine dinucleotide phosphate NADPH... 

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. 

This reaction fixes carbon but there is no net change in oxidation number. The CO2 is reduced to carboxyl but one of the carbon atoms in the RuBP is oxidized to yield the second carboxyl group. In subsequent steps, each mole of PGA reacts with a mole of NADPH in order to produce two moles of 3-phosphoglyceraldehyde, a product in which average oxidation number of carbon is 0. NADPH is the reduced form of nicotinamide adenine dinucleotide phosphate (see any biochemistry text for structures and further details). In biosynthetic processes, it functions as a hydride donor or reductant. A typical reaction is shown below. Note that NADPH + H is equivalent to NADP + H2. 

The electron donor in most reductive biosyntheses is NADPH, the reduced form of nicotinamide adenine dinucleotide phosphate (NADP see Figure 14.13). NADPH differs from NADH in that the 2 -hydroxyl group of its adenosine moiety is esterified with phosphate. NADPH carries electrons in the same way as NADH. However, NADPH is used almost exclusively for reductive biosyntheses, whereas NADH is used primarily for the generation of ATP. The extra phosphoryl group on NADPH is a tag that enables enzymes to distinguish between high-potential electrons to be used in anabolism and those to be used in catabolism. 

NAD, NADH, NADP, NADPH. Abbreviations for nicotinamide adenine dinucleotide [phosphate] in the oxidized and reduced forms, see nicotinamide coenzymes. 

The second, so-called indicator reaction, provides the specificity of the method, since hexokinase also converts other hexoses, such as D-fructose and D-mannose, into their phosphorylated compounds. The formation of the coenzyme NADPH (the reduced form of nicotinamide adenine dinucleotide phosphate) can be measured photometrically, preferably at the absorption band maximum at 340 nm (see Figure 2). The hexokinase method has been internationally recommended as a reference method. 

NADP acronym of Nicotinamide adenine dinucleotide phosphate (see). NADP represents the oxidized form, NADPH the reduced form. 

Nicotinamide functions in the animal body as the active group of two important coenzymes nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP).These coenzymes are involved in the mechanism of hydrogen transfer in living cells (see Chapter 9) NAD is involved in the oxidative phosphorylation system, the tricyclic acid (TCA) cycle and the metabolism of many molecules, including pyruvate, acetate, (3-hydroxy-butyrate, glycerol, fatty acids and glutamate NADPH is the hydrogen acceptor in the pentose phosphate pathway. 

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